Reaction Process: INOH:MI0036050

Adenosine

C10H13N5O4 (267.09674980000005)

Adenosine is a ribonucleoside composed of a molecule of adenine attached to a ribofuranose moiety via a beta-N(9)-glycosidic bond. It has a role as an anti-arrhythmia drug, a vasodilator agent, an analgesic, a human metabolite and a fundamental metabolite. It is a purines D-ribonucleoside and a member of adenosines. It is functionally related to an adenine. The structure of adenosine was first described in 1931, though the vasodilating effects were not described in literature until the 1940s. Adenosine is indicated as an adjunct to thallium-201 in myocardial perfusion scintigraphy, though it is rarely used in this indication, having largely been replaced by [dipyridamole] and [regadenson]. Adenosine is also indicated in the treatment of supraventricular tachycardia. Adenosine was granted FDA approval on 30 October 1989. Adenosine is a metabolite found in or produced by Escherichia coli (strain K12, MG1655). Adenosine is an Adenosine Receptor Agonist. The mechanism of action of adenosine is as an Adenosine Receptor Agonist. Adenosine is a natural product found in Smilax bracteata, Mikania laevigata, and other organisms with data available. Adenosine is a ribonucleoside comprised of adenine bound to ribose, with vasodilatory, antiarrhythmic and analgesic activities. Phosphorylated forms of adenosine play roles in cellular energy transfer, signal transduction and the synthesis of RNA. Adenosine is a nucleoside that is composed of adenine and d-ribose. Adenosine or adenosine derivatives play many important biological roles in addition to being components of DNA and RNA. For instance, adenosine plays an important role in energy transfer - as adenosine triphosphate (ATP) and adenosine diphosphate (ADP). It also plays a role in signal transduction as cyclic adenosine monophosphate, cAMP. Adenosine itself is both a neurotransmitter and potent vasodilator. When administered intravenously, adenosine causes transient heart block in the AV node. Because of the effects of adenosine on AV node-dependent supraventricular tachycardia, adenosine is considered a class V antiarrhythmic agent. Adenosine is a metabolite found in or produced by Saccharomyces cerevisiae. A nucleoside that is composed of adenine and d-ribose. Adenosine or adenosine derivatives play many important biological roles in addition to being components of DNA and RNA. Adenosine itself is a neurotransmitter. See also: Adenosine; Niacinamide (component of); Adenosine; Glycerin (component of); Adenosine; ginsenosides (component of) ... View More ... Adenosine is a nucleoside that is composed of adenine and D-ribose. Adenosine or adenosine derivatives play many important biological roles in addition to being components of DNA and RNA. For instance, adenosine plays an important role in energy transfer as adenosine triphosphate (ATP) and adenosine diphosphate (ADP). It also plays a role in signal transduction as cyclic adenosine monophosphate (cAMP). Adenosine itself is both a neurotransmitter and potent vasodilator. When administered intravenously adenosine causes transient heart block in the AV node. Due to the effects of adenosine on AV node-dependent supraventricular tachycardia, adenosine is considered a class V antiarrhythmic agent. Overdoses of adenosine intake (as a drug) can lead to several side effects including chest pain, feeling faint, shortness of breath, and tingling of the senses. Serious side effects include a worsening dysrhythmia and low blood pressure. When present in sufficiently high levels, adenosine can act as an immunotoxin and a metabotoxin. An immunotoxin disrupts, limits the function, or destroys immune cells. A metabotoxin is an endogenous metabolite that causes adverse health effects at chronically high levels. Chronically high levels of adenosine are associated with adenosine deaminase deficiency. Adenosine is a precursor to deoxyadenosine, which is a precursor to dATP. A buildup of dATP in cells inhibits ribonucleotide reductase and prevents DNA synthesis, so cells are unable to divide. Since developing T cells and B cells are some of the most mitotically active cells, they are unable to divide and propagate to respond to immune challenges. High levels of deoxyadenosine also lead to an increase in S-adenosylhomocysteine, which is toxic to immature lymphocytes. Adenosine is a nucleoside composed of a molecule of adenine attached to a ribose sugar molecule (ribofuranose) moiety via a beta-N9-glycosidic bond. [Wikipedia]. Adenosine is found in many foods, some of which are borage, japanese persimmon, nuts, and barley. COVID info from PDB, Protein Data Bank, COVID-19 Disease Map, clinicaltrial, clinicaltrials, clinical trial, clinical trials A ribonucleoside composed of a molecule of adenine attached to a ribofuranose moiety via a beta-N(9)-glycosidic bond. Adenosine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=58-61-7 (retrieved 2024-06-29) (CAS RN: 58-61-7). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). Adenosine (Adenine riboside), a ubiquitous endogenous autacoid, acts through the enrollment of four G protein-coupled receptors: A1, A2A, A2B, and A3. Adenosine affects almost all aspects of cellular physiology, including neuronal activity, vascular function, platelet aggregation, and blood cell regulation[1][2]. Adenosine (Adenine riboside), a ubiquitous endogenous autacoid, acts through the enrollment of four G protein-coupled receptors: A1, A2A, A2B, and A3. Adenosine affects almost all aspects of cellular physiology, including neuronal activity, vascular function, platelet aggregation, and blood cell regulation[1][2]. Adenosine (Adenine riboside), a ubiquitous endogenous autacoid, acts through the enrollment of four G protein-coupled receptors: A1, A2A, A2B, and A3. Adenosine affects almost all aspects of cellular physiology, including neuronal activity, vascular function, platelet aggregation, and blood cell regulation[1][2].

Trimethylglycine

C5H11NO2 (117.0789746)

Glycine betaine is the amino acid betaine derived from glycine. It has a role as a fundamental metabolite. It is an amino-acid betaine and a glycine derivative. It is a conjugate base of a N,N,N-trimethylglycinium. Betaine is a methyl group donor that functions in the normal metabolic cycle of methionine. It is a naturally occurring choline derivative commonly ingested through diet, with a role in regulating cellular hydration and maintaining cell function. Homocystinuria is an inherited disorder that leads to the accumulation of homocysteine in plasma and urine. Currently, no treatments are available to correct the genetic causes of homocystinuria. However, in order to normalize homocysteine levels, patients can be treated with vitamin B6 ([pyridoxine]), vitamin B12 ([cobalamin]), [folate] and specific diets. Betaine reduces plasma homocysteine levels in patients with homocystinuria. Although it is present in many food products, the levels found there are insufficient to treat this condition. The FDA and EMA have approved the product Cystadane (betaine anhydrous, oral solution) for the treatment of homocystinuria, and the EMA has approved the use of Amversio (betaine anhydrous, oral powder). Betaine is a metabolite found in or produced by Escherichia coli (strain K12, MG1655). Betaine is a Methylating Agent. The mechanism of action of betaine is as a Methylating Activity. Betaine is a modified amino acid consisting of glycine with three methyl groups that serves as a methyl donor in several metabolic pathways and is used to treat the rare genetic causes of homocystinuria. Betaine has had only limited clinical use, but has not been linked to instances of serum enzyme elevations during therapy or to clinically apparent liver injury. Betaine is a natural product found in Hypoestes phyllostachya, Barleria lupulina, and other organisms with data available. Betaine is a metabolite found in or produced by Saccharomyces cerevisiae. A naturally occurring compound that has been of interest for its role in osmoregulation. As a drug, betaine hydrochloride has been used as a source of hydrochloric acid in the treatment of hypochlorhydria. Betaine has also been used in the treatment of liver disorders, for hyperkalemia, for homocystinuria, and for gastrointestinal disturbances. (From Martindale, The Extra Pharmacopoeia, 30th ed, p1341) See also: Arnica montana Flower (part of); Betaine; panthenol (component of); Betaine; scutellaria baicalensis root (component of) ... View More ... A - Alimentary tract and metabolism > A16 - Other alimentary tract and metabolism products > A16A - Other alimentary tract and metabolism products > A16AA - Amino acids and derivatives D057847 - Lipid Regulating Agents > D000960 - Hypolipidemic Agents > D008082 - Lipotropic Agents Acquisition and generation of the data is financially supported in part by CREST/JST. D009676 - Noxae > D000963 - Antimetabolites CONFIDENCE standard compound; ML_ID 42 D005765 - Gastrointestinal Agents KEIO_ID B047

Taurine

C2H7NO3S (125.0146632)

Essential nutrient obtained from diet and by in vivo synthysis from methionine and cysteine. Present in meats, fish, legumes, human milk, molluscs and other foods. Dietary supplement, e.g. in Red Bull drink. Taurine is a sulfur amino acid like methionine, cystine, cysteine and homocysteine. It is a lesser-known amino acid because it is not incorporated into the structural building blocks of protein. Yet taurine is an essential amino acid in pre-term and newborn infants of humans and many other species. Adults can synthesize their own taurine, yet are probably dependent in part on dietary taurine. Taurine is abundant in the brain, heart, breast, gallbladder and kidney and has important roles in health and disease in these organs. Taurine has many diverse biological functions serving as a neurotransmitter in the brain, a stabilizer of cell membranes and a facilitator in the transport of ions such as sodium, potassium, calcium and magnesium. Taurine is highly concentrated in animal and fish protein, which are good sources of dietary taurine. It can be synthesized by the body from cysteine when vitamin B6 is present. Deficiency of taurine occurs in premature infants and neonates fed formula milk, and in various disease states. Inborn errors of taurine metabolism have been described. OMIM 168605, an unusual neuropsychiatric disorder inherited in an autosomal dominant fashion through 3 generations of a family. Symptoms began late in the fifth decade in 6 affected persons and death occurred after 4 to 6 years. The earliest and most prominent symptom was mental depression not responsive to antidepressant drugs or electroconvulsive therapy. Sleep disturbances, exhaustion and marked weight loss were features. Parkinsonism developed later, and respiratory failure occurred terminally. OMIM 145350 describes congestive cardiomyopathy and markedly elevated urinary taurine levels (about 5 times normal). Other family members had late or holosystolic mitral valve prolapse and elevated urinary taurine values (about 2.5 times normal). In 2 with mitral valve prolapse, congestive cardiomyopathy eventually developed while the amounts of urinary taurine doubled. Taurine, after GABA, is the second most important inhibitory neurotransmitter in the brain. Its inhibitory effect is one source of taurines anticonvulsant and antianxiety properties. It also lowers glutamic acid in the brain, and preliminary clinical trials suggest taurine may be useful in some forms of epilepsy. Taurine in the brain is usually associated with zinc or manganese. The amino acids alanine and glutamic acid, as well as pantothenic acid, inhibit taurine metabolism while vitamins A and B6, zinc and manganese help build taurine. Cysteine and B6 are the nutrients most directly involved in taurine synthesis. Taurine levels have been found to decrease significantly in many depressed patients. One reason that the findings are not entirely clear is because taurine is often elevated in the blood of epileptics who need it. It is often difficult to distinguish compensatory changes in human biochemistry from true metabolic or deficiency disease. Low levels of taurine are found in retinitis pigmentosa. Taurine deficiency in experimental animals produces degeneration of light-sensitive cells. Therapeutic applications of taurine to eye disease are likely to be forthcoming. Taurine has many important metabolic roles. Supplements can stimulate prolactin and insulin release. The parathyroid gland makes a peptide hormone called glutataurine (glutamic acid-taurine), which further demonstrates taurines role in endocrinology. Taurine increases bilirubin and cholesterol excretion in bile, critical to normal gallbladder function. It seems to inhibit the effect of morphine and potentiates the effects of opiate antagonists. Low plasma taurine levels have been found in a variety of conditions, i.e., depression, hypertension, hypothyroidism, gout, institutionalized patients, infertility, obesity, kidney fa... Taurine is a sulfur amino acid like methionine, cystine, cysteine, and homocysteine. It is a lesser-known amino acid because it is not incorporated into the structural building blocks of protein. Yet taurine is an essential amino acid in pre-term and newborn infants of humans and many other species. Adults can synthesize their own taurine, yet are probably dependent, in part, on dietary taurine. Taurine is abundant in the brain, heart, breast, gallbladder, and kidney and has important roles in health and disease in these organs. Taurine has many diverse biological functions including serving as a neurotransmitter in the brain, a stabilizer of cell membranes, and a facilitator in the transport of ions such as sodium, potassium, calcium, and magnesium. Taurine is highly concentrated in animal and fish protein, which are good sources of dietary taurine. It can be synthesized by the body from cysteine when vitamin B6 is present. Deficiency of taurine occurs in premature infants, neonates fed formula milk, and various disease states. Several inborn errors of taurine metabolism have been described. Perry syndrome is an unusual neuropsychiatric disorder inherited in an autosomal dominant fashion through three generations of a family. Symptoms began late in the fifth decade in 6 affected persons and death occurred after 4 to 6 years. The earliest and most prominent symptom was mental depression that was not responsive to antidepressant drugs or electroconvulsive therapy. Sleep disturbances, exhaustion, and marked weight loss were features. Parkinsonism developed later, and respiratory failure occurred terminally (OMIM: 168605). Hypertaurinuric cardiomyopathy describes congestive cardiomyopathy and markedly elevated urinary taurine levels (about 5 times normal). Other family members had late or holosystolic mitral valve prolapse and elevated urinary taurine values (about 2.5 times normal). In two with mitral valve prolapse, congestive cardiomyopathy eventually developed while the amounts of urinary taurine doubled (OMIM: 145350). Taurine, after GABA, is the second most important inhibitory neurotransmitter in the brain. Its inhibitory effect is one source of taurines anticonvulsant and antianxiety properties. It also lowers glutamic acid in the brain, and preliminary clinical trials suggest taurine may be useful in some forms of epilepsy. Taurine in the brain is usually associated with zinc or manganese. The amino acids alanine and glutamic acid, as well as pantothenic acid, inhibit taurine metabolism while vitamins A and B6, zinc, and manganese help build taurine. Cysteine and B6 are the nutrients most directly involved in taurine synthesis. Taurine levels have been found to decrease significantly in many depressed patients. One reason that the findings are not entirely clear is that taurine is often elevated in the blood of epileptics who need it. It is often difficult to distinguish compensatory changes in human biochemistry from true metabolic or deficiency disease. Low levels of taurine are found in retinitis pigmentosa. Taurine deficiency in experimental animals produces degeneration of light-sensitive cells. Therapeutic applications of taurine to eye disease are likely to be forthcoming. Taurine has many important metabolic roles. Supplements can stimulate prolactin and insulin release. The parathyroid gland makes a peptide hormone called glutataurine (glutamic acid-taurine), which further demonstrates taurines role in endocrinology. Taurine increases bilirubin and cholesterol excretion in bile, critical to normal gallbladder function. It seems to inhibit the effect of morphine and potentiates the effects of opiate antagonists. Low plasma taurine levels have been found in a variety of conditions, i.e. depression, hypertension, hypothyroidism, gout, institutionalized patients, infertility, obesity, kidney failure, and others (http://www.dcnutrition.com/AminoAcids/). Moreover, taurine is found to be associated with maple syrup uri... Large white crystals or white powder. Taurine is an amino sulfonic acid that is the 2-amino derivative of ethanesulfonic acid. It is a naturally occurring amino acid derived from methionine and cysteine metabolism. An abundant component of fish- and meat-based foods, it has been used as an oral supplement in the treatment of disorders such as cystic fibrosis and hypertension. It has a role as a human metabolite, an antioxidant, a mouse metabolite, a Saccharomyces cerevisiae metabolite, an Escherichia coli metabolite, a glycine receptor agonist, a nutrient and a radical scavenger. It is a conjugate acid of a 2-aminoethanesulfonate. It is a tautomer of a taurine zwitterion. Taurine, whose chemical name is 2-aminoethanesulfonic acid, is one of the most abundant amino acids in several organs. It plays important role in essential biological processes. This conditional amino acid can be either be manufactured by the body or obtained in the diet mainly by the consumption of fish and meat. The supplements containing taurine were FDA approved by 1984 and they are hypertonic injections composed by cristalline amino acids. Taurine is a metabolite found in or produced by Escherichia coli (strain K12, MG1655). A conditionally essential nutrient, important during mammalian development. It is present in milk but is isolated mostly from ox bile and strongly conjugates bile acids. See also: ... View More ... An amino sulfonic acid that is the 2-amino derivative of ethanesulfonic acid. It is a naturally occurring amino acid derived from methionine and cysteine metabolism. An abundant component of fish- and meat-based foods, it has been used as an oral supplement in the treatment of disorders such as cystic fibrosis and hypertension. [Spectral] Taurine (exact mass = 125.01466) and L-Threonine (exact mass = 119.05824) and 4-Hydroxy-L-proline (exact mass = 131.05824) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. [Spectral] Taurine (exact mass = 125.01466) and L-Glutamate (exact mass = 147.05316) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. Taurine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=107-35-7 (retrieved 2024-06-29) (CAS RN: 107-35-7). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). Taurine, a sulphur-containing amino acid and an organic osmolyte involved in cell volume regulation, provides a substrate for the formation of bile salts, and plays a role in the modulation of intracellular free calcium concentration. Taurine has the ability to activate autophagy in adipocytes[1][2][3]. Taurine, a sulphur-containing amino acid and an organic osmolyte involved in cell volume regulation, provides a substrate for the formation of bile salts, and plays a role in the modulation of intracellular free calcium concentration. Taurine has the ability to activate autophagy in adipocytes[1][2][3].

