Reaction Process: PathBank:SMP0002307

Pantothenic acid

C9H17NO5 (219.11066720000002)

(R)-pantothenic acid is a pantothenic acid having R-configuration. It has a role as an antidote to curare poisoning, a human blood serum metabolite and a geroprotector. It is a vitamin B5 and a pantothenic acid. It is a conjugate acid of a (R)-pantothenate. Pantothenic acid, also called pantothenate or vitamin B5 (a B vitamin), is a water-soluble vitamin discovered by Roger J. Williams in 1919. For many animals, pantothenic acid is an essential nutrient as it is required to synthesize coenzyme-A (CoA), as well as to synthesize and metabolize proteins, carbohydrates, and fats. Pantothenic acid is the amide between pantoic acid and β-alanine and commonly found as its alcohol analog, the provitamin panthenol, and as calcium pantothenate. Small quantities of pantothenic acid are found in nearly every food, with high amounts in whole-grain cereals, legumes, eggs, meat, royal jelly, avocado, and yogurt. Pantothenic acid is an ingredient in some hair and skin care products. Only the dextrorotatory (D) isomer of pantothenic acid possesses biological activity. while the levorotatory (L) form may antagonize the effects of the dextrorotatory isomer. Pantothenic acid is a metabolite found in or produced by Escherichia coli (strain K12, MG1655). Pantothenic acid is a natural product found in Chlamydomonas reinhardtii, Arabidopsis thaliana, and other organisms with data available. Pantothenic Acid is a water-soluble vitamin ubiquitously found in plants and animal tissues with antioxidant property. Vitamin B5 is a component of coenzyme A (CoA) and a part of the vitamin B2 complex. Vitamin B5 is a growth factor and is essential for various metabolic functions, including the metabolism of carbohydrates, proteins, and fatty acids. This vitamin is also involved in the synthesis of cholesterol, lipids, neurotransmitters, steroid hormones, and hemoglobin. (R)-Pantothenic acid is a metabolite found in or produced by Saccharomyces cerevisiae. A butyryl-beta-alanine that can also be viewed as pantoic acid complexed with BETA ALANINE. It is incorporated into COENZYME A and protects cells against peroxidative damage by increasing the level of GLUTATHIONE. See also: Broccoli (part of). Pantothenic acid, also called vitamin B5, is a water-soluble vitamin required to sustain life. Pantothenic acid is needed to form coenzyme-A (CoA), and is thus critical in the metabolism and synthesis of carbohydrates, proteins, and fats. Its name is derived from the Greek pantothen meaning "from everywhere" and small quantities of pantothenic acid are found in nearly every food, with high amounts in whole grain cereals, legumes, eggs, meat, and royal jelly. Pantothenic acid is classified as a member of the secondary alcohols. Secondary alcohols are compounds containing a secondary alcohol functional group, with the general structure HOC(R)(R) (R,R=alkyl, aryl). Pantothenic acid is considered to be soluble (in water) and acidic. (r)-pantothenate, also known as (+)-pantothenic acid or vitamin b5, is a member of the class of compounds known as secondary alcohols. Secondary alcohols are compounds containing a secondary alcohol functional group, with the general structure HOC(R)(R) (R,R=alkyl, aryl) (r)-pantothenate is soluble (in water) and a weakly acidic compound (based on its pKa). (r)-pantothenate can be found in a number of food items such as spirulina, nance, cereals and cereal products, and sparkleberry, which makes (r)-pantothenate a potential biomarker for the consumption of these food products (r)-pantothenate can be found primarily in blood and urine (r)-pantothenate exists in all eukaryotes, ranging from yeast to humans. D018977 - Micronutrients > D014815 - Vitamins A pantothenic acid having R-configuration. Acquisition and generation of the data is financially supported in part by CREST/JST. KEIO_ID P032; [MS2] KO009182 KEIO_ID P032; [MS3] KO009183 KEIO_ID P032 D-Pantothenic acid (Pantothenate) is an essential trace nutrient that functions as the obligate precursor of coenzyme A (CoA). D-Pantothenic acid plays key roles in myriad biological processes, including many that regulate carbohydrate, lipid, protein, and nucleic acid metabolism[1]. D-Pantothenic acid (Pantothenate) is an essential trace nutrient that functions as the obligate precursor of coenzyme A (CoA). D-Pantothenic acid plays key roles in myriad biological processes, including many that regulate carbohydrate, lipid, protein, and nucleic acid metabolism[1].

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).

Putrescine

C4H12N2 (88.1000432)