L-Glutamic acid

C5H9NO4 (147.0531554)

Glutamic acid (Glu), also known as L-glutamic acid or as glutamate, the name of its anion, is an alpha-amino acid. These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon). Amino acids are organic compounds that contain amino (‚ÄìNH2) and carboxyl (‚ÄìCOOH) functional groups, along with a side chain (R group) specific to each amino acid. L-glutamic acid is one of 20 proteinogenic amino acids, i.e., the amino acids used in the biosynthesis of proteins. Glutamic acid is found in all organisms ranging from bacteria to plants to animals. It is classified as an acidic, charged (at physiological pH), aliphatic amino acid. In humans it is a non-essential amino acid and can be synthesized via alanine or aspartic acid via alpha-ketoglutarate and the action of various transaminases. Glutamate also plays an important role in the bodys disposal of excess or waste nitrogen. Glutamate undergoes deamination, an oxidative reaction catalysed by glutamate dehydrogenase leading to alpha-ketoglutarate. In many respects glutamate is a key molecule in cellular metabolism. Glutamate is the most abundant fast excitatory neurotransmitter in the mammalian nervous system. At chemical synapses, glutamate is stored in vesicles. Nerve impulses trigger release of glutamate from the pre-synaptic cell. In the opposing post-synaptic cell, glutamate receptors, such as the NMDA receptor, bind glutamate and are activated. Because of its role in synaptic plasticity, it is believed that glutamic acid is involved in cognitive functions like learning and memory in the brain. Glutamate transporters are found in neuronal and glial membranes. They rapidly remove glutamate from the extracellular space. In brain injury or disease, they can work in reverse and excess glutamate can accumulate outside cells. This process causes calcium ions to enter cells via NMDA receptor channels, leading to neuronal damage and eventual cell death, and is called excitotoxicity. The mechanisms of cell death include: Damage to mitochondria from excessively high intracellular Ca2+. Glu/Ca2+-mediated promotion of transcription factors for pro-apoptotic genes, or downregulation of transcription factors for anti-apoptotic genes. Excitotoxicity due to glutamate occurs as part of the ischemic cascade and is associated with stroke and diseases like amyotrophic lateral sclerosis, lathyrism, and Alzheimers disease. Glutamic acid has been implicated in epileptic seizures. Microinjection of glutamic acid into neurons produces spontaneous depolarization around one second apart, and this firing pattern is similar to what is known as paroxysmal depolarizing shift in epileptic attacks. This change in the resting membrane potential at seizure foci could cause spontaneous opening of voltage activated calcium channels, leading to glutamic acid release and further depolarization (http://en.wikipedia.org/wiki/Glutamic_acid). Glutamate was discovered in 1866 when it was extracted from wheat gluten (from where it got its name. Glutamate has an important role as a food additive and food flavoring agent. In 1908, Japanese researcher Kikunae Ikeda identified brown crystals left behind after the evaporation of a large amount of kombu broth (a Japanese soup) as glutamic acid. These crystals, when tasted, reproduced a salty, savory flavor detected in many foods, most especially in seaweed. Professor Ikeda termed this flavor umami. He then patented a method of mass-producing a crystalline salt of glutamic acid, monosodium glutamate. L-glutamic acid is an optically active form of glutamic acid having L-configuration. It has a role as a nutraceutical, a micronutrient, an Escherichia coli metabolite, a mouse metabolite, a ferroptosis inducer and a neurotransmitter. It is a glutamine family amino acid, a proteinogenic amino acid, a glutamic acid and a L-alpha-amino acid. It is a conjugate acid of a L-glutamate(1-). It is an enantiomer of a D-glutamic acid. A peptide that is a homopolymer of glutamic acid. L-Glutamic acid is a metabolite found in or produced by Escherichia coli (strain K12, MG1655). Glutamic acid (Glu), also referred to as glutamate (the anion), is one of the 20 proteinogenic amino acids. It is not among the essential amino acids. Glutamate is a key molecule in cellular metabolism. In humans, dietary proteins are broken down by digestion into amino acids, which serves as metabolic fuel or other functional roles in the body. Glutamate is the most abundant fast excitatory neurotransmitter in the mammalian nervous system. At chemical synapses, glutamate is stored in vesicles. Nerve impulses trigger release of glutamate from the pre-synaptic cell. In the opposing post-synaptic cell, glutamate receptors, such as the NMDA receptor, bind glutamate and are activated. Because of its role in synaptic plasticity, it is believed that glutamic acid is involved in cognitive functions like learning and memory in the brain. Glutamate transporters are found in neuronal and glial membranes. They rapidly remove glutamate from the extracellular space. In brain injury or disease, they can work in reverse and excess glutamate can accumulate outside cells. This process causes calcium ions to enter cells via NMDA receptor channels, leading to neuronal damage and eventual cell death, and is called excitotoxicity. The mechanisms of cell death include: * Damage to mitochondria from excessively high intracellular Ca2+. * Glu/Ca2+-mediated promotion of transcription factors for pro-apoptotic genes, or downregulation of transcription factors for anti-apoptotic genes. Excitotoxicity due to glutamate occurs as part of the ischemic cascade and is associated with stroke and diseases like amyotrophic lateral sclerosis, lathyrism, and Alzheimers disease. glutamic acid has been implicated in epileptic seizures. Microinjection of glutamic acid into neurons produces spontaneous depolarization around one second apart, and this firing pattern is similar to what is known as paroxysmal depolarizing shift in epileptic attacks. This change in the resting membrane potential at seizure foci could cause spontaneous opening of voltage activated calcium channels, leading to glutamic acid release and further depolarization. A non-essential amino acid naturally occurring in the L-form. Glutamic acid is the most common excitatory neurotransmitter in the CENTRAL NERVOUS SYSTEM. See also: Monosodium Glutamate (active moiety of); Glatiramer Acetate (monomer of); Glatiramer (monomer of) ... View More ... obtained from acid hydrolysis of proteins. Since 1965 the industrial source of glutamic acid for MSG production has been bacterial fermentation of carbohydrate sources such as molasses and corn starch hydrolysate in the presence of a nitrogen source such as ammonium salts or urea. Annual production approx. 350000t worldwide in 1988. Seasoning additive in food manuf. (as Na, K and NH4 salts). Dietary supplement, nutrient Glutamic acid (symbol Glu or E;[4] the anionic form is known as glutamate) is an α-amino acid that is used by almost all living beings in the biosynthesis of proteins. It is a non-essential nutrient for humans, meaning that the human body can synthesize enough for its use. It is also the most abundant excitatory neurotransmitter in the vertebrate nervous system. It serves as the precursor for the synthesis of the inhibitory gamma-aminobutyric acid (GABA) in GABAergic neurons. Its molecular formula is C 5H 9NO 4. Glutamic acid exists in two optically isomeric forms; the dextrorotatory l-form is usually obtained by hydrolysis of gluten or from the waste waters of beet-sugar manufacture or by fermentation.[5][full citation needed] Its molecular structure could be idealized as HOOC−CH(NH 2)−(CH 2)2−COOH, with two carboxyl groups −COOH and one amino group −NH 2. However, in the solid state and mildly acidic water solutions, the molecule assumes an electrically neutral zwitterion structure −OOC−CH(NH+ 3)−(CH 2)2−COOH. It is encoded by the codons GAA or GAG. The acid can lose one proton from its second carboxyl group to form the conjugate base, the singly-negative anion glutamate −OOC−CH(NH+ 3)−(CH 2)2−COO−. This form of the compound is prevalent in neutral solutions. The glutamate neurotransmitter plays the principal role in neural activation.[6] This anion creates the savory umami flavor of foods and is found in glutamate flavorings such as MSG. In Europe, it is classified as food additive E620. In highly alkaline solutions the doubly negative anion −OOC−CH(NH 2)−(CH 2)2−COO− prevails. The radical corresponding to glutamate is called glutamyl. The one-letter symbol E for glutamate was assigned in alphabetical sequence to D for aspartate, being larger by one methylene –CH2– group.[7] DL-Glutamic acid is the conjugate acid of Glutamic acid, which acts as a fundamental metabolite. Comparing with the second phase of polymorphs α and β L-Glutamic acid, DL-Glutamic acid presents better stability[1]. DL-Glutamic acid is the conjugate acid of Glutamic acid, which acts as a fundamental metabolite. Comparing with the second phase of polymorphs α and β L-Glutamic acid, DL-Glutamic acid presents better stability[1]. L-Glutamic acid acts as an excitatory transmitter and an agonist at all subtypes of glutamate receptors (metabotropic, kainate, NMDA, and AMPA). L-Glutamic acid shows a direct activating effect on the release of DA from dopaminergic terminals. L-Glutamic acid is an excitatory amino acid neurotransmitter that acts as an agonist for all subtypes of glutamate receptors (metabolic rhodophylline, NMDA, and AMPA). L-Glutamic acid has an agonist effect on the release of DA from dopaminergic nerve endings. L-Glutamic acid can be used in the study of neurological diseases[1][2][3][4][5]. L-Glutamic acid acts as an excitatory transmitter and an agonist at all subtypes of glutamate receptors (metabotropic, kainate, NMDA, and AMPA). L-Glutamic acid shows a direct activating effect on the release of DA from dopaminergic terminals.

Adenosine triphosphate

C10H16N5O13P3 (506.9957476)

Adenosine triphosphate, also known as atp or atriphos, is a member of the class of compounds known as purine ribonucleoside triphosphates. Purine ribonucleoside triphosphates are purine ribobucleotides with a triphosphate group linked to the ribose moiety. Adenosine triphosphate is slightly soluble (in water) and an extremely strong acidic compound (based on its pKa). Adenosine triphosphate can be found in a number of food items such as lichee, alpine sweetvetch, pecan nut, and black mulberry, which makes adenosine triphosphate a potential biomarker for the consumption of these food products. Adenosine triphosphate can be found primarily in blood, cellular cytoplasm, cerebrospinal fluid (CSF), and saliva, as well as throughout most human tissues. Adenosine triphosphate exists in all living species, ranging from bacteria to humans. In humans, adenosine triphosphate is involved in several metabolic pathways, some of which include phosphatidylethanolamine biosynthesis PE(16:0/18:4(6Z,9Z,12Z,15Z)), carteolol action pathway, phosphatidylethanolamine biosynthesis PE(20:3(5Z,8Z,11Z)/15:0), and carfentanil action pathway. Adenosine triphosphate is also involved in several metabolic disorders, some of which include lysosomal acid lipase deficiency (wolman disease), phosphoenolpyruvate carboxykinase deficiency 1 (PEPCK1), propionic acidemia, and the oncogenic action of d-2-hydroxyglutarate in hydroxygluaricaciduria. Moreover, adenosine triphosphate is found to be associated with rachialgia, neuroinfection, stroke, and subarachnoid hemorrhage. Adenosine triphosphate is a non-carcinogenic (not listed by IARC) potentially toxic compound. Adenosine triphosphate is a drug which is used for nutritional supplementation, also for treating dietary shortage or imbalanc. Adenosine triphosphate (ATP) is a complex organic chemical that participates in many processes. Found in all forms of life, ATP is often referred to as the "molecular unit of currency" of intracellular energy transfer. When consumed in metabolic processes, it converts to either the di- or monophosphates, respectively ADP and AMP. Other processes regenerate ATP such that the human body recycles its own body weight equivalent in ATP each day. It is also a precursor to DNA and RNA . ATP is able to store and transport chemical energy within cells. ATP also plays an important role in the synthesis of nucleic acids. ATP can be produced by various cellular processes, most typically in mitochondria by oxidative phosphorylation under the catalytic influence of ATP synthase. The total quantity of ATP in the human body is about 0.1 mole. The energy used by human cells requires the hydrolysis of 200 to 300 moles of ATP daily. This means that each ATP molecule is recycled 2000 to 3000 times during a single day. ATP cannot be stored, hence its consumption must closely follow its synthesis (DrugBank). Metabolism of organophosphates occurs principally by oxidation, by hydrolysis via esterases and by reaction with glutathione. Demethylation and glucuronidation may also occur. Oxidation of organophosphorus pesticides may result in moderately toxic products. In general, phosphorothioates are not directly toxic but require oxidative metabolism to the proximal toxin. The glutathione transferase reactions produce products that are, in most cases, of low toxicity. Paraoxonase (PON1) is a key enzyme in the metabolism of organophosphates. PON1 can inactivate some organophosphates through hydrolysis. PON1 hydrolyzes the active metabolites in several organophosphates insecticides as well as, nerve agents such as soman, sarin, and VX. The presence of PON1 polymorphisms causes there to be different enzyme levels and catalytic efficiency of this esterase, which in turn suggests that different individuals may be more susceptible to the toxic effect of organophosphate exposure (T3DB). ATP is an adenosine 5-phosphate in which the 5-phosphate is a triphosphate group. It is involved in the transportation of chemical energy during metabolic pathways. It has a role as a nutraceutical, a micronutrient, a fundamental metabolite and a cofactor. It is an adenosine 5-phosphate and a purine ribonucleoside 5-triphosphate. It is a conjugate acid of an ATP(3-). An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter. Adenosine triphosphate is a metabolite found in or produced by Escherichia coli (strain K12, MG1655). Adenosine-5-triphosphate is a natural product found in Chlamydomonas reinhardtii, Arabidopsis thaliana, and other organisms with data available. Adenosine Triphosphate is an adenine nucleotide comprised of three phosphate groups esterified to the sugar moiety, found in all living cells. Adenosine triphosphate is involved in energy production for metabolic processes and RNA synthesis. In addition, this substance acts as a neurotransmitter. In cancer studies, adenosine triphosphate is synthesized to examine its use to decrease weight loss and improve muscle strength. Adenosine triphosphate (ATP) is a nucleotide consisting of a purine base (adenine) attached to the first carbon atom of ribose (a pentose sugar). Three phosphate groups are esterified at the fifth carbon atom of the ribose. ATP is incorporated into nucleic acids by polymerases in the processes of DNA replication and transcription. ATP contributes to cellular energy charge and participates in overall energy balance, maintaining cellular homeostasis. ATP can act as an extracellular signaling molecule via interactions with specific purinergic receptors to mediate a wide variety of processes as diverse as neurotransmission, inflammation, apoptosis, and bone remodelling. Extracellular ATP and its metabolite adenosine have also been shown to exert a variety of effects on nearly every cell type in human skin, and ATP seems to play a direct role in triggering skin inflammatory, regenerative, and fibrotic responses to mechanical injury, an indirect role in melanocyte proliferation and apoptosis, and a complex role in Langerhans cell-directed adaptive immunity. During exercise, intracellular homeostasis depends on the matching of adenosine triphosphate (ATP) supply and ATP demand. Metabolites play a useful role in communicating the extent of ATP demand to the metabolic supply pathways. Effects as different as proliferation or differentiation, chemotaxis, release of cytokines or lysosomal constituents, and generation of reactive oxygen or nitrogen species are elicited upon stimulation of blood cells with extracellular ATP. The increased concentration of adenosine triphosphate (ATP) in erythrocytes from patients with chronic renal failure (CRF) has been observed in many studies but the mechanism leading to these abnormalities still is controversial. (A3367, A3368, A3369, A3370, A3371). Adenosine triphosphate is a metabolite found in or produced by Saccharomyces cerevisiae. An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter. Adenosine triphosphate (ATP) is a nucleotide consisting of a purine base (adenine) attached to the first carbon atom of ribose (a pentose sugar). Three phosphate groups are esterified at the fifth carbon atom of the ribose. ATP is incorporated into nucleic acids by polymerases in the processes of DNA replication and transcription. ATP contributes to cellular energy charge and participates in overall energy balance, maintaining cellular homeostasis. ATP can act as an extracellular signaling molecule via interactions with specific purinergic receptors to mediate a wide variety of processes as diverse as neurotransmission, inflammation, apoptosis, and bone remodelling. Extracellular ATP and its metabolite adenosine have also been shown to exert a variety of effects on nearly every cell type in human skin, and ATP seems to play a direct role in triggering skin inflammatory, regenerative, and fibrotic responses to mechanical injury, an indirect role in melanocyte proliferation and apoptosis, and a complex role in Langerhans cell-directed adaptive immunity. During exercise, intracellular homeostasis depends on the matching of adenosine triphosphate (ATP) supply and ATP demand. Metabolites play a useful role in communicating the extent of ATP demand to the metabolic supply pathways. Effects as different as proliferation or differentiation, chemotaxis, release of cytokines or lysosomal constituents, and generation of reactive oxygen or nitrogen species are elicited upon stimulation of blood cells with extracellular ATP. The increased concentration of adenosine triphosphate (ATP) in erythrocytes from patients with chronic renal failure (CRF) has been observed in many studies but the mechanism leading to these abnormalities still is controversial. (PMID: 15490415, 15129319, 14707763, 14696970, 11157473). 5′-ATP. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=56-65-5 (retrieved 2024-07-01) (CAS RN: 56-65-5). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0).