Putrescine is a four-carbon alkane-alpha,omega-diamine. It is obtained by the breakdown of amino acids and is responsible for the foul odour of putrefying flesh. It has a role as a fundamental metabolite and an antioxidant. It is a conjugate base of a 1,4-butanediammonium. Putrescine is a toxic diamine formed by putrefaction from the decarboxylation of arginine and ornithine. Putrescine is a solid. This compound belongs to the polyamines. These are compounds containing more than one amine group. Known drug targets of putrescine include putrescine-binding periplasmic protein, ornithine decarboxylase, and S-adenosylmethionine decarboxylase proenzyme. Putrescine is a metabolite found in or produced by Escherichia coli (strain K12, MG1655). 1,4-Diaminobutane is a natural product found in Eupatorium cannabinum, Populus tremula, and other organisms with data available. Putrescine is a four carbon diamine produced during tissue decomposition by the decarboxylation of amino acids. Polyamines, including putrescine, may act as growth factors that promote cell division; however, putrescine is toxic at high doses. Putrescine is a uremic toxin. Uremic toxins can be subdivided into three major groups based upon their chemical and physical characteristics: 1) small, water-soluble, non-protein-bound compounds, such as urea; 2) small, lipid-soluble and/or protein-bound compounds, such as the phenols and 3) larger so-called middle-molecules, such as beta2-microglobulin. Chronic exposure of uremic toxins can lead to a number of conditions including renal damage, chronic kidney disease and cardiovascular disease.Putrescine is a polyamine. Putrescine is related to cadaverine (another polyamine). Both are produced by the breakdown of amino acids in living and dead organisms and both are toxic in large doses. Putrescine and cadaverine are largely responsible for the foul odor of putrefying flesh, but also contribute to the odor of such processes as bad breath and bacterial vaginosis. Putrescine is also found in semen. Putrescine attacks s-adenosyl methionine and converts it to spermidine. Spermidine in turn attacks another s-adenosyl methionine and converts it to spermine. Putrescine is synthesized in small quantities by healthy living cells by the action of ornithine decarboxylase. The polyamines, of which putrescine is one of the simplest, appear to be growth factors necessary for cell division. Putrescine apparently has specific role in skin physiology and neuroprotection. Pharmacological interventions have demonstrated convincingly that a steady supply of polyamines is a prerequisite for cell proliferation to occur. Genetic engineering of polyamine metabolism in transgenic rodents has shown that polyamines play a role in spermatogenesis, skin physiology, promotion of tumorigenesis and organ hypertrophy as well as neuronal protection. Transgenic activation of polyamine catabolism not only profoundly disturbs polyamine homeostasis in most tissues, but also creates a complex phenotype affecting skin, female fertility, fat depots, pancreatic integrity and regenerative growth. Transgenic expression of ornithine decarboxylase antizyme has suggested that this unique protein may act as a general tumor suppressor. Homozygous deficiency of the key biosynthetic enzymes of the polyamines, ornithine and S-adenosylmethionine decarboxylase is not compatible with murine embryogenesis. (A3286, A3287). Putrescine is a metabolite found in or produced by Saccharomyces cerevisiae. A toxic diamine formed by putrefaction from the decarboxylation of arginine and ornithine. Putrescine is a polyamine. Putrescine is related to cadaverine (another polyamine). Both are produced by the breakdown of amino acids in living and dead organisms and both are toxic in large doses. Putrescine and cadaverine are largely responsible for the foul odor of putrefying flesh, but also contribute to the odor of such processes as bad breath and bacterial vaginosis. Putrescine has been identified as a uremic toxin according to the European Uremic Toxin Working Group (PMID:22626821). It is also found in semen. Putrescine attacks s-adenosyl methionine and converts it to spermidine. Spermidine in turn attacks another s-adenosyl methionine and converts it to spermine. Putrescine is synthesized in small quantities by healthy living cells by the action of ornithine decarboxylase. The polyamines, of which putrescine is one of the simplest, appear to be growth factors necessary for cell division. Putrescine apparently has specific role in skin physiology and neuroprotection. (PMID:15009201, 16364196). Pharmacological interventions have demonstrated convincingly that a steady supply of polyamines is a prerequisite for cell proliferation to occur. Genetic engineering of polyamine metabolism in transgenic rodents has shown that polyamines play a role in spermatogenesis, skin physiology, promotion of tumorigenesis and organ hypertrophy as well as neuronal protection. Transgenic activation of polyamine catabolism not only profoundly disturbs polyamine homeostasis in most tissues, but also creates a complex phenotype affecting skin, female fertility, fat depots, pancreatic integrity and regenerative growth. Transgenic expression of ornithine decarboxylase antizyme has suggested that this unique protein may act as a general tumor suppressor. Homozygous deficiency of the key biosynthetic enzymes of the polyamines, ornithine and S-adenosylmethionine decarboxylase is not compatible with murine embryogenesis. Putrescine can be found in Citrobacter, Corynebacterium, Cronobacter and Enterobacter (PMID:27872963) (https://onlinelibrary.wiley.com/doi/full/10.1111/1541-4337.12099). Putrescine is an organic chemical compound related to cadaverine; both are produced by the breakdown of amino acids in living and dead organisms and both are toxic in large doses. The two compounds are largely responsible for the foul odor of putrefying flesh, but also contribute to the odor of such processes as bad breath and bacterial vaginosis. They are also found in semen and some microalgae, together with related molecules like spermine and spermidine. A four-carbon alkane-alpha,omega-diamine. It is obtained by the breakdown of amino acids and is responsible for the foul odour of putrefying flesh. Acquisition and generation of the data is financially supported in part by CREST/JST. KEIO_ID B001

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-methylthioadenosine (MTA)

C11H15N5O3S (297.089556)

5-Methylthioadenosine, also known as MTA or thiomethyladenosine, belongs to the class of organic compounds known as 5-deoxy-5-thionucleosides. These are 5-deoxyribonucleosides in which the ribose is thio-substituted at the 5position by a S-alkyl group. 5-Methylthioadenosine is metabolized solely by MTA-phosphorylase, to yield 5-methylthioribose-1-phosphate and adenine, a crucial step in the methionine and purine salvage pathways, respectively. 5-Methylthioadenosine exists in all living species, ranging from bacteria to humans. 5-Methylthioadenosine (MTA) is a naturally occurring sulfur-containing nucleoside present in all mammalian tissues. Within humans, 5-methylthioadenosine participates in a number of enzymatic reactions. In particular, 5-methylthioadenosine and spermidine can be biosynthesized from S-adenosylmethioninamine and putrescine through the action of the enzyme spermidine synthase. In addition, 5-methylthioadenosine can be converted into 5-methylthioribose 1-phosphate and L-methionine; which is catalyzed by the enzyme S-methyl-5-thioadenosine phosphorylase. It is produced from S-adenosylmethionine mainly through the polyamine biosynthetic pathway, where it behaves as a powerful inhibitory product. For instance, 5-Methylthioadenosine has been shown to influence the regulation of gene expression, proliferation, differentiation, and apoptosis (PMID:15313459). In humans, 5-methylthioadenosine is involved in the metabolic disorder called hypermethioninemia. Outside of the human body, 5-Methylthioadenosine has been detected, but not quantified in several different foods, such as soursops, allspices, summer grapes, alaska wild rhubarbs, and breadfruits. Elevated excretion appears in children with severe combined immunodeficiency syndrome (SCID) (PMID:3987052). Evidence suggests that 5-Methylthioadenosine can affect cellular processes in many ways. 5-Methylthioadenosine can be found in human urine. 5-deoxy-5-methylthioadenosine, also known as S-methyl-5-thioadenosine or mta, 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. 5-deoxy-5-methylthioadenosine is slightly soluble (in water) and a very weakly acidic compound (based on its pKa). 5-deoxy-5-methylthioadenosine can be found in a number of food items such as allspice, sesame, roselle, and bayberry, which makes 5-deoxy-5-methylthioadenosine a potential biomarker for the consumption of these food products. 5-deoxy-5-methylthioadenosine can be found primarily in blood and urine, as well as in human fibroblasts, platelet and prostate tissues. 5-deoxy-5-methylthioadenosine exists in all living species, ranging from bacteria to humans. In humans, 5-deoxy-5-methylthioadenosine is involved in a couple of metabolic pathways, which include methionine metabolism and spermidine and spermine biosynthesis. 5-deoxy-5-methylthioadenosine is also involved in several metabolic disorders, some of which include glycine n-methyltransferase deficiency, methionine adenosyltransferase deficiency, homocystinuria-megaloblastic anemia due to defect in cobalamin metabolism, cblg complementation type, and hypermethioninemia. 5'-Methylthioadenosine (5'-(Methylthio)-5'-deoxyadenosine) is a nucleoside generated from S-adenosylmethionine (SAM) during polyamine synthesis[1]. 5'-Methylthioadenosine suppresses tumors by inhibiting tumor cell proliferation, invasion, and the induction of apoptosis while controlling the inflammatory micro-environments of tumor tissue. 5'-Methylthioadenosine and its associated materials have striking regulatory effects on tumorigenesis[2]. 5'-Methylthioadenosine (5'-(Methylthio)-5'-deoxyadenosine) is a nucleoside generated from S-adenosylmethionine (SAM) during polyamine synthesis[1]. 5'-Methylthioadenosine suppresses tumors by inhibiting tumor cell proliferation, invasion, and the induction of apoptosis while controlling the inflammatory micro-environments of tumor tissue. 5'-Methylthioadenosine and its associated materials have striking regulatory effects on tumorigenesis[2]. 5'-Methylthioadenosine (5'-(Methylthio)-5'-deoxyadenosine) is a nucleoside generated from S-adenosylmethionine (SAM) during polyamine synthesis[1]. 5'-Methylthioadenosine suppresses tumors by inhibiting tumor cell proliferation, invasion, and the induction of apoptosis while controlling the inflammatory micro-environments of tumor tissue. 5'-Methylthioadenosine and its associated materials have striking regulatory effects on tumorigenesis[2].

Adenosine diphosphate

C10H15N5O10P2 (427.029415)

Adenosine diphosphate (ADP), also known as adenosine pyrophosphate (APP), is an important organic compound in metabolism and is essential to the flow of energy in living cells. ADP consists of three important structural components: a sugar backbone attached to adenine and two phosphate groups bonded to the 5 carbon atom of ribose. The diphosphate group of ADP is attached to the 5’ carbon of the sugar backbone, while the adenine attaches to the 1’ carbon. ADP belongs to the class of organic compounds known as purine ribonucleoside diphosphates. These are purine ribobucleotides with diphosphate group linked to the ribose moiety. It is an ester of pyrophosphoric acid with the nucleotide adenine. Adenosine diphosphate is a nucleotide. ADP exists in all living species, ranging from bacteria to humans. In humans, ADP is involved in d4-gdi signaling pathway. ADP is the product of ATP dephosphorylation by ATPases. ADP is converted back to ATP by ATP synthases. ADP consists of the pyrophosphate group, the pentose sugar ribose, and the nucleobase adenine. Adenosine diphosphate, abbreviated ADP, is a nucleotide. It is an ester of pyrophosphoric acid with the nucleotide adenine. ADP consists of the pyrophosphate group, the pentose sugar ribose, and the nucleobase adenine. 5′-ADP. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=58-64-0 (retrieved 2024-07-01) (CAS RN: 58-64-0). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). Adenosine 5'-diphosphate (Adenosine diphosphate) is a nucleoside diphosphate. Adenosine 5'-diphosphate is the product of ATP dephosphorylation by ATPases. Adenosine 5'-diphosphate induces human platelet aggregation and inhibits stimulated adenylate cyclase by an action at P2T-purinoceptors. Adenosine 5'-diphosphate (Adenosine diphosphate) is a nucleoside diphosphate. Adenosine 5'-diphosphate is the product of ATP dephosphorylation by ATPases. Adenosine 5'-diphosphate induces human platelet aggregation and inhibits stimulated adenylate cyclase by an action at P2T-purinoceptors.

Coenzyme A

C21H36N7O16P3S (767.1152046)

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. 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. Coenzyme A. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=85-61-0 (retrieved 2024-10-17) (CAS RN: 85-61-0). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0).

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.

L-Ornithine

C5H12N2O2 (132.0898732)