Adenosine monophosphate

C10H14N5O7P (347.0630824)

Adenosine monophosphate, also known as adenylic acid or amp, is a member of the class of compounds known as purine ribonucleoside monophosphates. Purine ribonucleoside monophosphates are nucleotides consisting of a purine base linked to a ribose to which one monophosphate group is attached. Adenosine monophosphate is slightly soluble (in water) and a moderately acidic compound (based on its pKa). Adenosine monophosphate can be found in a number of food items such as kiwi, taro, alaska wild rhubarb, and skunk currant, which makes adenosine monophosphate a potential biomarker for the consumption of these food products. Adenosine monophosphate can be found primarily in most biofluids, including blood, feces, cerebrospinal fluid (CSF), and urine, as well as throughout all human tissues. Adenosine monophosphate exists in all living species, ranging from bacteria to humans. In humans, adenosine monophosphate is involved in several metabolic pathways, some of which include josamycin action pathway, methacycline action pathway, nevirapine action pathway, and aspartate metabolism. Adenosine monophosphate is also involved in several metabolic disorders, some of which include hyperornithinemia-hyperammonemia-homocitrullinuria [hhh-syndrome], molybdenum cofactor deficiency, xanthinuria type I, and mitochondrial DNA depletion syndrome. Adenosine monophosphate is a drug which is used for nutritional supplementation, also for treating dietary shortage or imbalanc. Adenosine monophosphate, also known as 5-adenylic acid and abbreviated AMP, is a nucleotide that is found in RNA. It is an ester of phosphoric acid with the nucleoside adenosine. AMP consists of the phosphate group, the pentose sugar ribose, and the nucleobase adenine. AMP can be produced during ATP synthesis by the enzyme adenylate kinase. AMP has recently been approved as a Bitter Blocker additive to foodstuffs. When AMP is added to bitter foods or foods with a bitter aftertaste it makes them seem sweeter. This potentially makes lower calorie food products more palatable. [Spectral] AMP (exact mass = 347.06308) and Guanine (exact mass = 151.04941) and 3,4-Dihydroxy-L-phenylalanine (exact mass = 197.06881) and Glutathione disulfide (exact mass = 612.15196) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. [Spectral] AMP (exact mass = 347.06308) and Glutathione disulfide (exact mass = 612.15196) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. [Spectral] AMP (exact mass = 347.06308) and Adenine (exact mass = 135.0545) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. Adenosine monophosphate. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=67583-85-1 (retrieved 2024-07-01) (CAS RN: 61-19-8). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). Adenosine monophosphate is a key cellular metabolite regulating energy homeostasis and signal transduction. Adenosine monophosphate is a key cellular metabolite regulating energy homeostasis and signal transduction. Adenosine monophosphate is a key cellular metabolite regulating energy homeostasis and signal transduction.

5-Methyltetrahydrofolic acid

C20H25N7O6 (459.186623)

5 methyltetrahydrofolic acid (5-MTHF) is the most biologically active form of the B-vitamin known as folic acid, also known generically as folate. 5-MTHF functions, in concert with vitamin B12, as a methyl-group donor involved in the conversion of the amino acid homocysteine to methionine. Methyl (CH3) group donation is vital to many bodily processes, including serotonin, melatonin, and DNA synthesis. Therapeutically, 5-MTHF is instrumental in reducing homocysteine levels, preventing neural tube defects, and improving vascular endothelial function. Research on folate supplementation suggests it plays a key role in preventing cervical dysplasia and protecting against neoplasia in ulcerative colitis. Folic acid also shows promise as part of a nutritional protocol to treat vitiligo, and may reduce inflammation of the gingiva. Furthermore, certain neurological, cognitive, and psychiatric presentations may be secondary to folate deficiency. Such presentations include depression, peripheral neuropathy, myelopathy, restless legs syndrome, insomnia, dementia, forgetfulness, irritability, endogenous depression, organic psychosis, and schizophrenia-like syndromes. After ingestion, the process of conversion of folic acid to the metabolically active coenzyme forms is relatively complex. Synthesis of the active forms of folic acid requires several enzymes, adequate liver and intestinal function, and adequate supplies of riboflavin (B2), niacin (B3), pyridoxine (B6), zinc, vitamin C, and serine. After formation of the coenzyme forms of the vitamin in the liver, these metabolically active compounds are secreted into the small intestine with bile (the folate enterohepatic cycle), where they are reabsorbed and distributed to tissues throughout the body. Human pharmacokinetic studies indicate folic acid has high bioavailability, with large oral doses of folic acid substantially raising plasma levels in healthy subjects in a time and dose dependent manner. Red blood cells (RBCs) appear to be the storage depot for folic acid, as RBC levels remain elevated for periods in excess of 40 days following discontinuation of supplementation. Folic acid is poorly transported to the brain and rapidly cleared from the central nervous system. The primary methods of elimination of absorbed folic acid are fecal (through bile) and urinary. Despite the biochemical complexity of this process, evidence suggests oral supplementation with folic acid increases the bodys pool of 5-MTHF in healthy individuals. However, enzyme defects, mal-absorption, digestive system pathology, and liver disease can result in impaired ability to activate folic acid. In fact, some individuals have a severe congenital deficiency of the enzyme Methyl tetrahydrofolate reductase (5-MTHFR), which is needed to convert folic acid to 5-MTHF. Milder forms of this enzyme defect likely interact with dietary folate status to determine risk for some disease conditions. In individuals with a genetic defect of this enzyme (whether mild or severe), supplementation with 5- MTHF might be preferable to folic acid supplementation. (PMID: 17176169). 5 methyltetrahydrofolic acid (5-MTHF) is the most biologically active form of the B-vitamin folic acid, also known generically as folate. 5-MTHF functions, in concert with vitamin B12, as a methyl-group donor involved in the conversion of the amino acid homocysteine to methionine. Methyl (CH3) group donation is vital to many bodily processes, including serotonin, melatonin, and DNA synthesis. Therapeutically, 5-MTHF is instrumental in reducing homocysteine levels, preventing neural tube defects, and improving vascular endothelial function. Research on folate supplementation suggests it plays a key role in preventing cervical dysplasia and protecting against neoplasia in ulcerative colitis. Folic acid also shows promise as part of a nutritional protocol to treat vitiligo, and may reduce inflammation of the gingiva. Furthermore, certain neurological, cognitive, and psychiatric presentations may be secondary to folate deficiency. Such presentations include depression, peripheral neuropathy, myelopathy, restless legs syndrome, insomnia, dementia, forgetfulness, irritability, endogenous depression, organic psychosis, and schizophrenia-like syndromes. After ingestion, the process of conversion of folic acid to the metabolically active coenzyme forms is relatively complex. Synthesis of the active forms of folic acid requires several enzymes, adequate liver and intestinal function, and adequate supplies of riboflavin (B2), niacin (B3), pyridoxine (B6), zinc, vitamin C, and serine. After formation of the coenzyme forms of the vitamin in the liver, these metabolically active compounds are secreted into the small intestine with bile (the folate enterohepatic cycle), where they are reabsorbed and distributed to tissues throughout the body. Human pharmacokinetic studies indicate folic acid has high bioavailability, with large oral doses of folic acid substantially raising plasma levels in healthy subjects in a time and dose dependent manner. Red blood cells (RBCs) appear to be the storage depot for folic acid, as RBC levels remain elevated for periods in excess of 40 days following discontinuation of supplementation. Folic acid is poorly transported to the brain and rapidly cleared from the central nervous system. The primary methods of elimination of absorbed folic acid are fecal (through bile) and urinary. Despite the biochemical complexity of this process, evidence suggests oral supplementation with folic acid increases the bodys pool of 5-MTHF in healthy individuals. However, enzyme defects, mal-absorption, digestive system pathology, and liver disease can result in impaired ability to activate folic acid. In fact, some individuals have a severe congenital deficiency of the enzyme Methyl tetrahydrofolate reductase (5-MTHFR), which is needed to convert folic acid to 5-MTHF. Milder forms of this enzyme defect likely interact with dietary folate status to determine risk for some disease conditions. In individuals with a genetic defect of this enzyme (whether mild or severe), supplementation with 5- MTHF might be preferable to folic acid supplementation. (PMID: 17176169) [HMDB] 5-Methyltetrahydrofolic acid (5-Methyl THF) is a biologically active form of folic acid. 5-Methyltetrahydrofolic acid is a methylated derivate of tetrahydrofolate. 5-Methyltetrahydrofolic acid is the predominant natural dietary folate and the principal form of folate in plasma and cerebrospinal fluid[1]. Levomefolic acid (5-MTHF) is an orally active, brain-penetrant natural active form of folic acid and is one of the most widely used folic acid food supplements[1][2].

Oxoglutaric acid

C5H6O5 (146.0215226)

Oxoglutaric acid, also known as alpha-ketoglutarate, alpha-ketoglutaric acid, AKG, or 2-oxoglutaric acid, is classified as a gamma-keto acid or a gamma-keto acid derivative. gamma-Keto acids are organic compounds containing an aldehyde substituted with a keto group on the C4 carbon atom. alpha-Ketoglutarate is considered to be soluble (in water) and acidic. alpha-Ketoglutarate is a key molecule in the TCA cycle, playing a fundamental role in determining the overall rate of this important metabolic process (PMID: 26759695). In the TCA cycle, AKG is decarboxylated to succinyl-CoA and carbon dioxide by AKG dehydrogenase, which functions as a key control point of the TCA cycle. Additionally, AKG can be generated from isocitrate by oxidative decarboxylation catalyzed by the enzyme known as isocitrate dehydrogenase (IDH). In addition to these routes of production, AKG can be produced from glutamate by oxidative deamination via glutamate dehydrogenase, and as a product of pyridoxal phosphate-dependent transamination reactions (mediated by branched-chain amino acid transaminases) in which glutamate is a common amino donor. AKG is a nitrogen scavenger and a source of glutamate and glutamine that stimulates protein synthesis and inhibits protein degradation in muscles. In particular, AKG can decrease protein catabolism and increase protein synthesis to enhance bone tissue formation in skeletal muscles (PMID: 26759695). Interestingly, enteric feeding of AKG supplements can significantly increase circulating plasma levels of hormones such as insulin, growth hormone, and insulin-like growth factor-1 (PMID: 26759695). It has recently been shown that AKG can extend the lifespan of adult C. elegans by inhibiting ATP synthase and TOR (PMID: 24828042). In combination with molecular oxygen, alpha-ketoglutarate is required for the hydroxylation of proline to hydroxyproline in the production of type I collagen. A recent study has shown that alpha-ketoglutarate promotes TH1 differentiation along with the depletion of glutamine thereby favouring Treg (regulatory T-cell) differentiation (PMID: 26420908). alpha-Ketoglutarate has been found to be associated with fumarase deficiency, 2-ketoglutarate dehydrogenase complex deficiency, and D-2-hydroxyglutaric aciduria, which are all inborn errors of metabolism (PMID: 8338207). Oxoglutaric acid has been found to be a metabolite produced by Corynebacterium and yeast (PMID: 27872963) (YMDB). [Spectral] 2-Oxoglutarate (exact mass = 146.02152) and S-Adenosyl-L-homocysteine (exact mass = 384.12159) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. [Spectral] 2-Oxoglutarate (exact mass = 146.02152) and (S)-Malate (exact mass = 134.02152) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. Flavouring ingredient

Coenzyme A

C21H36N7O16P3S (767.1152046000001)

Coenzyme A (CoA, CoASH, or HSCoA) is a coenzyme notable for its role in the synthesis and oxidization of fatty acids and the oxidation of pyruvate in the citric acid cycle. It is adapted from beta-mercaptoethylamine, panthothenate, and adenosine triphosphate. It is also a parent compound for other transformation products, including but not limited to, phenylglyoxylyl-CoA, tetracosanoyl-CoA, and 6-hydroxyhex-3-enoyl-CoA. Coenzyme A is synthesized in a five-step process from pantothenate and cysteine. In the first step pantothenate (vitamin B5) is phosphorylated to 4-phosphopantothenate by the enzyme pantothenate kinase (PanK, CoaA, CoaX). In the second step, a cysteine is added to 4-phosphopantothenate by the enzyme phosphopantothenoylcysteine synthetase (PPC-DC, CoaB) to form 4-phospho-N-pantothenoylcysteine (PPC). In the third step, PPC is decarboxylated to 4-phosphopantetheine by phosphopantothenoylcysteine decarboxylase (CoaC). In the fourth step, 4-phosphopantetheine is adenylylated to form dephospho-CoA by the enzyme phosphopantetheine adenylyl transferase (CoaD). Finally, dephospho-CoA is phosphorylated using ATP to coenzyme A by the enzyme dephosphocoenzyme A kinase (CoaE). Since coenzyme A is, in chemical terms, a thiol, it can react with carboxylic acids to form thioesters, thus functioning as an acyl group carrier. CoA assists in transferring fatty acids from the cytoplasm to the mitochondria. A molecule of coenzyme A carrying an acetyl group is also referred to as acetyl-CoA. When it is not attached to an acyl group, it is usually referred to as CoASH or HSCoA. Coenzyme A is also the source of the phosphopantetheine group that is added as a prosthetic group to proteins such as acyl carrier proteins and formyltetrahydrofolate dehydrogenase. Acetyl-CoA is an important molecule itself. It is the precursor to HMG CoA which is a vital component in cholesterol and ketone synthesis. Furthermore, it contributes an acetyl group to choline to produce acetylcholine in a reaction catalysed by choline acetyltransferase. Its main task is conveying the carbon atoms within the acetyl group to the citric acid cycle to be oxidized for energy production (Wikipedia). Coenzyme A (CoA, CoASH, or HSCoA) is a coenzyme, notable for its role in the synthesis and oxidization of fatty acids, and the oxidation of pyruvate in the citric acid cycle. It is adapted from beta-mercaptoethylamine, panthothenate and adenosine triphosphate. Acetyl-CoA is an important molecule itself. It is the precursor to HMG CoA, which is a vital component in cholesterol and ketone synthesis. Furthermore, it contributes an acetyl group to choline to produce acetylcholine, in a reaction catalysed by choline acetyltransferase. Its main task is conveying the carbon atoms within the acetyl group to the citric acid cycle to be oxidized for energy production. -- Wikipedia [HMDB]. Coenzyme A is found in many foods, some of which are grape, cowpea, pili nut, and summer savory. COVID info from COVID-19 Disease Map, WikiPathways Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS Coenzyme A (CoASH) is a ubiquitous and essential cofactor, which is an acyl group carrier and carbonyl-activating group for the citric acid cycle and fatty acid metabolism. Coenzyme A plays a central role in the oxidation of pyruvate in the citric acid cycle and the metabolism of carboxylic acids, including short- and long-chain fatty acids[1]. Coenzyme A (CoASH) is a ubiquitous and essential cofactor, which is an acyl group carrier and carbonyl-activating group for the citric acid cycle and fatty acid metabolism. Coenzyme A plays a central role in the oxidation of pyruvate in the citric acid cycle and the metabolism of carboxylic acids, including short- and long-chain fatty acids[1]. Coenzyme A, a ubiquitous essential cofactor, is an acyl group carrier and carbonyl-activating group for the citric acid cycle and fatty acid metabolism. Coenzyme A plays a central role in the metabolism of carboxylic acids, including short- and long-chain fatty acids[1].