Ornithine, also known as (S)-2,5-diaminopentanoic acid or ornithine, (L)-isomer, is a member of the class of compounds known as L-alpha-amino acids. L-alpha-amino acids are alpha amino acids which have the L-configuration of the alpha-carbon atom. Ornithine is soluble (in water) and a moderately acidic compound (based on its pKa). Ornithine can be found in a number of food items such as pine nut, lingonberry, turnip, and cassava, which makes ornithine a potential biomarker for the consumption of these food products. Ornithine can be found primarily in most biofluids, including urine, cerebrospinal fluid (CSF), feces, and saliva, as well as throughout most human tissues. Ornithine exists in all living species, ranging from bacteria to humans. In humans, ornithine is involved in few metabolic pathways, which include arginine and proline metabolism, glycine and serine metabolism, spermidine and spermine biosynthesis, and urea cycle. Ornithine is also involved in several metabolic disorders, some of which include ornithine transcarbamylase deficiency (OTC deficiency), prolidase deficiency (PD), citrullinemia type I, and arginine: glycine amidinotransferase deficiency (AGAT deficiency). Moreover, ornithine is found to be associated with cystinuria, alzheimers disease, leukemia, and uremia. Ornithine is a non-carcinogenic (not listed by IARC) potentially toxic compound. Ornithine is a drug which is used for nutritional supplementation, also for treating dietary shortage or imbalance. it has been claimed that ornithine improves athletic performance, has anabolic effects, has wound-healing effects, and is immuno-enhancing. Ornithine is a non-proteinogenic amino acid that plays a role in the urea cycle. Ornithine is abnormally accumulated in the body in ornithine transcarbamylase deficiency. The radical is ornithyl . L-Ornithine is metabolised to L-arginine. L-arginine stimulates the pituitary release of growth hormone. Burns or other injuries affect the state of L-arginine in tissues throughout the body. As De novo synthesis of L-arginine during these conditions is usually not sufficient for normal immune function, nor for normal protein synthesis, L-ornithine may have immunomodulatory and wound-healing activities under these conditions (by virtue of its metabolism to L-arginine) (DrugBank). Chronically high levels of ornithine are associated with at least 9 inborn errors of metabolism including: Cystathionine Beta-Synthase Deficiency, Hyperornithinemia with gyrate atrophy, Hyperornithinemia-hyperammonemia-homocitrullinuria syndrome, Hyperornithinemia-hyperammonemia-homocitrullinuria syndrome, Hyperprolinemia Type II, Lysinuric Protein Intolerance, Ornithine Aminotransferase Deficiency, Ornithine Transcarbamylase Deficiency and Prolinemia Type II (T3DB). Ornithine or L-ornithine, also known as (S)-2,5-diaminopentanoic acid is a member of the class of compounds known as L-alpha-amino acids. L-alpha-amino acids are alpha amino acids which have the L-configuration of the alpha-carbon atom. L-ornithine is soluble (in water) and a moderately basic compound. Ornithine is a non-proteinogenic amino acid that plays a role in the urea cycle. It is considered to be a non-essential amino acid. 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. L-Ornithine is one of the products of the action of the enzyme arginase on L-arginine, creating urea. Therefore, ornithine is a central part of the urea cycle, which allows for the disposal of excess nitrogen. Outside the human body, L-ornithine is abundant in a number of food items such as wild rice, brazil nuts, common oregano, and common grapes. L-ornithine can be found throughout most human tissues; and in most biofluids, some of which include blood, urine, cerebrospinal fluid (CSF), sweat, saliva, and feces. L-ornithine exists in all living species, from bacteria to plants to humans. L-Ornithine is also a precursor of citrulline and arginine. In order for ornithine that is produced in the cytosol to be converted to citrulline, it must first cross the inner mitochondrial membrane into the mitochondrial matrix where it is carbamylated by the enzyme known as ornithine transcarbamylase. This transfer is mediated by the mitochondrial ornithine transporter (SLC25A15; AF112968; ORNT1). Mutations in the mitochondrial ornithine transporter result in hyperammonemia, hyperornithinemia, homocitrullinuria (HHH) syndrome, a disorder of the urea cycle (PMID: 16256388). The pathophysiology of the disease may involve diminished ornithine transport into mitochondria, resulting in ornithine accumulation in the cytoplasm and reduced ability to clear carbamoyl phosphate and ammonia loads (OMIM 838970). In humans, L-ornithine is involved in a number of other metabolic disorders, some of which include, ornithine transcarbamylase deficiency (OTC deficiency), argininemia, and guanidinoacetate methyltransferase deficiency (GAMT deficiency). Ornithine is abnormally accumulated in the body in ornithine transcarbamylase deficiency. Moreover, Ornithine is found to be associated with cystinuria, hyperdibasic aminoaciduria I, and lysinuric protein intolerance, which are inborn errors of metabolism. It has been claimed that ornithine improves athletic performance, has anabolic effects, has wound-healing effects, and is immuno-enhancing. L-Ornithine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=70-26-8 (retrieved 2024-07-01) (CAS RN: 70-26-8). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). L-Ornithine ((S)-2,5-Diaminopentanoic acid) is a non-proteinogenic amino acid, is mainly used in urea cycle removing excess nitrogen in vivo. L-Ornithine shows nephroprotective[1][2]. L-Ornithine ((S)-2,5-Diaminopentanoic acid) is a non-proteinogenic amino acid, is mainly used in urea cycle removing excess nitrogen in vivo. L-Ornithine shows nephroprotective[1][2].

Spermine

C10H26N4 (202.2157356)

Spermine, also known as gerontine or musculamine, belongs to the class of organic compounds known as dialkylamines. These are organic compounds containing a dialkylamine group, characterized by two alkyl groups bonded to the amino nitrogen. The resultin N-carbamoylputrescine is acted on by a hydrolase to split off urea group, leaving putrescine. The precursor for synthesis of spermine is the amino acid ornithine. The intermediate is spermidine. Spermine is a drug. Spermine exists in all living species, ranging from bacteria to humans. 5-methylthioadenosine and spermine can be biosynthesized from S-adenosylmethioninamine and spermidine through its interaction with the enzyme spermine synthase. Another pathway in plants starts with decarboxylation of L-arginine to produce agmatine. In humans, spermine is involved in spermidine and spermine biosynthesis. Outside of the human body, spermine is found, on average, in the highest concentration in oats. Spermine has also been detected, but not quantified in several different foods, such as sapodilla, mexican groundcherries, cloves, sourdocks, and sunflowers. This could make spermine a potential biomarker for the consumption of these foods. This decarboxylation gives putrescine. The name spermin was first used by the German chemists Ladenburg and Abel in 1888, and the correct structure of spermine was not finally established until 1926, simultaneously in England (by Dudley, Rosenheim, and Starling) and Germany (by Wrede et al.). In one pathway L-glutamine is the precursor to L-ornithine, after which the synthesis of spermine from L-ornithine follows the same pathway as in animals. Spermine is a potentially toxic compound. [Spectral] Spermine (exact mass = 202.21575) and Spermidine (exact mass = 145.1579) 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. Occurs as phosphate in ox pancreas, yeast and meat products IPB_RECORD: 270; CONFIDENCE confident structure KEIO_ID S011; [MS2] KO009230 KEIO_ID S011 Spermine (NSC 268508) functions directly as a free radical scabenger to protect DNA from free radical attack. Spermine has antiviral effects. Spermine (NSC 268508) functions directly as a free radical scabenger to protect DNA from free radical attack. Spermine has antiviral effects.

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].

Dephospho-CoA

C21H35N7O13P2S (687.1488720000001)

Dephospho-CoA, also known as 3-dephospho-CoA, belongs to the class of organic compounds known as purine ribonucleoside diphosphates. These are purine ribonucleosides with a diphosphate group linked to the ribose moiety. Thus, dephospho-CoA is considered to be a fatty ester lipid molecule. Dephospho-CoA is a very hydrophobic molecule, practically insoluble (in water), and relatively neutral. Outside of the human body, dephospho-CoA has been detected, but not quantified in, several different foods, such as wild leeks, summer savouries, arctic blackberries, biscuits, and persimmons. This could make dephospho-CoA a potential biomarker for the consumption of these foods. Dephospho-CoA is an intermediate in pantothenate and CoA biosynthesis. It is a substrate for bifunctional coenzyme A synthase which contains the dephospho-CoA kinase (EC 2.7.1.24). This enzyme catalyzes the final step in CoA biosynthesis: the phosphorylation of the 3-hydroxyl group of ribose using ATP as a phosphate donor. The reaction is ATP + 3-dephospho-CoA = ADP + CoA. Dephospho-CoA is a substrate for Ectonucleotide pyrophosphatase/phosphodiesterase 1, Ectonucleotide pyrophosphatase/phosphodiesterase 3 and Ectonucleotide pyrophosphatase/phosphodiesterase 2. [HMDB]. Dephospho-CoA is found in many foods, some of which are cardamom, epazote, lemon balm, and mammee apple. Acquisition and generation of the data is financially supported in part by CREST/JST.