L-Cystathionine

C7H14N2O4S (222.0674244)

Cystathionine is a dipeptide formed by serine and homocysteine. Cystathioninuria is a prominent manifestation of vitamin-B6 deficiency. The transsulfuration of methionine yields homocysteine, which combines with serine to form cystathionine, the proximate precursor of cysteine through the enzymatic activity of cystathionase. In conditions in which cystathionine gamma-synthase or cystathionase is deficient, for example, there is cystathioninuria. Although cystathionine has not been detected in normal human serum or plasma by most conventional methods, gas chromatographic/mass spectrometric methodology detected a mean concentration of cystathionine in normal human serum of 140 nM, with a range of 65 to 301 nM. Cystathionine concentrations in CSF have been 10, 1, and 0.5 uM, and "not detected". Only traces (i.e., <1 uM) of cystathionine are present in normal CSF.587. Gamma-cystathionase deficiency (also known as Cystathioninuria), which is an autosomal recessive disorder (NIH: 2428), provided the first instance in which, in a human, the major biochemical abnormality due to a defined enzyme defect was clearly shown to be alleviated by administration of large doses of pyridoxine. The response in gamma-cystathionase-deficient patients is not attributable to correction of a preexisting deficiency of this vitamin (OMMBID, Chap. 88). Isolated from Phallus impudicus (common stinkhorn) CONFIDENCE standard compound; INTERNAL_ID 146 KEIO_ID C019; [MS2] KO008910 KEIO_ID C047 KEIO_ID C019 Acquisition and generation of the data is financially supported in part by CREST/JST. CONFIDENCE standard compound; ML_ID 30 L-Cystathionine is a nonprotein thioether and is a key amino acid associated with the metabolic state of sulfur-containing amino acids. L-Cystathionine protects against Homocysteine-induced mitochondria-dependent apoptosis of vascular endothelial cells (HUVECs). L-Cystathionine plays an important role in cardiovascular protection[1][2]. L-Cystathionine is a nonprotein thioether and is a key amino acid associated with the metabolic state of sulfur-containing amino acids. L-Cystathionine protects against Homocysteine-induced mitochondria-dependent apoptosis of vascular endothelial cells (HUVECs). L-Cystathionine plays an important role in cardiovascular protection[1][2].

Homocysteine

C4H9NO2S (135.0353974)

A high level of blood serum homocysteine is a powerful risk factor for cardiovascular disease. Unfortunately, one study which attempted to decrease the risk by lowering homocysteine was not fruitful. This study was conducted on nearly 5000 Norwegian heart attack survivors who already had severe, late-stage heart disease. No study has yet been conducted in a preventive capacity on subjects who are in a relatively good state of health.; Elevated levels of homocysteine have been linked to increased fractures in elderly persons. The high level of homocysteine will auto-oxidize and react with reactive oxygen intermediates and damage endothelial cells and has a higher risk to form a thrombus. Homocysteine does not affect bone density. Instead, it appears that homocysteine affects collagen by interfering with the cross-linking between the collagen fibers and the tissues they reinforce. Whereas the HOPE-2 trial showed a reduction in stroke incidence, in those with stroke there is a high rate of hip fractures in the affected side. A trial with 2 homocysteine-lowering vitamins (folate and B12) in people with prior stroke, there was an 80\\\\\\% reduction in fractures, mainly hip, after 2 years. Interestingly, also here, bone density (and the number of falls) were identical in the vitamin and the placebo groups.; Homocysteine is a sulfur-containing amino acid that arises during methionine metabolism. Although its concentration in plasma is only about 10 micromolar (uM), even moderate hyperhomocysteinemia is associated with increased incidence of cardiovascular disease and Alzheimers disease. Elevations in plasma homocysteine are commonly found as a result of vitamin deficiencies, polymorphisms of enzymes of methionine metabolism, and renal disease. Pyridoxal, folic acid, riboflavin, and Vitamin B(12) are all required for methionine metabolism, and deficiency of each of these vitamins result in elevated plasma homocysteine. A polymorphism of methylenetetrahydrofolate reductase (C677T), which is quite common in most populations with a homozygosity rate of 10-15 \\\\\\%, is associated with moderate hyperhomocysteinemia, especially in the context of marginal folate intake. Plasma homocysteine is inversely related to plasma creatinine in patients with renal disease. This is due to an impairment in homocysteine removal in renal disease. The role of these factors, and of modifiable lifestyle factors, in affecting methionine metabolism and in determining plasma homocysteine levels is discussed. Homocysteine is an independent cardiovascular disease (CVD) risk factor modifiable by nutrition and possibly exercise. Homocysteine was first identified as an important biological compound in 1932 and linked with human disease in 1962 when elevated urinary homocysteine levels were found in children with mental retardation. This condition, called homocysteinuria, was later associated with premature occlusive CVD, even in children. These observations led to research investigating the relationship of elevated homocysteine levels and CVD in a wide variety of populations including middle age and elderly men and women with and without traditional risk factors for CVD. (PMID 17136938, 15630149); Homocysteine is an amino acid with the formula HSCH2CH2CH(NH2)CO2H. It is a homologue of the amino acid cysteine, differing by an additional methylene (-CH2-) group. It is biosynthesized from methionine by the removal of its terminal C? methyl group. Homocysteine can be recycled into methionine or converted into cysteine with the aid of B-vitamins.; Studies reported in 2006 have shown that giving vitamins [folic acid, B6 and B12] to reduce homocysteine levels may not quickly offer benefit, however a significant 25\\\\\\% reduction in stroke was found in the HOPE-2 study even in patients mostly with existing serious arterial decline although the overall death rate was not significantly changed by the intervention in the trial. Clearly, reducing homocysteine does not quickly repair existing... Homocysteine (CAS: 454-29-5) is a sulfur-containing amino acid that arises during methionine metabolism. Although its concentration in plasma is only about 10 micromolar (uM), even moderate hyperhomocysteinemia is associated with an increased incidence of cardiovascular disease and Alzheimers disease. Elevations in plasma homocysteine are commonly found as a result of vitamin deficiencies, polymorphisms of enzymes of methionine metabolism, and renal disease. It has been identified as a uremic toxin according to the European Uremic Toxin Working Group (PMID: 22626821). Pyridoxal, folic acid, riboflavin, and vitamin B(12) are all required for methionine metabolism, and deficiency of each of these vitamins result in elevated plasma homocysteine. A polymorphism of methylenetetrahydrofolate reductase (C677T), which is quite common in most populations with a homozygosity rate of 10-15 \\\\\\%, is associated with moderate hyperhomocysteinemia, especially in the context of marginal folate intake. Plasma homocysteine is inversely related to plasma creatinine in patients with renal disease. This is due to an impairment in homocysteine removal in renal disease. The role of these factors, and of modifiable lifestyle factors, in affecting methionine metabolism and in determining plasma homocysteine levels is discussed. Homocysteine is an independent cardiovascular disease (CVD) risk factor modifiable by nutrition and possibly exercise. Homocysteine was first identified as an important biological compound in 1932 and linked with human disease in 1962 when elevated urinary homocysteine levels were found in children with mental retardation. This condition, called homocystinuria, was later associated with premature occlusive CVD, even in children. These observations led to research investigating the relationship of elevated homocysteine levels and CVD in a wide variety of populations including middle age and elderly men and women with and without traditional risk factors for CVD (PMID: 17136938 , 15630149). Moreover, homocysteine is found to be associated with cystathionine beta-synthase deficiency, cystathioninuria, methylenetetrahydrofolate reductase deficiency, and sulfite oxidase deficiency, which are inborn errors of metabolism. [Spectral] L-Homocysteine (exact mass = 135.0354) and L-Valine (exact mass = 117.07898) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. Homocysteine is biosynthesized naturally via a multi-step process.[9] First, methionine receives an adenosine group from ATP, a reaction catalyzed by S-adenosyl-methionine synthetase, to give S-adenosyl methionine (SAM-e). SAM-e then transfers the methyl group to an acceptor molecule, (e.g., norepinephrine as an acceptor during epinephrine synthesis, DNA methyltransferase as an intermediate acceptor in the process of DNA methylation). The adenosine is then hydrolyzed to yield L-homocysteine. L-Homocysteine has two primary fates: conversion via tetrahydrofolate (THF) back into L-methionine or conversion to L-cysteine.[10] Biosynthesis of cysteine Mammals biosynthesize the amino acid cysteine via homocysteine. Cystathionine β-synthase catalyses the condensation of homocysteine and serine to give cystathionine. This reaction uses pyridoxine (vitamin B6) as a cofactor. Cystathionine γ-lyase then converts this double amino acid to cysteine, ammonia, and α-ketobutyrate. Bacteria and plants rely on a different pathway to produce cysteine, relying on O-acetylserine.[11] Methionine salvage Homocysteine can be recycled into methionine. This process uses N5-methyl tetrahydrofolate as the methyl donor and cobalamin (vitamin B12)-related enzymes. More detail on these enzymes can be found in the article for methionine synthase. Other reactions of biochemical significance Homocysteine can cyclize to give homocysteine thiolactone, a five-membered heterocycle. Because of this "self-looping" reaction, homocysteine-containing peptides tend to cleave themselves by reactions generating oxidative stress.[12] Homocysteine also acts as an allosteric antagonist at Dopamine D2 receptors.[13] It has been proposed that both homocysteine and its thiolactone may have played a significant role in the appearance of life on the early Earth.[14] L-Homocysteine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=454-28-4 (retrieved 2024-06-29) (CAS RN: 6027-13-0). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). DL-Homocysteine is a weak neurotoxin, and can affect the production of kynurenic acid in the brain. DL-Homocysteine is a weak neurotoxin, and can affect the production of kynurenic acid in the brain. L-Homocysteine, a homocysteine metabolite, is a homocysteine that has L configuration. L-Homocysteine induces upregulation of cathepsin V that mediates vascular endothelial inflammation in hyperhomocysteinaemia[1][2].

3-Sulfinoalanine

C3H7NO4S (153.0095782)

3-Sulfinoalanine or cysteinesulfinic acid is a N-methyl-D-aspartate agonist. It is a product of cysteine dioxygenase or CDO [EC 1.13.11.20]. In humans cysteine catabolism is tightly regulated via regulation of cysteine dioxygenase (CDO) levels in the liver, with the turnover of CDO protein being dramatically decreased when intracellular cysteine levels increase. This occurs in response to changes in the intracellular cysteine concentration via changes in the rate of CDO ubiquitination and degradation. Expressed at high levels in the liver with lower levels in the kidney, brain, and lung, cysteine dioxygenase catalyzes the addition of molecular oxygen to the sulfhydryl group of cysteine, yielding cysteinesulfinic acid. The oxidative catabolism of cysteine to cysteinesulfinate by CDO represents an irreversible loss of cysteine from the free amino acid pool. Once generated, cysteinesulfinate is shuttled into several pathways including hypotaurine/taurine synthesis, sulfite/sulfate production, and the generation of pyruvate. [HMDB] 3-Sulfinoalanine or cysteinesulfinic acid is an N-methyl-D-aspartate agonist. It is a product of cysteine dioxygenase or CDO (EC 1.13.11.20). In humans, cysteine catabolism is tightly regulated via regulation of cysteine dioxygenase (CDO) levels in the liver, with the turnover of CDO protein being dramatically decreased when intracellular cysteine levels increase. This occurs in response to changes in the intracellular cysteine concentration via changes in the rate of CDO ubiquitination and degradation. Expressed at high levels in the liver with lower levels in the kidney, brain, and lung, cysteine dioxygenase catalyzes the addition of molecular oxygen to the sulfhydryl group of cysteine, yielding cysteinesulfinic acid. The oxidative catabolism of cysteine to cysteinesulfinate by CDO represents an irreversible loss of cysteine from the free amino acid pool. Once generated, cysteinesulfinate is shuttled into several pathways including hypotaurine/taurine synthesis, sulfite/sulfate production, and the generation of pyruvate. [Spectral] 3-Sulfino-L-alanine (exact mass = 153.00958) and L-Isoleucine (exact mass = 131.09463) and alpha-D-Glucose 6-phosphate (exact mass = 260.02972) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. [Spectral] 3-Sulfino-L-alanine (exact mass = 153.00958) and alpha-D-Glucose 6-phosphate (exact mass = 260.02972) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. [Spectral] 3-Sulfino-L-alanine (exact mass = 153.00958) and sn-Glycerol 3-phosphate (exact mass = 172.01367) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. KEIO_ID C015 L-Cysteinesulfinic acid is a potent agonist at several rat metabotropic glutamate receptors (mGluRs) with pEC50s of 3.92, 4.6, 3.9, 2.7, 4.0, and 3.94 for mGluR1, mGluR5, mGluR2, mGluR4, mGluR6, and mGluR8, respectively[1]. L-Cysteinesulfinic acid is a potent agonist at several rat metabotropic glutamate receptors (mGluRs) with pEC50s of 3.92, 4.6, 3.9, 2.7, 4.0, and 3.94 for mGluR1, mGluR5, mGluR2, mGluR4, mGluR6, and mGluR8, respectively[1].

L-Cystine

C6H12N2O4S2 (240.0238472)

Cystine is an oxidized dimeric form of cysteine. It is formed by linking two cysteine residues via a disulfide bond (Cys-S-S-Cys) between the -SH groups. Cystine is found in high concentrations in digestive enzymes and in the cells of the immune system, skeletal and connective tissues, skin, and hair. Hair and skin are 10-14\\\% cystine. Cystine is the preferred form of cysteine for the synthesis of glutathione in cells involved in the immune system (e.g. macrophages and astrocytes). Lymphocytes and neurons prefer cysteine for glutathione production. Optimizing glutathione levels in macrophages and astrocytes with cystine allows these cells to provide cysteine to lymphocytes and neurons directly upon demand (Wikipedia). (-)-Cystine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=56-89-3 (retrieved 2024-06-29) (CAS RN: 56-89-3). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0).

L-Serine

C3H7NO3 (105.0425912)

Serine (Ser) or L-serine is an alpha-amino acid. These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon). Amino acids are organic compounds that contain amino (–NH2) and carboxyl (–COOH) functional groups, along with a side chain (R group) specific to each amino acid. L-serine is one of 20 proteinogenic amino acids, i.e., the amino acids used in the biosynthesis of proteins. Serine is found in all organisms ranging from bacteria to plants to animals. It is classified as a polar, uncharged (at physiological pH), aliphatic amino acid. In humans, serine is a nonessential amino acid that can be easily derived from glycine. A non-essential amino acid is an amino acid that can be synthesized from central metabolic pathway intermediates in humans and is not required in the diet. Like all the amino acid building blocks of protein and peptides, serine can become essential under certain conditions, and is thus important in maintaining health and preventing disease. L-Serine may be derived from four possible sources: dietary intake; biosynthesis from the glycolytic intermediate 3-phosphoglycerate; from glycine; and by protein and phospholipid degradation. Little data is available on the relative contributions of each of these four sources of l-serine to serine homoeostasis. It is very likely that the predominant source of l-serine will be very different in different tissues and during different stages of human development. In the biosynthetic pathway, the glycolytic intermediate 3-phosphoglycerate is converted into phosphohydroxypyruvate, in a reaction catalyzed by 3-phosphoglycerate dehydrogenase (3- PGDH; EC 1.1.1.95). Phosphohydroxypyruvate is metabolized to phosphoserine by phosphohydroxypyruvate aminotransferase (EC 2.6.1.52) and, finally, phosphoserine is converted into l-serine by phosphoserine phosphatase (PSP; EC 3.1.3.3). In liver tissue, the serine biosynthetic pathway is regulated in response to dietary and hormonal changes. Of the three synthetic enzymes, the properties of 3-PGDH and PSP are the best documented. Hormonal factors such as glucagon and corticosteroids also influence 3-PGDH and PSP activities in interactions dependent upon the diet. L-serine is the predominant source of one-carbon groups for the de novo synthesis of purine nucleotides and deoxythymidine monophosphate. It has long been recognized that, in cell cultures, L-serine is a conditional essential amino acid, because it cannot be synthesized in sufficient quantities to meet the cellular demands for its utilization. In recent years, L-serine and the products of its metabolism have been recognized not only to be essential for cell proliferation, but also to be necessary for specific functions in the central nervous system. The findings of altered levels of serine and glycine in patients with psychiatric disorders and the severe neurological abnormalities in patients with defects of L-serine synthesis underscore the importance of L-serine in brain development and function. (PMID 12534373). [Spectral] L-Serine (exact mass = 105.04259) and D-2-Aminobutyrate (exact mass = 103.06333) and 4-Aminobutanoate (exact mass = 103.06333) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. Dietary supplement. L-Serine is found in many foods, some of which are cold cut, mammee apple, coho salmon, and carrot. L-Serine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=56-45-1 (retrieved 2024-07-01) (CAS RN: 56-45-1). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). L-Serine ((-)-Serine; (S)-Serine), one of the so-called non-essential amino acids, plays a central role in cellular proliferation. L-Serine ((-)-Serine; (S)-Serine), one of the so-called non-essential amino acids, plays a central role in cellular proliferation.