Spermidine

C7H19N3 (145.1578894)

Spermidine, also known as SPD, belongs to the class of organic compounds known as dialkylamines. These are organic compounds containing a dialkylamine group, characterized by two alkyl groups bonded to the amino nitrogen. Abnormal bleeding, such as bleeding spontaneously or profusely from a very minor injury can also occur. Spermidine exists in all living species, ranging from bacteria to humans. Within humans, spermidine participates in a number of enzymatic reactions. In particular, 5-methylthioadenosine and spermidine can be biosynthesized from S-adenosylmethioninamine and putrescine by the enzyme spermidine synthase. In addition, S-adenosylmethioninamine and spermidine can be converted into 5-methylthioadenosine and spermine through the action of the enzyme spermine synthase. In humans, spermidine is involved in spermidine and spermine biosynthesis. Outside of the human body, spermidine is found, on average, in the highest concentration within cow milk and oats. Spermidine has also been detected, but not quantified in several different foods, such as common chokecherries, watercress, agars, strawberry guava, and bog bilberries. This could make spermidine a potential biomarker for the consumption of these foods. Spermidine is consideres as an uremic toxine. Increased levels of uremic toxins can stimulate the production of reactive oxygen species. Chronic exposure to uremic toxins can lead to a number of conditions including renal damage, chronic kidney disease and cardiovascular disease. As a uremic toxin, this compound can cause uremic syndrome. Uremic toxins such as spermidine are actively transported into the kidneys via organic ion transporters (especially OAT3). Constituent of meat products. Isol from the edible shaggy ink cap mushroom (Coprinus comatus) and from commercial/household prepared sauerkraut COVID info from clinicaltrial, clinicaltrials, clinical trial, clinical trials IPB_RECORD: 269; CONFIDENCE confident structure CONFIDENCE standard compound; INTERNAL_ID 220 KEIO_ID S003 Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS Spermidine maintains cell membrane stability, increases antioxidant enzymes activities, improving photosystem II (PSII), and relevant gene expression. Spermidine significantly decreases the H2O2 and O2.- contents[1]. Spermidine maintains cell membrane stability, increases antioxidant enzymes activities, improving photosystem II (PSII), and relevant gene expression. Spermidine significantly decreases the H2O2 and O2.- contents[1].

Cytidine monophosphate

C9H14N3O8P (323.05184940000004)

Cytidine monophosphate, also known as 5-cytidylic acid and abbreviated CMP, is a nucleotide. It is an ester of phosphoric acid with the nucleoside cytidine. CMP consists of the phosphate group, the pentose sugar ribose, and the nucleobase cytosine. Cytidine monophosphate (CMP) is derived from cytidine triphosphate (CTP) with subsequent loss of two phosphates. The synthesis of the pyrimidines CTP and UTP occurs in the cytoplasm and starts with the formation of carbamoyl phosphate from glutamine and CO2. Next, aspartate undergoes a condensation reaction with carbamoyl-phosphate to form orotic acid. In a subsequent cyclization reaction, the enzyme Aspartate carbamoyltransferase forms N-carbamoyl-aspartate which is converted into dihydroorotic acid by Dihydroorotase. The latter is converted to orotate by Dihydroorotate oxidase. Orotate is covalently linked with a phosphorylated ribosyl unit with Orotate phosphoribosyltransferase (aka "PRPP transferase") catalyzing reaction, yielding orotidine monophosphate (OMP). Orotidine-5-phosphate is decarboxylated by Orotidine-5-phosphate decarboxylase to form uridine monophosphate (UMP). UMP is phosphorylated by two kinases to uridine triphosphate (UTP) via two sequential reactions with ATP. CTP is subsequently formed by amination of UTP by the catalytic activity of CTP synthetase. Cytosine monophosphate (CMP) and uridine monophosphate (UMP) have been prescribed for the treatment of neuromuscular affections in humans. Patients treated with CMP/UMP recover from altered neurological functions. Additionally, the administration of CMP/UMP appears to favour the entry of glucose in the muscle and CMP/UMP may be important in maintaining the level of hepatic glycogen constant during exercise. [PMID:18663991]. Cytidine monophosphate, also known as cmp or cytidylic acid, is a member of the class of compounds known as pyrimidine ribonucleoside monophosphates. Pyrimidine ribonucleoside monophosphates are pyrimidine ribobucleotides with monophosphate group linked to the ribose moiety. Cytidine monophosphate is soluble (in water) and a moderately acidic compound (based on its pKa). Cytidine monophosphate can be found in a number of food items such as elliotts blueberry, small-leaf linden, orange mint, and malabar spinach, which makes cytidine monophosphate a potential biomarker for the consumption of these food products. Cytidine monophosphate can be found primarily in saliva, as well as throughout all human tissues. Cytidine monophosphate exists in all living species, ranging from bacteria to humans. In humans, cytidine monophosphate is involved in several metabolic pathways, some of which include cardiolipin biosynthesis cl(i-13:0/i-18:0/i-17:0/18:2(9z,11z)), cardiolipin biosynthesis cl(i-13:0/i-24:0/a-21:0/i-15:0), cardiolipin biosynthesis cl(i-13:0/i-22:0/i-20:0/i-15:0), and cardiolipin biosynthesis cl(i-12:0/a-17:0/i-20:0/a-21:0). Cytidine monophosphate is also involved in several metabolic disorders, some of which include beta ureidopropionase deficiency, MNGIE (mitochondrial neurogastrointestinal encephalopathy), UMP synthase deficiency (orotic aciduria), and dihydropyrimidinase deficiency. Acquisition and generation of the data is financially supported in part by CREST/JST. COVID info from WikiPathways Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS Cytidine 5'-monophosphate (5'-Cytidylic acid) is a nucleotide which is used as a monomer in RNA. Cytidine 5'-monophosphate consists of the nucleobase cytosine, the pentose sugar ribose, and the phosphate group[1]. Cytidine 5'-monophosphate (5'-Cytidylic acid) is a nucleotide which is used as a monomer in RNA. Cytidine 5'-monophosphate consists of the nucleobase cytosine, the pentose sugar ribose, and the phosphate group[1].