L-Methionine

C5H11NO2S (149.0510466)

Methionine (Met), also known as L-methionine, is an alpha-amino acid. These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon). Amino acids are organic compounds that contain amino (–NH2) and carboxyl (–COOH) functional groups, along with a side chain (R group) specific to each amino acid. Methionine is one of 20 proteinogenic amino acids, i.e., the amino acids used in the biosynthesis of proteins. Methionine is found in all organisms ranging from bacteria to plants to animals. It is classified as an aliphatic, non-polar amino acid. Methionine is an essential amino acid (there are 9 essential amino acids), meaning the body cannot synthesize it, and it must be obtained from the diet. It is required for normal growth and development of humans, other mammals, and avian species. In addition to being a substrate for protein synthesis, methionine is an intermediate in transmethylation reactions, serving as the major methyl group donor in vivo, including the methyl groups for DNA and RNA intermediates. Methionine is a methyl acceptor for 5-methyltetrahydrofolate-homocysteine methyltransferase (methionine synthase), the only reaction that allows for the recycling of this form of folate, and is also a methyl acceptor for the catabolism of betaine. Methionine is the metabolic precursor for cysteine. Only the sulfur atom from methionine is transferred to cysteine; the carbon skeleton of cysteine is donated by serine (PMID: 16702340 ). There is a general consensus concerning normal sulfur amino acid (SAA) requirements. WHO recommendations amount to 13 mg/kg per 24 h in healthy adults. This amount is roughly doubled in artificial nutrition regimens. In disease or after trauma, requirements may be altered for methionine, cysteine, and taurine. Although in specific cases of congenital enzyme deficiency, prematurity, or diminished liver function, hypermethioninemia or hyperhomocysteinemia may occur, SAA supplementation can be considered safe in amounts exceeding 2-3 times the minimum recommended daily intake. Apart from some very specific indications (e.g. acetaminophen poisoning) the usefulness of SAA supplementation is not yet established (PMID: 16702341 ). Methionine is known to exacerbate psychopathological symptoms in schizophrenic patients, but there is no evidence of similar effects in healthy subjects. The role of methionine as a precursor of homocysteine is the most notable cause for concern. Acute doses of methionine can lead to acute increases in plasma homocysteine, which can be used as an index of the susceptibility to cardiovascular disease. Sufficiently high doses of methionine can actually result in death. Longer-term studies in adults have indicated no adverse consequences of moderate fluctuations in dietary methionine intake, but intakes higher than 5 times the normal amount resulted in elevated homocysteine levels. These effects of methionine on homocysteine and vascular function are moderated by supplements of vitamins B-6, B-12, C, and folic acid (PMID: 16702346 ). When present in sufficiently high levels, methionine can act as an atherogen and a metabotoxin. An atherogen is a compound that when present at chronically high levels causes atherosclerosis and cardiovascular disease. A metabotoxin is an endogenously produced metabolite that causes adverse health effects at chronically high levels. Chronically high levels of methionine are associated with at least ten inborn errors of metabolism, including cystathionine beta-synthase deficiency, glycine N-methyltransferase deficiency, homocystinuria, tyrosinemia, galactosemia, homocystinuria-megaloblastic anemia due to defects in cobalamin metabolism, methionine adenosyltransferase deficiency, methylenetetrahydrofolate reductase deficiency, and S-adenosylhomocysteine (SAH) hydrolase deficiency. Chronically elevated levels of methionine in infants can lead to intellectual disability and othe... [Spectral] L-Methionine (exact mass = 149.05105) and Adenosine (exact mass = 267.09675) and S-Adenosyl-L-homocysteine (exact mass = 384.12159) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. [Spectral] L-Methionine (exact mass = 149.05105) and Tyramine (exact mass = 137.08406) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. l-Methionine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=63-68-3 (retrieved 2024-07-01) (CAS RN: 63-68-3). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). L-Methionine is the L-isomer of Methionine, an essential amino acid for human development. Methionine acts as a hepatoprotectant. L-Methionine is the L-isomer of Methionine, an essential amino acid for human development. Methionine acts as a hepatoprotectant.

S-adenosylhomocysteine (SAH)

C14H20N6O5S (384.12158300000004)

S-Adenosyl-L-homocysteine (SAH) is formed by the demethylation of S-adenosyl-L-methionine. S-Adenosylhomocysteine (AdoHcy or SAH) is also the immediate precursor of all of the homocysteine produced in the body. The reaction is catalyzed by S-adenosylhomocysteine hydrolase and is reversible with the equilibrium favoring formation of SAH. In vivo, the reaction is driven in the direction of homocysteine formation by the action of the enzyme adenosine deaminase which converts the second product of the S-adenosylhomocysteine hydrolase reaction, adenosine, to inosine. Except for methyl transfer from betaine and from methylcobalamin in the methionine synthase reaction, SAH is the product of all methylation reactions that involve S-adenosylmethionine (SAM) as the methyl donor. Methylation is significant in epigenetic regulation of protein expression via DNA and histone methylation. The inhibition of these SAM-mediated processes by SAH is a proven mechanism for metabolic alteration. Because the conversion of SAH to homocysteine is reversible, with the equilibrium favoring the formation of SAH, increases in plasma homocysteine are accompanied by an elevation of SAH in most cases. Disturbances in the transmethylation pathway indicated by abnormal SAH, SAM, or their ratio have been reported in many neurodegenerative diseases, such as dementia, depression, and Parkinsons disease (PMID:18065573, 17892439). Therefore, when present in sufficiently high levels, S-adenosylhomocysteine can act as an immunotoxin and a metabotoxin. An immunotoxin disrupts, limits the function, or destroys immune cells. A metabotoxin is an endogenous metabolite that causes adverse health effects at chronically high levels. Chronically high levels of S-adenosylhomocysteine are associated with S-adenosylhomocysteine (SAH) hydrolase deficiency and adenosine deaminase deficiency. S-Adenosylhomocysteine forms when there are elevated levels of homocysteine and adenosine. S-Adenosyl-L-homocysteine is a potent inhibitor of S-adenosyl-L-methionine-dependent methylation reactions. It is toxic to immature lymphocytes and can lead to immunosuppression (PMID:221926). S-adenosylhomocysteine, also known as adohcy or sah, is a member of the class of compounds known as 5-deoxy-5-thionucleosides. 5-deoxy-5-thionucleosides are 5-deoxyribonucleosides in which the ribose is thio-substituted at the 5position by a S-alkyl group. S-adenosylhomocysteine is slightly soluble (in water) and a moderately acidic compound (based on its pKa). S-adenosylhomocysteine can be found in a number of food items such as rapini, european plum, rambutan, and pepper (c. pubescens), which makes S-adenosylhomocysteine a potential biomarker for the consumption of these food products. S-adenosylhomocysteine can be found primarily in blood, cerebrospinal fluid (CSF), feces, and urine, as well as throughout most human tissues. S-adenosylhomocysteine exists in all living species, ranging from bacteria to humans. In humans, S-adenosylhomocysteine is involved in several metabolic pathways, some of which include phosphatidylcholine biosynthesis PC(14:0/18:3(9Z,12Z,15Z)), phosphatidylcholine biosynthesis PC(22:4(7Z,10Z,13Z,16Z)/22:0), phosphatidylcholine biosynthesis PC(20:3(5Z,8Z,11Z)/22:2(13Z,16Z)), and phosphatidylcholine biosynthesis PC(18:3(6Z,9Z,12Z)/22:5(7Z,10Z,13Z,16Z,19Z)). S-adenosylhomocysteine is also involved in several metabolic disorders, some of which include 3-phosphoglycerate dehydrogenase deficiency, hawkinsinuria, non ketotic hyperglycinemia, and tyrosine hydroxylase deficiency. Moreover, S-adenosylhomocysteine is found to be associated with neurodegenerative disease and parkinsons disease. S-adenosylhomocysteine is a non-carcinogenic (not listed by IARC) potentially toxic compound. S-Adenosyl-L-homocysteine (SAH) is an amino acid derivative used in several metabolic pathways in most organisms. It is an intermediate in the synthesis of cysteine and adenosine . [Spectral] S-Adenosyl-L-homocysteine (exact mass = 384.12159) and Adenosine (exact mass = 267.09675) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. [Spectral] S-Adenosyl-L-homocysteine (exact mass = 384.12159) and Cytidine (exact mass = 243.08552) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. Acquisition and generation of the data is financially supported in part by CREST/JST. COVID info from PDB, Protein Data Bank, WikiPathways Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS SAH (S-Adenosylhomocysteine) is an amino acid derivative and a modulartor in several metabolic pathways. It is an intermediate in the synthesis of cysteine and adenosine[1]. SAH is an inhibitor for METTL3-METTL14 heterodimer complex (METTL3-14) with an IC50 of 0.9 μM[2]. SAH (S-Adenosylhomocysteine) is an amino acid derivative and a modulartor in several metabolic pathways. It is an intermediate in the synthesis of cysteine and adenosine[1]. SAH is an inhibitor for METTL3-METTL14 heterodimer complex (METTL3-14) with an IC50 of 0.9 μM[2].

L-Cysteine

C3H7NO2S (121.0197482)

Cysteine (Cys), also known as L-cysteine is an alpha-amino acid. These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon). Amino acids are organic compounds that contain amino (–NH2) and carboxyl (–COOH) functional groups, along with a side chain (R group) specific to each amino acid. L-alanine is one of 20 proteinogenic amino acids, i.e., the amino acids used in the biosynthesis of proteins. Cysteine is found in all organisms ranging from bacteria to plants to animals. It is classified as an aliphatic, non-polar, sulfur-containing amino acid. Cysteine is an important source of sulfur in human metabolism, and although it is classified as a non-essential amino acid, cysteine may be essential for infants, the elderly, and individuals with certain metabolic disease or who suffer from malabsorption syndromes. Cysteine can occasionally be considered as an essential or conditionally essential amino acid. Cysteine is unique amongst the twenty natural amino acids as it contains a thiol group. Thiol groups can undergo oxidation/reduction (redox) reactions; when cysteine is oxidized it can form cystine, which is two cysteine residues joined by a disulfide bond. This reaction is reversible since the reduction of this disulphide bond regenerates two cysteine molecules. The disulphide bonds of cystine are crucial to defining the structures of many proteins. Cysteine is often involved in electron-transfer reactions, and help the enzyme catalyze its reaction. Cysteine is also part of the antioxidant glutathione. N-Acetyl-L-cysteine (NAC) is a form of cysteine where an acetyl group is attached to cysteines nitrogen atom and is sold as a dietary supplement. Cysteine is named after cystine, which comes from the Greek word kustis meaning bladder (cystine was first isolated from kidney stones). Oxidation of cysteine can produce a disulfide bond with another thiol and further oxidation can produce sulphfinic or sulfonic acids. The cysteine thiol group is also a nucleophile and can undergo addition and substitution reactions. Thiol groups become much more reactive when they are ionized, and cysteine residues in proteins have pKa values close to neutrality, so they are often in their reactive thiolate form in the cell. The thiol group also has a high affinity for heavy metals and proteins containing cysteine will bind metals such as mercury, lead, and cadmium tightly. Due to this ability to undergo redox reactions, cysteine has antioxidant properties. Cysteine is important in energy metabolism. As cystine, it is a structural component of many tissues and hormones. Cysteine has clinical uses ranging from treating baldness to psoriasis to preventing smokers hack. In some cases, oral cysteine therapy has proved excellent for treatment of asthmatics, enabling them to stop theophylline and other medications. Cysteine also enhances the effect of topically applied silver, tin, and zinc salts in preventing dental cavities. In the future, cysteine may play a role in the treatment of cobalt toxicity, diabetes, psychosis, cancer, and seizures (http://www.dcnutrition.com/AminoAcids/). Cysteine has been identified as a uremic toxin according to the European Uremic Toxin Working Group (PMID: 22626821). [Spectral] L-Cysteine (exact mass = 121.01975) and D-2-Aminobutyrate (exact mass = 103.06333) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. [Spectral] L-Cysteine (exact mass = 121.01975) and Creatine (exact mass = 131.06948) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. Detoxicant, dietary supplement, dough strengthener, yeast nutrient for leavened bakery products. Flavouring agent. Enzymic browning inhibitor. L-Cysteine is found in many foods, some of which are bilberry, mugwort, cowpea, and sweet bay. L-(+)-Cysteine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=52-90-4 (retrieved 2024-07-01) (CAS RN: 52-90-4). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). L-Cysteine is a conditionally essential amino acid, which acts as a precursor for biologically active molecules such as hydrogen sulphide (H2S), glutathione and taurine. L-Cysteine suppresses ghrelin and reduces appetite in rodents and humans[1]. L-Cysteine is a conditionally essential amino acid, which acts as a precursor for biologically active molecules such as hydrogen sulphide (H2S), glutathione and taurine. L-Cysteine suppresses ghrelin and reduces appetite in rodents and humans[1].

Taurocholate

C26H45NO7S (515.291658)

Taurocholic acid is a bile acid and is the product of the conjugation of cholic acid with taurine. Its sodium salt is the chief ingredient of the bile of carnivorous animals. Bile acids are steroid acids found predominantly in the bile of mammals. The distinction between different bile acids is minute, depending only on the presence or absence of hydroxyl groups on positions 3, 7, and 12. Bile acids are physiological detergents that facilitate excretion, absorption, and transport of fats and sterols in the intestine and liver. Bile acids are also steroidal amphipathic molecules derived from the catabolism of cholesterol. They modulate bile flow and lipid secretion, are essential for the absorption of dietary fats and vitamins, and have been implicated in the regulation of all the key enzymes involved in cholesterol homeostasis. Bile acids recirculate through the liver, bile ducts, small intestine, and portal vein to form an enterohepatic circuit. They exist as anions at physiological pH, and consequently require a carrier for transport across the membranes of the enterohepatic tissues. The unique detergent properties of bile acids are essential for the digestion and intestinal absorption of hydrophobic nutrients. Bile acids have potent toxic properties (e.g. membrane disruption) and there are a plethora of mechanisms to limit their accumulation in blood and tissues (PMID: 11316487, 16037564, 12576301, 11907135). Taurocholic acid, as with all bile acids, acts as a detergent to solubilize fats for absorption and is itself absorbed. It is used as a cholagogue and choleretic (a bile purging agent). Hydrolysis of taurocholic acid yields taurine, a nonessential amino acid. Taurocholic acid is one of the main components of urinary nonsulfated bile acids in biliary atresia. Raised levels of taurocholate in fetal serum in obstetric cholestasis may result in the development of a fetal dysrhythmia and sudden intra-uterine death (PMID: 3944741, 11256973). Taurocholic acid. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=81-24-3 (retrieved 2024-07-01) (CAS RN: 81-24-3). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). Taurocholic acid (N-Choloyltaurine) is a bile acid involved in the emulsification of fats. Taurocholic acid (N-Choloyltaurine) is a bile acid involved in the emulsification of fats.