Beta-Alanine

C3H7NO2 (89.0476762)

beta-Alanine is the only naturally occurring beta-amino acid - an amino acid in which the amino group is at the beta-position from the carboxylate group. It is formed in vivo by the degradation of dihydrouracil and carnosine. It is a component of the naturally occurring peptides carnosine and anserine and also of pantothenic acid (vitamin B-5), which itself is a component of coenzyme A. Under normal conditions, beta-alanine is metabolized into acetic acid. beta-Alanine can undergo a transanimation reaction with pyruvate to form malonate-semialdehyde and L-alanine. The malonate semialdehyde can then be converted into malonate via malonate-semialdehyde dehydrogenase. Malonate is then converted into malonyl-CoA and enter fatty acid biosynthesis. Since neuronal uptake and neuronal receptor sensitivity to beta-alanine have been demonstrated, beta-alanine may act as a false transmitter replacing gamma-aminobutyric acid. When present in sufficiently high levels, beta-alanine can act as a neurotoxin, a mitochondrial toxin, and a metabotoxin. A neurotoxin is a compound that damages the brain or nerve tissue. A mitochondrial toxin is a compound that damages mitochondria and reduces cellular respiration as well as oxidative phosphorylation. A metabotoxin is an endogenously produced metabolite that causes adverse health effects at chronically high levels. Chronically high levels of beta-alanine are associated with at least three inborn errors of metabolism, including GABA-transaminase deficiency, hyper-beta-alaninemia, and methylmalonate semialdehyde dehydrogenase deficiency. beta-Alanine is a central nervous system (CNS) depressant and is an inhibitor of GABA transaminase. The associated inhibition of GABA transaminase and displacement of GABA from CNS binding sites can also lead to GABAuria (high levels of GABA in the urine) and convulsions. In addition to its neurotoxicity, beta-alanine reduces cellular levels of taurine, which are required for normal respiratory chain function. Cellular taurine depletion is known to reduce respiratory function and elevate mitochondrial superoxide generation, which damages mitochondria and increases oxidative stress (PMID: 27023909). Individuals suffering from mitochondrial defects or mitochondrial toxicity typically develop neurotoxicity, hypotonia, respiratory distress, and cardiac failure. beta-Alanine is a biomarker for the consumption of meat, especially red meat. Widely distributed in plants including algae, fungi and many higher plants. Flavouring ingredient β-Alanine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=107-95-9 (retrieved 2024-07-01) (CAS RN: 107-95-9). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). β-Alanine is a non-essential amino acid that is shown to be metabolized into carnosine, which functions as an intracellular buffer. β-Alanine is a non-essential amino acid that is shown to be metabolized into carnosine, which functions as an intracellular buffer. β-Alanine is a non-essential amino acid that is shown to be metabolized into carnosine, which functions as an intracellular buffer.

NADP+

[C21H29N7O17P3]+ (744.0832754)

[Spectral] NADP+ (exact mass = 743.07545) and NAD+ (exact mass = 663.10912) 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

Cytidine triphosphate

C9H16N3O14P3 (482.9845146)

Cytidine triphosphate (CTP), also known as 5-CTP, is pyrimidine nucleoside triphosphate. Formally, CTP is an ester of cytidine and triphosphoric acid. It belongs to the class of organic compounds known as pentose phosphates. These are carbohydrate derivatives containing a pentose substituted by one or more phosphate groups. CTP, much like ATP, consists of a base (cytosine), a ribose sugar, and three phosphate groups. CTP is a high-energy molecule similar to ATP, but its role as an energy coupler is limited to a much smaller subset of metabolic reactions. CTP exists in all living species, ranging from bacteria to plants to humans and is used in the synthesis of RNA via RNA polymerase. Another enzyme known as cytidine triphosphate synthetase (CTPS) mediates the conversion of uridine triphosphate (UTP) into cytidine triphosphate (CTP) which is the rate-limiting step of de novo CTP biosynthesis. CTPS catalyzes a complex set of reactions that include the ATP-dependent transfer of the amide nitrogen from glutamine (i.e., glutaminase reaction) to the C-4 position of UTP to generate CTP. GTP stimulates the glutaminase reaction by accelerating the formation of a covalent glutaminyl enzyme intermediate. CTPS activity regulates the intracellular rates of RNA synthesis, DNA synthesis, and phospholipid synthesis. CTPS is an established target for a number of antiviral, antineoplastic, and antiparasitic drugs. CTP also acts as an inhibitor of the enzyme known as aspartate carbamoyltransferase, which is used in pyrimidine biosynthesis. CTP also reacts with nitrogen-containing alcohols to form coenzymes that participate in the formation of phospholipids. In particular, CTP is the direct precursor of the activated, phospholipid pathway intermediates CDP-diacylglycerol, CDP-choline, and CDP-ethanolamine ((PMID: 18439916). CDP-diacylglycerol is the source of the phosphatidyl moiety for phosphatidylserine, phosphatidylethanolamine, and phosphatidylcholine (synthesized by way of the CDP-diacylglycerol pathway) as well as phosphatidylglycerol, cardiolipin, and phosphatidylinositol (PMID: 18439916). Cytidine triphosphate, also known as 5-ctp or cytidine 5-triphosphoric acid, is a member of the class of compounds known as pentose phosphates. Pentose phosphates are carbohydrate derivatives containing a pentose substituted by one or more phosphate groups. Cytidine triphosphate is soluble (in water) and an extremely strong acidic compound (based on its pKa). Cytidine triphosphate can be found in a number of food items such as lowbush blueberry, black radish, american pokeweed, and cherry tomato, which makes cytidine triphosphate a potential biomarker for the consumption of these food products. Cytidine triphosphate can be found primarily in cellular cytoplasm, as well as throughout all human tissues. Cytidine triphosphate exists in all living species, ranging from bacteria to humans. In humans, cytidine triphosphate is involved in several metabolic pathways, some of which include cardiolipin biosynthesis cl(i-14:0/i-17:0/i-16:0/i-21:0), cardiolipin biosynthesis cl(a-13:0/a-21:0/i-22:0/i-17:0), phosphatidylethanolamine biosynthesis PE(18:2(9Z,12Z)/24:0), and cardiolipin biosynthesis cl(i-13:0/a-21:0/a-15:0/i-16:0). Cytidine triphosphate is also involved in several metabolic disorders, some of which include sialuria or french type sialuria, tay-sachs disease, MNGIE (mitochondrial neurogastrointestinal encephalopathy), and g(m2)-gangliosidosis: variant B, tay-sachs disease. Cytidine triphosphate is a high-energy molecule similar to ATP, but its role as an energy coupler is limited to a much smaller subset of metabolic reactions. Cytidine triphosphate is a coenzyme in metabolic reactions like the synthesis of glycerophospholipids and glycosylation of proteins . Cytidine 5′-triphosphate (Cytidine triphosphate; 5'-CTP) is a nucleoside triphosphate and serves as a building block for nucleotides and nucleic acids, lipid biosynthesis. Cytidine triphosphate synthase can catalyze the formation of cytidine 5′-triphosphate from uridine 5′-triphosphate (UTP). Cytidine 5′-triphosphate is an essential biomolecule?in the de novo?pyrimidine biosynthetic pathway in?T. gondii[1].

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

Hydrogen peroxide

H2O2 (34.0054792)

Hydrogen peroxide (H2O2) is a very pale blue liquid that appears colourless in a dilute solution. H2O2 is slightly more viscous than water and is a weak acid. H2O2 is unstable and slowly decomposes in the presence of light. It has strong oxidizing properties and is, therefore, a powerful bleaching agent that is mostly used for bleaching paper. H2O2 has also found use as a disinfectant and as an oxidizer. H2O2 in the form of carbamide peroxide is widely used for tooth whitening (bleaching), both in professionally- and in self-administered products. H2O2 is a well-documented component of living cells and is a normal metabolite of oxygen in the aerobic metabolism of cells and tissues. A total of 31 human cellular H2O2 generating enzymes has been identified so far (PMID: 25843657). H2O2 plays important roles in host defence and oxidative biosynthetic reactions. At high levels (>100 nM) H2O2 is toxic to most cells due to its ability to non-specifically oxidize proteins, membranes and DNA, leading to general cellular damage and dysfunction. However, at low levels (<10 nM), H2O2 functions as a signalling agent, particularly in higher organisms. In plants, H2O2 plays a role in signalling to cause cell shape changes such as stomatal closure and root growth. As a messenger molecule in vertebrates, H2O2 diffuses through cells and tissues to initiate cell shape changes, to drive vascular remodelling, and to activate cell proliferation and recruitment of immune cells. H2O2 also plays a role in redox sensing, signalling, and redox regulation (PMID: 28110218). This is normally done through molecular redox “switches” such as thiol-containing proteins. The production and decomposition of H2O2 are tightly regulated (PMID: 17434122). In humans, H2O2 can be generated in response to various stimuli, including cytokines and growth factors. H2O2 is degraded by several enzymes including catalase and superoxide dismutase (SOD), both of which play important roles in keeping the amount of H2O2 in the body below toxic levels. H2O2 also appears to play a role in vitiligo. Vitiligo is a skin pigment disorder leading to patchy skin colour, especially among dark-skinned individuals. Patients with vitiligo have low catalase levels in their skin, leading to higher levels of H2O2. High levels of H2O2 damage the epidermal melanocytes, leading to a loss of pigment (PMID: 10393521). Accumulating evidence suggests that hydrogen peroxide H2O2 plays an important role in cancer development. Experimental data have shown that cancer cells produce high amounts of H2O2. An increase in the cellular levels of H2O2 has been linked to several key alterations in cancer, including DNA changes, cell proliferation, apoptosis resistance, metastasis, angiogenesis and hypoxia-inducible factor 1 (HIF-1) activation (PMID: 17150302, 17335854, 16677071, 16607324, 16514169). H2O2 is found in most cells, tissues, and biofluids. H2O2 levels in the urine can be significantly increased with the consumption of coffee and other polyphenolic-containing beverages (wine, tea) (PMID: 12419961). In particular, roasted coffee has high levels of 1,2,4-benzenetriol which can, on its own, lead to the production of H2O2. Normal levels of urinary H2O2 in non-coffee drinkers or fasted subjects are between 0.5-3 uM/mM creatinine whereas, for those who drink coffee, the levels are between 3-10 uM/mM creatinine (PMID: 12419961). It is thought that H2O2 in urine could act as an antibacterial agent and that H2O2 is involved in the regulation of glomerular function (PMID: 10766414). A - Alimentary tract and metabolism > A01 - Stomatological preparations > A01A - Stomatological preparations > A01AB - Antiinfectives and antiseptics for local oral treatment D - Dermatologicals > D08 - Antiseptics and disinfectants > D08A - Antiseptics and disinfectants S - Sensory organs > S02 - Otologicals > S02A - Antiinfectives > S02AA - Antiinfectives It is used in foods as a bleaching agent, antimicrobial agent and oxidising agent C254 - Anti-Infective Agent > C28394 - Topical Anti-Infective Agent D009676 - Noxae > D016877 - Oxidants > D010545 - Peroxides D000890 - Anti-Infective Agents

S-Adenosylmethioninamine

C14H23N6O3S+ (355.15522680000004)

S-Adenosylmethioninamine is a biological sulfonium compound known as the major biological methyl donor. It is also a donor of methylene groups, amino groups, ribosyl groups and aminopropyl groups (PMID 15130560). S-Adenosylmethioninamine is a prodcut of enzyme adenosylmethionine decarboxylase [EC 4.1.1.50] in methionine metabolism pathway (KEGG). [HMDB] S-Adenosylmethioninamine is a biological sulfonium compound known as the major biological methyl donor. It is also a donor of methylene groups, amino groups, ribosyl groups and aminopropyl groups (PMID 15130560). S-Adenosylmethioninamine is a prodcut of enzyme adenosylmethionine decarboxylase [EC 4.1.1.50] in methionine metabolism pathway (KEGG).

D-4'-Phosphopantothenate

C9H18NO8P (299.0769998)

D-4-Phosphopantothenate is a product of the enzyme pantothenate kinase [EC 2.7.1.33] and is involved in the pantothenate and CoA biosynthesis pathway (KEGG). D-4-Phosphopantothenate is an intermediate in coenzyme A (CoA) biosynthesis pathway. Coenzyme A is a cofactor of ubiquitous occurrence in plants, bacteria, and animals. It is needed in a large number of enzymatic reactions central to intermediary metabolism, including the oxidation of fatty acids, carbohydrates, and amino acids.