Hypotaurine

C2H7NO2S (109.0197482)

Hypotaurine belongs to the class of organic compounds known as sulfinic acids. Sulfinic acids are compounds containing a sulfinic acid functional group, with the general structure RS(=O)OH (R = organyl, not H). Hypotaurine exists in all living species, ranging from bacteria to humans. Within humans, hypotaurine participates in a number of enzymatic reactions. In particular, hypotaurine can be biosynthesized from cysteamine; which is catalyzed by the enzyme 2-aminoethanethiol dioxygenase. In addition, hypotaurine can be biosynthesized from 3-sulfinoalanine through its interaction with the enzyme cysteine sulfinic acid decarboxylase. In humans, hypotaurine is involved in taurine and hypotaurine metabolism. [Spectral] Hypotaurine (exact mass = 109.01975) and Cytosine (exact mass = 111.04326) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. Hypotaurine is a product of enzyme cysteamine dioxygenase [EC 1.13.11.19] in taurine and hypotaurine metabolism pathway (KEGG). It may function as an antioxidant and a protective agent under physiological conditions (PMID 14992269). [HMDB] Hypotaurine (2-aminoethanesulfinic acid), an intermediate in taurine biosynthesis from cysteine in astrocytes, is an endogenous inhibitory amino acid of the glycine receptor. Antioxidant[1].

Alpha-ketobutyrate

C4H6O3 (102.0316926)

3-methyl pyruvic acid, also known as alpha-ketobutyric acid or 2-oxobutyric acid, belongs to short-chain keto acids and derivatives class of compounds. Those are keto acids with an alkyl chain the contains less than 6 carbon atoms. Thus, 3-methyl pyruvic acid is considered to be a fatty acid lipid molecule. 3-methyl pyruvic acid is soluble (in water) and a weakly acidic compound (based on its pKa). 3-methyl pyruvic acid can be found in a number of food items such as pepper (c. baccatum), triticale, european plum, and black walnut, which makes 3-methyl pyruvic acid a potential biomarker for the consumption of these food products. 3-methyl pyruvic acid can be found primarily in blood, cerebrospinal fluid (CSF), saliva, and urine. 3-methyl pyruvic acid exists in all living species, ranging from bacteria to humans. In humans, 3-methyl pyruvic acid is involved in several metabolic pathways, some of which include methionine metabolism, homocysteine degradation, threonine and 2-oxobutanoate degradation, and propanoate metabolism. 3-methyl pyruvic acid is also involved in several metabolic disorders, some of which include dimethylglycine dehydrogenase deficiency, methylenetetrahydrofolate reductase deficiency (MTHFRD), s-adenosylhomocysteine (SAH) hydrolase deficiency, and hyperglycinemia, non-ketotic. 2-Ketobutyric acid, also known as alpha-ketobutyrate or 2-oxobutyrate, belongs to the class of organic compounds known as short-chain keto acids and derivatives. These are keto acids with an alkyl chain the contains less than 6 carbon atoms. 2-Ketobutyric acid is a substance that is involved in the metabolism of many amino acids (glycine, methionine, valine, leucine, serine, threonine, isoleucine) as well as propanoate metabolism and C-5 branched dibasic acid metabolism. It is also one of the degradation products of threonine. It can be converted into propionyl-CoA (and subsequently methylmalonyl CoA, which can be converted into succinyl CoA, a citric acid cycle intermediate), and thus enter the citric acid cycle. More specifically, 2-ketobutyric acid is a product of the lysis of cystathionine. 2-Oxobutanoic acid is a product in the enzymatic cleavage of cystathionine.

Dimethylglycine

C4H9NO2 (103.0633254)

Dimethylglycine (DMG) is an amino acid derivative found in the cells of all plants and animals and can be obtained in the diet in small amounts from grains and meat. The human body produces DMG when metabolizing choline into glycine. Dimethylglycine that is not metabolized in the liver is transported by the circulatory system to body tissue. Dimethylglycine was popular with Russian athletes and cosmonauts owing to its reputed ability to increase endurance and reduce fatigue. DMG is also a byproduct of homocysteine metabolism. Homocysteine and betaine are converted to methionine and N,N-dimethylglycine by betaine-homocysteine methyltransferase. DMG in the urine is a biomarker for the consumption of legumes. It is also a microbial metabolite (PMID: 25901889). Dimethylglycine (DMG) is an amino acid derivative found in the cells of all plants and animals and can be obtained in the diet in small amounts from grains and meat. The human body produces DMG when metabolizing choline into Glycine. Dimethylglycine that is not metabolized in the liver is transported by the circulatory system to body tissue. Dimethylglycine was popular with Russian athletes and cosmonauts owing to its reputed ability to increase endurance and reduce fatigue. DMG is also a byproduct of homocysteine metabolism. Homocysteine and betaine are converted to methionine and N, N-dimethylglycine by betaine-homocysteine methyltransferase. [HMDB]. Dimethylglycine in the urine is a biomarker for the consumption of legumes. N,N-Dimethylglycine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=1118-68-9 (retrieved 2024-07-16) (CAS RN: 1118-68-9). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). N-Methylsarcosine is an amino acid building block for protein, found in a small amount in the body.

Cysteic acid

C3H7NO5S (169.00449319999998)

Cysteic acid is a crystalline amino acid formed in the oxidation of cysteine; it is a precursor of taurine. A crystalline amino acid formed in the oxidation of cysteine; it is a precursor of taurine. [HMDB]

Pyruvic acid

C3H4O3 (88.0160434)

Pyruvic acid, also known as 2-oxopropanoic acid or alpha-ketopropionic acid, belongs to alpha-keto acids and derivatives class of compounds. Those are organic compounds containing an aldehyde substituted with a keto group on the adjacent carbon. Thus, pyruvic acid is considered to be a fatty acid lipid molecule. Pyruvic acid is soluble (in water) and a moderately acidic compound (based on its pKa). Pyruvic acid can be synthesized from propionic acid. Pyruvic acid is also a parent compound for other transformation products, including but not limited to, 4-hydroxy-3-iodophenylpyruvate, 3-acylpyruvic acid, and methyl pyruvate. Pyruvic acid can be found in a number of food items such as kumquat, groundcherry, coconut, and prunus (cherry, plum), which makes pyruvic acid a potential biomarker for the consumption of these food products. Pyruvic acid can be found primarily in most biofluids, including sweat, blood, urine, and feces, as well as throughout most human tissues. Pyruvic acid exists in all living species, ranging from bacteria to humans. In humans, pyruvic acid is involved in several metabolic pathways, some of which include glycogenosis, type IB, glycolysis, urea cycle, and gluconeogenesis. Pyruvic acid is also involved in several metabolic disorders, some of which include non ketotic hyperglycinemia, pyruvate dehydrogenase complex deficiency, fructose-1,6-diphosphatase deficiency, and 4-hydroxybutyric aciduria/succinic semialdehyde dehydrogenase deficiency. Moreover, pyruvic acid is found to be associated with anoxia, schizophrenia, fumarase deficiency, and meningitis. Pyruvic acid is a non-carcinogenic (not listed by IARC) potentially toxic compound. Pyruvic acid is a drug which is used for nutritional supplementation, also for treating dietary shortage or imbalanc. Pyruvic acid can be made from glucose through glycolysis, converted back to carbohydrates (such as glucose) via gluconeogenesis, or to fatty acids through a reaction with acetyl-CoA. It can also be used to construct the amino acid alanine and can be converted into ethanol or lactic acid via fermentation . Those taking large doses of supplemental pyruvate—usually greater than 5 grams daily—have reported gastrointestinal symptoms, including abdominal discomfort and bloating, gas and diarrhea. One child receiving pyruvate intravenously for restrictive cardiomyopathy died (DrugBank). Pyruvate serves as a biological fuel by being converted to acetyl coenzyme A, which enters the tricarboxylic acid or Krebs cycle where it is metabolized to produce ATP aerobically. Energy can also be obtained anaerobically from pyruvate via its conversion to lactate. Pyruvate injections or perfusions increase contractile function of hearts when metabolizing glucose or fatty acids. This inotropic effect is striking in hearts stunned by ischemia/reperfusion. The inotropic effect of pyruvate requires intracoronary infusion. Among possible mechanisms for this effect are increased generation of ATP and an increase in ATP phosphorylation potential. Another is activation of pyruvate dehydrogenase, promoting its own oxidation by inhibiting pyruvate dehydrogenase kinase. Pyruvate dehydrogenase is inactivated in ischemia myocardium. Yet another is reduction of cytosolic inorganic phosphate concentration. Pyruvate, as an antioxidant, is known to scavenge such reactive oxygen species as hydrogen peroxide and lipid peroxides. Indirectly, supraphysiological levels of pyruvate may increase cellular reduced glutathione (T3DB). Pyruvic acid or pyruvate is a simple alpha-keto acid. It is a three-carbon molecule containing a carboxylic acid group and a ketone functional group. Pyruvate is the simplest alpha-keto acid and according to official nomenclature by IUPAC, it is called alpha-keto propanoic acid. Like other keto acids, pyruvic acid can tautomerize from its ketone form to its enol form, containing a double bond and an alcohol. Pyruvate is found in all living organisms ranging from bacteria to plants to humans. It is intermediate compound in the metabolism of carbohydrates, proteins, and fats. Pyruvate is a key intermediate in several metabolic pathways throughout the cell. In particular, pyruvic acid can be made from glucose through glycolysis, converted back to carbohydrates (such as glucose) via gluconeogenesis, or to fatty acids through a reaction with acetyl-CoA. Pyruvic acid supplies energy to cells through the citric acid cycle (TCA or Krebs cycle) when oxygen is present (aerobic respiration), and alternatively ferments to produce lactate when oxygen is lacking (lactic acid). In glycolysis, phosphoenolpyruvate (PEP) is converted to pyruvate by pyruvate kinase. This reaction is strongly exergonic and irreversible. In gluconeogenesis, it takes two enzymes, pyruvate carboxylase and PEP carboxykinase, to catalyze the reverse transformation of pyruvate to PEP. Pyruvic acid is also a metabolite of Corynebacterium (PMID: 27872963). Pyruvic acid. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=127-17-3 (retrieved 2024-07-01) (CAS RN: 127-17-3). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). Pyruvic acid is an intermediate metabolite in the metabolism of carbohydrates, proteins, and fats. Pyruvic acid is an intermediate metabolite in the metabolism of carbohydrates, proteins, and fats.

AdoMet

C15H22N6O5S (398.1372322)

[Spectral] S-Adenosyl-L-methionine (exact mass = 398.13724) and L-Histidine (exact mass = 155.06948) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. A - Alimentary tract and metabolism > A16 - Other alimentary tract and metabolism products > A16A - Other alimentary tract and metabolism products > A16AA - Amino acids and derivatives Acquisition and generation of the data is financially supported in part by CREST/JST. C26170 - Protective Agent > C275 - Antioxidant COVID info from COVID-19 Disease Map Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS

Phosphate

H3O4P (97.9768968)

Phosphate is a salt of phosphoric acid and is an essential component of life. Organic phosphates are important in biochemistry, biogeochemistry, and ecology. In biological systems, phosphorus is found as a free phosphate ion in solution and is called inorganic phosphate, to distinguish it from phosphates bound in various phosphate esters. Inorganic phosphate is generally denoted Pi and at physiological (neutral) pH primarily consists of a mixture of HPO2-4 and H2PO-4 ions. Phosphates are most commonly found in the form of adenosine phosphates (AMP, ADP, and ATP) and in DNA and RNA, and can be released by the hydrolysis of ATP or ADP. Similar reactions exist for the other nucleoside diphosphates and triphosphates. Phosphoanhydride bonds in ADP and ATP, or other nucleoside diphosphates and triphosphates, contain high amounts of energy which give them their vital role in all living organisms. Phosphate must be actively transported into cells against its electrochemical gradient. In vertebrates, two unrelated families of Na+-dependent Pi transporters carry out this task. Remarkably, the two families transport different Pi species: whereas type II Na+/Pi cotransporters (SCL34) prefer divalent HPO4(2), type III Na+/Pi cotransporters (SLC20) transport monovalent H2PO4. The SCL34 family comprises both electrogenic and electroneutral members that are expressed in various epithelia and other polarized cells. Through regulated activity in apical membranes of the gut and kidney, they maintain body Pi homeostasis, and in salivary and mammary glands, liver, and testes they play a role in modulating the Pi content of luminal fluids. Phosphate levels in the blood play an important role in hormone signalling and in bone homeostasis. In classical endocrine regulation, low serum phosphate induces the renal production of the secosteroid hormone 1,25-dihydroxyvitamin D3 (1,25(OH)2D3). This active metabolite of vitamin D acts to restore circulating mineral (i.e. phosphate and calcium) levels by increasing absorption in the intestine, reabsorption in the kidney, and mobilization of calcium and phosphate from bone. Thus, chronic renal failure is associated with hyperparathyroidism, which in turn contributes to osteomalacia (softening of the bones). Another complication of chronic renal failure is hyperphosphatemia (low levels of phosphate in the blood). Hyperphosphatemia (excess levels of phosphate in the blood) is a prevalent condition in kidney dialysis patients and is associated with increased risk of mortality. Hypophosphatemia (hungry bone syndrome) has been associated with postoperative electrolyte aberrations and after parathyroidectomy (PMID: 17581921, 11169009, 11039261, 9159312, 17625581). Fibroblast growth factor 23 (FGF-23) has recently been recognized as a key mediator of phosphate homeostasis and its most notable effect is the promotion of phosphate excretion. FGF-23 was discovered to be involved in diseases such as autosomal dominant hypophosphatemic rickets, X-linked hypophosphatemia, and tumour-induced osteomalacia in which phosphate wasting was coupled to inappropriately low levels of 1,25(OH)2D3. FGF-23 is regulated by dietary phosphate in humans. In particular, it was found that phosphate restriction decreased FGF-23, and phosphate loading increased FGF-23. In agriculture, phosphate refers to one of the three primary plant nutrients, and it is a component of fertilizers. In ecological terms, because of its important role in biological systems, phosphate is a highly sought after resource. Consequently, it is often a limiting reagent in environments, and its availability may govern the rate of growth of organisms. Addition of high levels of phosphate to environments and to micro-environments in which it is typically rare can have significant ecological consequences. In the context of pollution, phosphates are a principal component of total dissolved solids, a major indicator of water quality. Dihydrogen phosphate is an inorganic sal... Found in fruit juices. It is used in foods as an acidulant for drinks and candies, pH control agent, buffering agent, flavour enhancer, flavouring agent, sequestrant, stabiliser and thickener, and synergist D001697 - Biomedical and Dental Materials > D003764 - Dental Materials

Nadide

[C21H28N7O14P2]+ (664.1169428000001)

[Spectral] NAD+ (exact mass = 663.10912) and 3,4-Dihydroxy-L-phenylalanine (exact mass = 197.06881) and Cytidine (exact mass = 243.08552) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. [Spectral] NAD+ (exact mass = 663.10912) and NADP+ (exact mass = 743.07545) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. COVID info from COVID-19 Disease Map Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS

1,4-Dihydronicotinamide adenine dinucleotide

C21H29N7O14P2 (665.1247674)

Nicotinamide adenine dinucleotide (NAD) is a coenzyme central to metabolism. Found in all living cells, NAD is called a dinucleotide because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine nucleobase and the other nicotinamide. NAD exists in two forms: an oxidized and reduced form, abbreviated as NAD+ and NADH (H for hydrogen) respectively. NADH is the reduced form of NAD+, and NAD+ is the oxidized form of NADH. NAD (or nicotinamide adenine dinucleotide) is used extensively in glycolysis and the citric acid cycle of cellular respiration. The reducing potential stored in NADH can be either converted into ATP through the electron transport chain or used for anabolic metabolism. ATP "energy" is necessary for an organism to live. Green plants obtain ATP through photosynthesis, while other organisms obtain it via cellular respiration. NAD is a coenzyme composed of ribosylnicotinamide 5-diphosphate coupled to adenosine 5-phosphate by a pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). NADP is formed through the addition of a phosphate group to the 2 position of the adenosyl nucleotide through an ester linkage. NADH is the reduced form of NAD+, and NAD+ is the oxidized form of NADH, A coenzyme composed of ribosylnicotinamide 5-diphosphate coupled to adenosine 5-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). It forms NADP with the addition of a phosphate group to the 2 position of the adenosyl nucleotide through an ester linkage.(Dorland, 27th ed) [HMDB]. NADH is found in many foods, some of which are dill, ohelo berry, fox grape, and black-eyed pea. Acquisition and generation of the data is financially supported in part by CREST/JST. COVID info from COVID-19 Disease Map Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS

Water

H2O (18.0105642)

Water is a chemical substance that is essential to all known forms of life. It appears colorless to the naked eye in small quantities, though it is actually slightly blue in color. It covers 71\\% of Earths surface. Current estimates suggest that there are 1.4 billion cubic kilometers (330 million m3) of it available on Earth, and it exists in many forms. It appears mostly in the oceans (saltwater) and polar ice caps, but it is also present as clouds, rain water, rivers, freshwater aquifers, lakes, and sea ice. Water in these bodies perpetually moves through a cycle of evaporation, precipitation, and runoff to the sea. Clean water is essential to human life. In many parts of the world, it is in short supply. From a biological standpoint, water has many distinct properties that are critical for the proliferation of life that set it apart from other substances. It carries out this role by allowing organic compounds to react in ways that ultimately allow replication. All known forms of life depend on water. Water is vital both as a solvent in which many of the bodys solutes dissolve and as an essential part of many metabolic processes within the body. Metabolism is the sum total of anabolism and catabolism. In anabolism, water is removed from molecules (through energy requiring enzymatic chemical reactions) in order to grow larger molecules (e.g. starches, triglycerides and proteins for storage of fuels and information). In catabolism, water is used to break bonds in order to generate smaller molecules (e.g. glucose, fatty acids and amino acids to be used for fuels for energy use or other purposes). Water is thus essential and central to these metabolic processes. Water is also central to photosynthesis and respiration. Photosynthetic cells use the suns energy to split off waters hydrogen from oxygen. Hydrogen is combined with CO2 (absorbed from air or water) to form glucose and release oxygen. All living cells use such fuels and oxidize the hydrogen and carbon to capture the suns energy and reform water and CO2 in the process (cellular respiration). Water is also central to acid-base neutrality and enzyme function. An acid, a hydrogen ion (H+, that is, a proton) donor, can be neutralized by a base, a proton acceptor such as hydroxide ion (OH-) to form water. Water is considered to be neutral, with a pH (the negative log of the hydrogen ion concentration) of 7. Acids have pH values less than 7 while bases have values greater than 7. Stomach acid (HCl) is useful to digestion. However, its corrosive effect on the esophagus during reflux can temporarily be neutralized by ingestion of a base such as aluminum hydroxide to produce the neutral molecules water and the salt aluminum chloride. Human biochemistry that involves enzymes usually performs optimally around a biologically neutral pH of 7.4. (Wikipedia). Water, also known as purified water or dihydrogen oxide, is a member of the class of compounds known as homogeneous other non-metal compounds. Homogeneous other non-metal compounds are inorganic non-metallic compounds in which the largest atom belongs to the class of other nonmetals. Water can be found in a number of food items such as caraway, oxheart cabbage, alaska wild rhubarb, and japanese walnut, which makes water a potential biomarker for the consumption of these food products. Water can be found primarily in most biofluids, including ascites Fluid, blood, cerebrospinal fluid (CSF), and lymph, as well as throughout all human tissues. Water exists in all living species, ranging from bacteria to humans. In humans, water is involved in several metabolic pathways, some of which include cardiolipin biosynthesis CL(20:4(5Z,8Z,11Z,14Z)/18:0/20:4(5Z,8Z,11Z,14Z)/18:2(9Z,12Z)), cardiolipin biosynthesis cl(i-13:0/i-15:0/i-20:0/i-24:0), cardiolipin biosynthesis CL(18:0/18:0/20:4(5Z,8Z,11Z,14Z)/22:5(7Z,10Z,13Z,16Z,19Z)), and cardiolipin biosynthesis cl(a-13:0/i-18:0/i-13:0/i-19:0). Water is also involved in several metabolic disorders, some of which include de novo triacylglycerol biosynthesis tg(i-21:0/i-13:0/21:0), de novo triacylglycerol biosynthesis tg(22:0/20:0/i-20:0), de novo triacylglycerol biosynthesis tg(a-21:0/i-20:0/i-14:0), and de novo triacylglycerol biosynthesis tg(i-21:0/a-17:0/i-12:0). Water is a drug which is used for diluting or dissolving drugs for intravenous, intramuscular or subcutaneous injection, according to instructions of the manufacturer of the drug to be administered [fda label]. Water plays an important role in the world economy. Approximately 70\\% of the freshwater used by humans goes to agriculture. Fishing in salt and fresh water bodies is a major source of food for many parts of the world. Much of long-distance trade of commodities (such as oil and natural gas) and manufactured products is transported by boats through seas, rivers, lakes, and canals. Large quantities of water, ice, and steam are used for cooling and heating, in industry and homes. Water is an excellent solvent for a wide variety of chemical substances; as such it is widely used in industrial processes, and in cooking and washing. Water is also central to many sports and other forms of entertainment, such as swimming, pleasure boating, boat racing, surfing, sport fishing, and diving .

Oxygen

O2 (31.98983)

Oxygen is the third most abundant element in the universe after hydrogen and helium and the most abundant element by mass in the Earths crust. Diatomic oxygen gas constitutes 20.9\\% of the volume of air. All major classes of structural molecules in living organisms, such as proteins, carbohydrates, and fats, contain oxygen, as do the major inorganic compounds that comprise animal shells, teeth, and bone. Oxygen in the form of O2 is produced from water by cyanobacteria, algae and plants during photosynthesis and is used in cellular respiration for all living organisms. Green algae and cyanobacteria in marine environments provide about 70\\% of the free oxygen produced on earth and the rest is produced by terrestrial plants. Oxygen is used in mitochondria to help generate adenosine triphosphate (ATP) during oxidative phosphorylation. For animals, a constant supply of oxygen is indispensable for cardiac viability and function. To meet this demand, an adult human, at rest, inhales 1.8 to 2.4 grams of oxygen per minute. This amounts to more than 6 billion tonnes of oxygen inhaled by humanity per year. At a resting pulse rate, the heart consumes approximately 8-15 ml O2/min/100 g tissue. This is significantly more than that consumed by the brain (approximately 3 ml O2/min/100 g tissue) and can increase to more than 70 ml O2/min/100 g myocardial tissue during vigorous exercise. As a general rule, mammalian heart muscle cannot produce enough energy under anaerobic conditions to maintain essential cellular processes; thus, a constant supply of oxygen is indispensable to sustain cardiac function and viability. However, the role of oxygen and oxygen-associated processes in living systems is complex, and they and can be either beneficial or contribute to cardiac dysfunction and death (through reactive oxygen species). Reactive oxygen species (ROS) are a family of oxygen-derived free radicals that are produced in mammalian cells under normal and pathologic conditions. Many ROS, such as the superoxide anion (O2-)and hydrogen peroxide (H2O2), act within blood vessels, altering mechanisms mediating mechanical signal transduction and autoregulation of cerebral blood flow. Reactive oxygen species are believed to be involved in cellular signaling in blood vessels in both normal and pathologic states. The major pathway for the production of ROS is by way of the one-electron reduction of molecular oxygen to form an oxygen radical, the superoxide anion (O2-). Within the vasculature there are several enzymatic sources of O2-, including xanthine oxidase, the mitochondrial electron transport chain, and nitric oxide (NO) synthases. Studies in recent years, however, suggest that the major contributor to O2- levels in vascular cells is the membrane-bound enzyme NADPH-oxidase. Produced O2- can react with other radicals, such as NO, or spontaneously dismutate to produce hydrogen peroxide (H2O2). In cells, the latter reaction is an important pathway for normal O2- breakdown and is usually catalyzed by the enzyme superoxide dismutase (SOD). Once formed, H2O2 can undergo various reactions, both enzymatic and nonenzymatic. The antioxidant enzymes catalase and glutathione peroxidase act to limit ROS accumulation within cells by breaking down H2O2 to H2O. Metabolism of H2O2 can also produce other, more damaging ROS. For example, the endogenous enzyme myeloperoxidase uses H2O2 as a substrate to form the highly reactive compound hypochlorous acid. Alternatively, H2O2 can undergo Fenton or Haber-Weiss chemistry, reacting with Fe2+/Fe3+ ions to form toxic hydroxyl radicals (-.OH). (PMID: 17027622, 15765131) [HMDB]. Oxygen is found in many foods, some of which are soy bean, watermelon, sweet basil, and spinach. Oxygen is the third most abundant element in the universe after hydrogen and helium and the most abundant element by mass in the Earths crust. Diatomic oxygen gas constitutes 20.9\\% of the volume of air. All major classes of structural molecules in living organisms, such as proteins, carbohydrates, and fats, contain oxygen, as do the major inorganic compounds that comprise animal shells, teeth, and bone. Oxygen in the form of O2 is produced from water by cyanobacteria, algae and plants during photosynthesis and is used in cellular respiration for all living organisms. Green algae and cyanobacteria in marine environments provide about 70\\% of the free oxygen produced on earth and the rest is produced by terrestrial plants. Oxygen is used in mitochondria to help generate adenosine triphosphate (ATP) during oxidative phosphorylation. For animals, a constant supply of oxygen is indispensable for cardiac viability and function. To meet this demand, an adult human, at rest, inhales 1.8 to 2.4 grams of oxygen per minute. This amounts to more than 6 billion tonnes of oxygen inhaled by humanity per year. At a resting pulse rate, the heart consumes approximately 8-15 ml O2/min/100 g tissue. This is significantly more than that consumed by the brain (approximately 3 ml O2/min/100 g tissue) and can increase to more than 70 ml O2/min/100 g myocardial tissue during vigorous exercise. As a general rule, mammalian heart muscle cannot produce enough energy under anaerobic conditions to maintain essential cellular processes; thus, a constant supply of oxygen is indispensable to sustain cardiac function and viability. However, the role of oxygen and oxygen-associated processes in living systems is complex, and they and can be either beneficial or contribute to cardiac dysfunction and death (through reactive oxygen species). Reactive oxygen species (ROS) are a family of oxygen-derived free radicals that are produced in mammalian cells under normal and pathologic conditions. Many ROS, such as the superoxide anion (O2-)and hydrogen peroxide (H2O2), act within blood vessels, altering mechanisms mediating mechanical signal transduction and autoregulation of cerebral blood flow. Reactive oxygen species are believed to be involved in cellular signaling in blood vessels in both normal and pathologic states. The major pathway for the production of ROS is by way of the one-electron reduction of molecular oxygen to form an oxygen radical, the superoxide anion (O2-). Within the vasculature there are several enzymatic sources of O2-, including xanthine oxidase, the mitochondrial electron transport chain, and nitric oxide (NO) synthases. Studies in recent years, however, suggest that the major contributor to O2- levels in vascular cells is the membrane-bound enzyme NADPH-oxidase. Produced O2- can react with other radicals, such as NO, or spontaneously dismutate to produce hydrogen peroxide (H2O2). In cells, the latter reaction is an important pathway for normal O2- breakdown and is usually catalyzed by the enzyme superoxide dismutase (SOD). Once formed, H2O2 can undergo various reactions, both enzymatic and nonenzymatic. The antioxidant enzymes catalase and glutathione peroxidase act to limit ROS accumulation within cells by breaking down H2O2 to H2O. Metabolism of H2O2 can also produce other, more damaging ROS. For example, the endogenous enzyme myeloperoxidase uses H2O2 as a substrate to form the highly reactive compound hypochlorous acid. Alternatively, H2O2 can undergo Fenton or Haber-Weiss chemistry, reacting with Fe2+/Fe3+ ions to form toxic hydroxyl radicals (-.OH). (PMID: 17027622, 15765131). V - Various > V03 - All other therapeutic products > V03A - All other therapeutic products > V03AN - Medical gases

Carbon dioxide

CO2 (43.98983)

Carbon dioxide is a colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals. Carbon dioxide is produced during respiration by all animals, fungi and microorganisms that depend on living and decaying plants for food, either directly or indirectly. It is, therefore, a major component of the carbon cycle. Additionally, carbon dioxide is used by plants during photosynthesis to make sugars which may either be consumed again in respiration or used as the raw material to produce polysaccharides such as starch and cellulose, proteins and the wide variety of other organic compounds required for plant growth and development. When inhaled at concentrations much higher than usual atmospheric levels, it can produce a sour taste in the mouth and a stinging sensation in the nose and throat. These effects result from the gas dissolving in the mucous membranes and saliva, forming a weak solution of carbonic acid. Carbon dioxide is used by the food industry, the oil industry, and the chemical industry. Carbon dioxide is used to produce carbonated soft drinks and soda water. Traditionally, the carbonation in beer and sparkling wine comes about through natural fermentation, but some manufacturers carbonate these drinks artificially. Leavening agent, propellant, aerating agent, preservative. Solvent for supercritical extraction e.g. of caffeine in manufacture of caffeine-free instant coffee. It is used in carbonation of beverages, in the frozen food industry and as a component of controlled atmosphere packaging (CAD) to inhibit bacterial growth. Especies effective against Gram-negative spoilage bacteria, e.g. Pseudomonas V - Various > V03 - All other therapeutic products > V03A - All other therapeutic products > V03AN - Medical gases

Pyrophosphate

H4O7P2 (177.9432294)

The anion, the salts, and the esters of pyrophosphoric acid are called pyrophosphates. The pyrophosphate anion is abbreviated PPi and is formed by the hydrolysis of ATP into AMP in cells. This hydrolysis is called pyrophosphorolysis. The pyrophosphate anion has the structure P2O74-, and is an acid anhydride of phosphate. It is unstable in aqueous solution and rapidly hydrolyzes into inorganic phosphate. Pyrophosphate is an osteotoxin (arrests bone development) and an arthritogen (promotes arthritis). It is also a metabotoxin (an endogenously produced metabolite that causes adverse health affects at chronically high levels). Chronically high levels of pyrophosphate are associated with hypophosphatasia. Hypophosphatasia (also called deficiency of alkaline phosphatase or phosphoethanolaminuria) is a rare, and sometimes fatal, metabolic bone disease. Hypophosphatasia is associated with a molecular defect in the gene encoding tissue non-specific alkaline phosphatase (TNSALP). TNSALP is an enzyme that is tethered to the outer surface of osteoblasts and chondrocytes. TNSALP hydrolyzes several substances, including inorganic pyrophosphate (PPi) and pyridoxal 5-phosphate (PLP), a major form of vitamin B6. When TSNALP is low, inorganic pyrophosphate (PPi) accumulates outside of cells and inhibits the formation of hydroxyapatite, one of the main components of bone, causing rickets in infants and children and osteomalacia (soft bones) in adults. Vitamin B6 must be dephosphorylated by TNSALP before it can cross the cell membrane. Vitamin B6 deficiency in the brain impairs synthesis of neurotransmitters which can cause seizures. In some cases, a build-up of calcium pyrophosphate dihydrate crystals in the joints can cause pseudogout. COVID info from WikiPathways Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS

ammonia

H3N (17.0265478)

An azane that consists of a single nitrogen atom covelently bonded to three hydrogen atoms. Ammonia, also known as nh3 or ammonia solution, is a member of the class of compounds known as homogeneous other non-metal compounds. Homogeneous other non-metal compounds are inorganic non-metallic compounds in which the largest atom belongs to the class of other nonmetals. Ammonia can be found in a number of food items such as rose hip, yardlong bean, cereals and cereal products, and ceylon cinnamon, which makes ammonia a potential biomarker for the consumption of these food products. Ammonia can be found primarily in blood, cellular cytoplasm, cerebrospinal fluid (CSF), and urine, as well as throughout all human tissues. Ammonia exists in all eukaryotes, ranging from yeast to humans. In humans, ammonia is involved in several metabolic pathways, some of which include glucose-alanine cycle, phenylalanine and tyrosine metabolism, homocysteine degradation, and d-arginine and d-ornithine metabolism. Ammonia is also involved in several metabolic disorders, some of which include ureidopropionase deficiency, hyperornithinemia-hyperammonemia-homocitrullinuria [hhh-syndrome], non ketotic hyperglycinemia, and beta-mercaptolactate-cysteine disulfiduria. Moreover, ammonia is found to be associated with 3-Hydroxy-3-methylglutaryl-CoA lyase deficiency, 3-Methyl-crotonyl-glycinuria, citrullinemia type I, and short bowel syndrome. Ammonia is a non-carcinogenic (not listed by IARC) potentially toxic compound. Ammonia or azane is a compound of nitrogen and hydrogen with the formula NH3. The simplest pnictogen hydride, ammonia is a colourless gas with a characteristic pungent smell. It is a common nitrogenous waste, particularly among aquatic organisms, and it contributes significantly to the nutritional needs of terrestrial organisms by serving as a precursor to food and fertilizers. Ammonia, either directly or indirectly, is also a building block for the synthesis of many pharmaceutical products and is used in many commercial cleaning products . Acute Exposure: EYES: irrigate opened eyes for several minutes under running water. INGESTION: do not induce vomiting. Rinse mouth with water (never give anything by mouth to an unconscious person). Seek immediate medical advice. SKIN: should be treated immediately by rinsing the affected parts in cold running water for at least 15 minutes, followed by thorough washing with soap and water. If necessary, the person should shower and change contaminated clothing and shoes, and then must seek medical attention. INHALATION: supply fresh air. If required provide artificial respiration. (z)-n-coumaroyl-5-hydroxyanthranilic acid is a member of the class of compounds known as avenanthramides. Avenanthramides are a group of phenolic alkaloids consisting of conjugate of three phenylpropanoids (ferulic, caffeic, or p-coumaric acid) and anthranilic acid (z)-n-coumaroyl-5-hydroxyanthranilic acid is practically insoluble (in water) and a weakly acidic compound (based on its pKa). (z)-n-coumaroyl-5-hydroxyanthranilic acid can be found in cereals and cereal products and oat, which makes (z)-n-coumaroyl-5-hydroxyanthranilic acid a potential biomarker for the consumption of these food products.