4'-Phosphopantothenoylcysteine

C12H23N2O9PS (402.0861838)

4-Phosphopantothenoylcysteine, also known as pantothenoylcysteine 4-phosphate, belongs to the class of organic compounds known as hybrid peptides. Hybrid peptides are compounds containing at least two different types of amino acids (alpha, beta, gamma, delta) linked to each other through a peptide bond. 4-Phosphopantothenoylcysteine is an extremely weak basic (essentially neutral) compound (based on its pKa). Within humans, 4-phosphopantothenoylcysteine participates in a number of enzymatic reactions. In particular, cytidine monophosphate and 4-phosphopantothenoylcysteine can be biosynthesized from cytidine triphosphate, D-4-phosphopantothenate, and L-cysteine through the action of the enzyme phosphopantothenate--cysteine ligase. 4-Phosphopantothenoylcysteine (PPC) is an intermediate in the biosynthetic machinery (pathway) that converts pantothenate (vitamin B5) into coenzyme A (CoA). The enzyme phosphopantothenoylcysteine decarboxylase catalyzes the decarboxylation of PPC into 4-phosphopantetheine. Coenzyme A is the principal acyl carrier and is required for many synthetic and degradative reactions in intermediary metabolism, and is an essential cofactor in all living systems (PMID: 15450493, 16371361, 14501115). 4-Phosphopantothenoylcysteine (PPC) is an intermediate in the biosynthetic machinery (pathway) that converts pantothenate (vitamin B5) into coenzyme A (CoA). The enzyme Phosphopantothenoylcysteine decarboxylase catalyzes the decarboxylation of PPC to 4-phosphopantetheine. Coenzyme A is the principal acyl carrier and is required for many synthetic and degradative reactions in intermediary metabolism, and is an essential cofactor in all living systems. (PMID: 15450493, 16371361, 14501115) [HMDB]

3-Aminopropionaldehyde

C3H7NO (73.0527612)

3-aminopropionaldehyde is a member of the class of compounds known as alpha-hydrogen aldehydes. Alpha-hydrogen aldehydes are aldehydes with the general formula HC(H)(R)C(=O)H, where R is an organyl group. 3-aminopropionaldehyde is soluble (in water) and a very weakly acidic compound (based on its pKa). 3-aminopropionaldehyde can be found in a number of food items such as lemon, natal plum, common wheat, and leek, which makes 3-aminopropionaldehyde a potential biomarker for the consumption of these food products. 3-aminopropionaldehyde exists in all living organisms, ranging from bacteria to humans. In humans, 3-aminopropionaldehyde is involved in the beta-alanine metabolism. 3-aminopropionaldehyde is also involved in few metabolic disorders, which include carnosinuria, carnosinemia, gaba-transaminase deficiency, and ureidopropionase deficiency. 3-Aminopropanal is a reactive aldehyde that mediates progressive neuronal necrosis and glial apoptosis. (PMID 11943872). Increased activity of polyamine oxidase catabolizes polyamines (such as spermine, spermidine and putrescine) to produce 3-aminopropanal. (PMID 15246852).

Hydrogen Ion

H+ (1.0078246)

Hydrogen ion, also known as proton or h+, is a member of the class of compounds known as other non-metal hydrides. Other non-metal hydrides are inorganic compounds in which the heaviest atom bonded to a hydrogen atom is belongs to the class of other non-metals. Hydrogen ion can be found in a number of food items such as lowbush blueberry, groundcherry, parsley, and tarragon, which makes hydrogen ion a potential biomarker for the consumption of these food products. Hydrogen ion exists in all living organisms, ranging from bacteria to humans. In humans, hydrogen ion is involved in several metabolic pathways, some of which include cardiolipin biosynthesis cl(i-13:0/a-25:0/a-21:0/i-15:0), cardiolipin biosynthesis cl(a-13:0/a-17:0/i-13:0/a-25:0), cardiolipin biosynthesis cl(i-12:0/i-13:0/a-17:0/a-15:0), and cardiolipin biosynthesis CL(16:1(9Z)/22:5(4Z,7Z,10Z,13Z,16Z)/18:1(11Z)/22:5(7Z,10Z,13Z,16Z,19Z)). Hydrogen ion is also involved in several metabolic disorders, some of which include de novo triacylglycerol biosynthesis TG(20:3(8Z,11Z,14Z)/22:6(4Z,7Z,10Z,13Z,16Z,19Z)/22:5(7Z,10Z,13Z,16Z,19Z)), de novo triacylglycerol biosynthesis TG(18:2(9Z,12Z)/20:0/20:4(5Z,8Z,11Z,14Z)), de novo triacylglycerol biosynthesis TG(18:4(6Z,9Z,12Z,15Z)/18:3(9Z,12Z,15Z)/18:4(6Z,9Z,12Z,15Z)), and de novo triacylglycerol biosynthesis TG(24:0/20:5(5Z,8Z,11Z,14Z,17Z)/24:0). A hydrogen ion is created when a hydrogen atom loses or gains an electron. A positively charged hydrogen ion (or proton) can readily combine with other particles and therefore is only seen isolated when it is in a gaseous state or a nearly particle-free space. Due to its extremely high charge density of approximately 2×1010 times that of a sodium ion, the bare hydrogen ion cannot exist freely in solution as it readily hydrates, i.e., bonds quickly. The hydrogen ion is recommended by IUPAC as a general term for all ions of hydrogen and its isotopes. Depending on the charge of the ion, two different classes can be distinguished: positively charged ions and negatively charged ions . Hydrogen ion is recommended by IUPAC as a general term for all ions of hydrogen and its isotopes. Depending on the charge of the ion, two different classes can be distinguished: positively charged ions and negatively charged ions. Under aqueous conditions found in biochemistry, hydrogen ions exist as the hydrated form hydronium, H3O+, but these are often still referred to as hydrogen ions or even protons by biochemists. [Wikipedia])

S-Adenosyl-L-methionine

C15H23N6O5S+ (399.1450568)

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Phosphate Ion

O4P-3 (94.953423)

Pantoate

C6H11O4- (147.0657306)

D-pantetheine 4-phosphate(2-)

C11H21N2O7PS-2 (356.08070460000005)

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Diphosphate

O7P2-4 (173.911931)

In chemistry, the anion, the salts, and the esters of pyrophosphoric acid are called pyrophosphates. The 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. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=14000-31-8 (retrieved 2024-10-08) (CAS RN: 14000-31-8). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0).

ent-NADPH

C21H30N7O17P3 (745.0911)

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