Hydrogen sulfide

H2S (33.9877212)

Hydrogen sulfide, also known as h2s or acide sulfhydrique, is a member of the class of compounds known as other non-metal sulfides. Other non-metal sulfides are inorganic compounds containing a sulfur atom of an oxidation state of -2, in which the heaviest atom bonded to the oxygen belongs to the class of other non-metals. Hydrogen sulfide can be found in a number of food items such as small-leaf linden, agar, devilfish, and nutmeg, which makes hydrogen sulfide a potential biomarker for the consumption of these food products. Hydrogen sulfide can be found primarily in blood and feces, as well as throughout most human tissues. Hydrogen sulfide exists in all living species, ranging from bacteria to humans. In humans, hydrogen sulfide is involved in a couple of metabolic pathways, which include cysteine metabolism and cystinosis, ocular nonnephropathic. Hydrogen sulfide is also involved in beta-mercaptolactate-cysteine disulfiduria, which is a metabolic disorder. Moreover, hydrogen sulfide is found to be associated with hydrogen sulfide poisoning. Hydrogen sulfide is a non-carcinogenic (not listed by IARC) potentially toxic compound. Hydrogen sulfide often results from the microbial breakdown of organic matter in the absence of oxygen gas, such as in swamps and sewers; this process is commonly known as anaerobic digestion. H 2S also occurs in volcanic gases, natural gas, and in some sources of well water. The human body produces small amounts of H 2S and uses it as a signaling molecule . Treatment involves immediate inhalation of amyl nitrite, injections of sodium nitrite, inhalation of pure oxygen, administration of bronchodilators to overcome eventual bronchospasm, and in some cases hyperbaric oxygen therapy (HBO). HBO therapy has anecdotal support and remains controversial (L1139) (T3DB). Hydrogen sulfide is a highly toxic and flammable gas. Because it is heavier than air it tends to accumulate at the bottom of poorly ventilated spaces. Although very pungent at first, it quickly deadens the sense of smell, so potential victims may be unaware of its presence until it is too late. H2S arises from virtually anywhere where elemental sulfur comes into contact with organic material, especially at high temperatures. Hydrogen sulfide is a covalent hydride chemically related to water (H2O) since oxygen and sulfur occur in the same periodic table group. It often results when bacteria break down organic matter in the absence of oxygen, such as in swamps, and sewers (alongside the process of anaerobic digestion). It also occurs in volcanic gases, natural gas and some well waters. It is also important to note that Hydrogen sulfide is a central participant in the sulfur cycle, the biogeochemical cycle of sulfur on Earth. As mentioned above, sulfur-reducing and sulfate-reducing bacteria derive energy from oxidizing hydrogen or organic molecules in the absence of oxygen by reducing sulfur or sulfate to hydrogen sulfide. Other bacteria liberate hydrogen sulfide from sulfur-containing amino acids. Several groups of bacteria can use hydrogen sulfide as fuel, oxidizing it to elemental sulfur or to sulfate by using oxygen or nitrate as oxidant. The purple sulfur bacteria and the green sulfur bacteria use hydrogen sulfide as electron donor in photosynthesis, thereby producing elemental sulfur. (In fact, this mode of photosynthesis is older than the mode of cyanobacteria, algae and plants which uses water as electron donor and liberates oxygen). Hydrogen sulfide can be found in Alcaligenes, Chromobacteriumn, Klebsiella, Proteus and Pseudomonas (PMID: 13061742). D018377 - Neurotransmitter Agents > D064426 - Gasotransmitters D004785 - Environmental Pollutants > D000393 - Air Pollutants

Tetrahydrofolic acid

C19H23N7O6 (445.1709738)

Tetrahydrofolate is a soluble coenzyme (vitamin B9) that is synthesized de novo by plants and microorganisms, and absorbed from the diet by animals. It is composed of three distinct parts: a pterin ring, a p-ABA (p-aminobenzoic acid) and a polyglutamate chain with a number of residues varying between 1 and 8. Only the tetra-reduced form of the molecule serves as a coenzyme for C1 transfer reactions. In biological systems, the C1-units exist under various oxidation states and the different tetrahydrofolate derivatives constitute a family of related molecules named indistinctly under the generic term folate. (PMID 16042593). Folate is important for cells and tissues that rapidly divide. Cancer cells divide rapidly, and drugs that interfere with folate metabolism are used to treat cancer. Methotrexate is a drug often used to treat cancer because it inhibits the production of the active form, tetrahydrofolate. Unfortunately, methotrexate can be toxic, producing side effects such as inflammation in the digestive tract that make it difficult to eat normally. -- Wikipedia; Signs of folic acid deficiency are often subtle. Diarrhea, loss of appetite, and weight loss can occur. Additional signs are weakness, sore tongue, headaches, heart palpitations, irritability, and behavioral disorders. Women with folate deficiency who become pregnant are more likely to give birth to low birth weight and premature infants, and infants with neural tube defects. In adults, anemia is a sign of advanced folate deficiency. In infants and children, folate deficiency can slow growth rate. Some of these symptoms can also result from a variety of medical conditions other than folate deficiency. It is important to have a physician evaluate these symptoms so that appropriate medical care can be given. -- Wikipedia; Folinic acid is a form of folate that can help rescue or reverse the toxic effects of methotrexate. Folinic acid is not the same as folic acid. Folic acid supplements have little established role in cancer chemotherapy. There have been cases of severe adverse effects of accidental substitution of folic acid for folinic acid in patients receiving methotrexate cancer chemotherapy. It is important for anyone receiving methotrexate to follow medical advice on the use of folic or folinic acid supplements. -- Wikipedia. Low concentrations of folate, vitamin B12, or vitamin B6 may increase the level of homocysteine, an amino acid normally found in blood. There is evidence that an elevated homocysteine level is an independent risk factor for heart disease and stroke. The evidence suggests that high levels of homocysteine may damage coronary arteries or make it easier for blood clotting cells called platelets to clump together and form a clot. However, there is currently no evidence available to suggest that lowering homocysteine with vitamins will reduce your risk of heart disease. Clinical intervention trials are needed to determine whether supplementation with folic acid, vitamin B12 or vitamin B6 can lower your risk of developing coronary heart disease. -- Wikipedia. Tetrahydrofolate is a soluble coenzyme (vitamin B9) that is synthesized de novo by plants and microorganisms, and absorbed from the diet by animals. It is composed of three distinct parts: a pterin ring, a p-ABA (p-aminobenzoic acid) and a polyglutamate chain with a number of residues varying between 1 and 8. Only the tetra-reduced form of the molecule serves as a coenzyme for C1 transfer reactions. In biological systems, the C1-units exist under various oxidation states and the different tetrahydrofolate derivatives constitute a family of related molecules named indistinctly under the generic term folate. (PMID 16042593)

3-Mercaptopyruvic acid

C3H4O3S (119.9881154)

3-Mercaptopyruvic acid, also known as 3-mercapto-2-oxopropanoate or beta-thiopyruvate, belongs to the class of organic compounds known as alpha-keto acids and derivatives. These are organic compounds containing an aldehyde substituted with a keto group on the adjacent carbon. 3-Mercaptopyruvic acid is an intermediate in cysteine metabolism. 3-Mercaptopyruvic acid exists in all living organisms, ranging from bacteria to humans. Within humans, 3-mercaptopyruvic acid participates in a number of enzymatic reactions. In particular, 3-mercaptopyruvic acid and cyanide can be converted into pyruvic acid and thiocyanate; which is mediated by the enzyme 3-mercaptopyruvate sulfurtransferase. In addition, 3-mercaptopyruvic acid can be biosynthesized from 3-mercaptolactic acid; which is mediated by the enzyme L-lactate dehydrogenase. It has been studied as a potential treatment for cyanide poisoning, but its half-life is too short for it to be clinically effective. In humans, 3-mercaptopyruvic acid is involved in cystinosis, ocular nonnephropathic. Outside of the human body, 3-mercaptopyruvic acid has been detected, but not quantified in several different foods, such as lima beans, spinachs, shallots, mexican groundcherries, and white lupines. This could make 3-mercaptopyruvic acid a potential biomarker for the consumption of these foods. 3-mercaptopyruvic acid, also known as beta-mercaptopyruvate or beta-thiopyruvic acid, belongs to alpha-keto acids and derivatives class of compounds. Those are organic compounds containing an aldehyde substituted with a keto group on the adjacent carbon. 3-mercaptopyruvic acid is slightly soluble (in water) and a moderately acidic compound (based on its pKa). 3-mercaptopyruvic acid can be found in a number of food items such as garland chrysanthemum, rubus (blackberry, raspberry), tarragon, and arrowhead, which makes 3-mercaptopyruvic acid a potential biomarker for the consumption of these food products. 3-mercaptopyruvic acid exists in all living organisms, ranging from bacteria to humans. In humans, 3-mercaptopyruvic acid is involved in a couple of metabolic pathways, which include cysteine metabolism and cystinosis, ocular nonnephropathic. 3-mercaptopyruvic acid is also involved in beta-mercaptolactate-cysteine disulfiduria, which is a metabolic disorder. 3-Mercaptopyruvic acid is an intermediate in cysteine metabolism. It has been studied as a potential treatment for cyanide poisoning, but its half-life is too short for it to be clinically effective. Instead, prodrugs, such as sulfanegen, are being evaluated to compensate for the short half-life of 3-mercaptopyruvic acid .

Hydrogen cyanide

CHN (27.010898599999997)

Hydrogen cyanide (with the historical common name of Prussic acid) is a chemical compound with chemical formula HCN. It is a colorless, extremely poisonous liquid that boils slightly above room temperature at 26 °C (79 °F). Hydrogen cyanide is a linear molecule, with a triple bond between carbon and nitrogen. A minor tautomer of HCN is HNC, hydrogen isocyanide. Hydrogen cyanide is weakly acidic with a pKa of 9.2. It partly ionizes in water solution to give the cyanide anion, CN. (Wikipedia) D009676 - Noxae > D011042 - Poisons > D002619 - Chemical Warfare Agents

Thiocyanate

CHNS (58.9829706)

Choloyl-CoA

C45H74N7O20P3S (1157.3921994000002)

Choloyl-CoA is an intermediate metabolite in the Bile acid biosynthesis (KEGG). The conjugation of bile acids to glycine and taurine for excretion into bile occurs via a reaction catalyzed by the enzyme Bile acid-CoA:amino acid N-acyltransferase (BACAT) catalyzes. Choloyl-CoA is an intermediate metabolite in the Bile acid biosynthesis (KEGG) D005765 - Gastrointestinal Agents > D001647 - Bile Acids and Salts D005765 - Gastrointestinal Agents > D002793 - Cholic Acids

Thiocysteine

C3H7NO2S2 (152.9918202)

The reactive species in the phosphofructokinase modulation system could be considered thiocysteine (R-S-S-) or cystine trisulfide (R-S-S-S-R) produced from cystine in the presence of gamma-Cystathionase (CST, EC 4.4.1.1). The desulfuration reaction of cystine in vivo produces thiocysteine containing a bound sulfur atom. Persulfide generated from L-cysteine inactivates tyrosine aminotransferase. Thiocysteine is the reactive (unstable) intermediate of thiocystine which functions as a persulfide in transferring its sulfane sulfur to thiophilic acceptors. Thiocystine conversion to unstable thiocysteine is accelerated by sulfhydryl compounds, or reagents that cleave sulfur-sulfur bonds to yield sulfhydryl groups. Thiocystine is proposed as the storage form of sulfane sulfur in biological systems. Liver cytosols contain factors that produce an inhibitor of tyrosine aminotransferase in 3 steps: initial oxidation of cysteine to form cystine; desulfurization of cystine catalyzed by cystathionase to form the persulfide, thiocysteine; and reaction of thiocysteine (or products of its decomposition) with proteins to form protein-bound sulfane. (PMID: 2903161, 454618, 7287665) [HMDB] The reactive species in the phosphofructokinase modulation system could be considered thiocysteine (R-S-S-) or cystine trisulfide (R-S-S-S-R) produced from cystine in the presence of gamma-Cystathionase (CST, EC 4.4.1.1). The desulfuration reaction of cystine in vivo produces thiocysteine containing a bound sulfur atom. Persulfide generated from L-cysteine inactivates tyrosine aminotransferase. Thiocysteine is the reactive (unstable) intermediate of thiocystine which functions as a persulfide in transferring its sulfane sulfur to thiophilic acceptors. Thiocystine conversion to unstable thiocysteine is accelerated by sulfhydryl compounds, or reagents that cleave sulfur-sulfur bonds to yield sulfhydryl groups. Thiocystine is proposed as the storage form of sulfane sulfur in biological systems. Liver cytosols contain factors that produce an inhibitor of tyrosine aminotransferase in 3 steps: initial oxidation of cysteine to form cystine; desulfurization of cystine catalyzed by cystathionase to form the persulfide, thiocysteine; and reaction of thiocysteine (or products of its decomposition) with proteins to form protein-bound sulfane. (PMID: 2903161, 454618, 7287665).

3-Sulfinylpyruvic acid

C3H4O5S (151.9779454)

3-Sulfinylpyruvic acid is a compound found in the mammalian cysteine metabolic pathway. It is the deaminated form of cysteine sulfinic acid which subsequently spontaneously reacts to form pyruvate and release sulfur dioxide (PMID: 3925121, 6822523). It is the byproduct of oxidoreductases (EC 1.4.1.-), and aspartate transaminase (EC 2.6.1.1). It is also often associated with hepatic disease, and the presence of aspartate transaminase is used in diagnostic biochemical assays of such ailments (PMID: 17310554). b-Sulfinyl pyruvate is a putative product. It decomposes to puruvate and SO2 spontaneously. (PMID: 6822523) [HMDB]

3-Sulfopyruvic acid

C3H4O6S (167.9728604)

Sulfopyruvate, also known as 2-carboxy-2-oxoethanesulfonic acid or beta-sulfopyruvic acid, belongs to alpha-keto acids and derivatives class of compounds. Those are organic compounds containing an aldehyde substituted with a keto group on the adjacent carbon. Sulfopyruvate is soluble (in water) and an extremely strong acidic compound (based on its pKa). Sulfopyruvate can be found in a number of food items such as french plantain, sago palm, sweet cherry, and ostrich fern, which makes sulfopyruvate a potential biomarker for the consumption of these food products. Sulfopyruvate exists in all living organisms, ranging from bacteria to humans. 3-Sulfopyruvic acid is the product of the transamination of cysteinesulfonate in a reaction catalyzed by aspartate aminotransferase. 3-sulfopyruvic acid is stable and is reduced by malate dehydrogenase to beta-sulfolactate, which is excreted in the urine. Cysteinesulfonate, 3-sulfopyruvic acid, and beta-sulfolactate are reversibly interconverted in vivo. (PMID: 3346220).

3-Mercaptolactic acid

C3H6O3S (122.0037646)

3-Mercaptolactic acid is a thiol that has been confirmed to be found in urine (PMID 8852041). [HMDB] 3-Mercaptolactic acid is a thiol that has been confirmed to be found in urine (PMID 8852041).