Reaction Process: Reactome:R-SPO-196849

Nicotinic acid

C6H5NO2 (123.032027)

Nicotinic acid is an odorless white crystalline powder with a feebly acid taste. pH (saturated aqueous solution) 2.7. pH (1.3\\\\\% solution) 3-3.5. (NTP, 1992) Nicotinic acid is a pyridinemonocarboxylic acid that is pyridine in which the hydrogen at position 3 is replaced by a carboxy group. It has a role as an antidote, an antilipemic drug, a vasodilator agent, a metabolite, an EC 3.5.1.19 (nicotinamidase) inhibitor, an Escherichia coli metabolite, a mouse metabolite, a human urinary metabolite and a plant metabolite. It is a vitamin B3, a pyridinemonocarboxylic acid and a pyridine alkaloid. It is a conjugate acid of a nicotinate. Niacin is a B vitamin used to treat vitamin deficiencies as well as hyperlipidemia, dyslipidemia, hypertriglyceridemia, and to reduce the risk of myocardial infarctions. Nicotinic acid is a metabolite found in or produced by Escherichia coli (strain K12, MG1655). Niacin is a Nicotinic Acid. Niacin, also known as nicotinic acid and vitamin B3, is a water soluble, essential B vitamin that, when given in high doses, is effective in lowering low density lipoprotein (LDL) cholesterol and raising high density lipoprotein (HDL) cholesterol, which makes this agent of unique value in the therapy of dyslipidemia. Niacin can cause mild-to-moderate serum aminotransferase elevations and high doses and certain formulations of niacin have been linked to clinically apparent, acute liver injury which can be severe as well as fatal. Niacin is a water-soluble vitamin belonging to the vitamin B family, which occurs in many animal and plant tissues, with antihyperlipidemic activity. Niacin is converted to its active form niacinamide, which is a component of the coenzymes nicotinamide adenine dinucleotide (NAD) and its phosphate form, NADP. These coenzymes play an important role in tissue respiration and in glycogen, lipid, amino acid, protein, and purine metabolism. Although the exact mechanism of action by which niacin lowers cholesterol is not fully understood, it may act by inhibiting the synthesis of very low density lipoproteins (VLDL), inhibiting the release of free fatty acids from adipose tissue, increasing lipoprotein lipase activity, and reducing the hepatic synthesis of VLDL-C and LDL-C. Nicotinic acid, also known as niacin or vitamin B3, is a water-soluble vitamin whose derivatives such as NADH, NAD, NAD+, and NADP play essential roles in energy metabolism in the living cell and DNA repair. The designation vitamin B3 also includes the amide form, nicotinamide or niacinamide. Severe lack of niacin causes the deficiency disease pellagra, whereas a mild deficiency slows down the metabolism decreasing cold tolerance. The recommended daily allowance of niacin is 2-12 mg a day for children, 14 mg a day for women, 16 mg a day for men, and 18 mg a day for pregnant or breast-feeding women. It is found in various animal and plant tissues and has pellagra-curative, vasodilating, and antilipemic properties. The liver can synthesize niacin from the essential amino acid tryptophan (see below), but the synthesis is extremely slow and requires vitamin B6; 60 mg of tryptophan are required to make one milligram of niacin. Bacteria in the gut may also perform the conversion but are inefficient. A water-soluble vitamin of the B complex occurring in various animal and plant tissues. It is required by the body for the formation of coenzymes NAD and NADP. It has PELLAGRA-curative, vasodilating, and antilipemic properties. Nicotinic acid, also known as niacin or vitamin B3, is a water-soluble vitamin whose derivatives such as NADH, NAD, NAD+, and NADP play essential roles in energy metabolism in the living cell and DNA repair. The designation vitamin B3 also includes the amide form, nicotinamide or niacinamide. Severe lack of niacin causes the deficiency disease pellagra, whereas a mild deficiency slows down the metabolism decreasing cold tolerance. The recommended daily allowance of niacin is 2-12 mg a day for children, 14 mg a day for women, 16 mg a day for men, and 18 mg a day for pregnant or breast-feeding women. It is found in various animal and plant tissues and has pellagra-curative, vasodilating, and antilipemic properties. The liver can synthesize niacin from the essential amino acid tryptophan, but the synthesis is extremely slow and requires vitamin B6; 60 mg of tryptophan are required to make one milligram of niacin. Bacteria in the gut may also perform the conversion but are inefficient. Nicotinic acid. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=59-67-6 (retrieved 2024-06-29) (CAS RN: 59-67-6). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). Niacin (Vitamin B3) is an orally active water-soluble B3 vitamin that is an essential nutrient for humans. Niacin (Vitamin B3) plays a key role in energy metabolism, cell signaling cascades regulating gene expression and apoptosis. Niacin (Vitamin B3) is also used in the study of cardiovascular diseases[1][2]. Niacin (Vitamin B3) is an orally active water-soluble B3 vitamin that is an essential nutrient for humans. Niacin (Vitamin B3) plays a key role in energy metabolism, cell signaling cascades regulating gene expression and apoptosis. Niacin (Vitamin B3) is also used in the study of cardiovascular diseases[1][2].

Folic acid

C19H19N7O6 (441.1396754)

Folic acid appears as odorless orange-yellow needles or platelets. Darkens and chars from approximately 482 °F. Folic acid is an N-acyl-amino acid that is a form of the water-soluble vitamin B9. Its biologically active forms (tetrahydrofolate and others) are essential for nucleotide biosynthesis and homocysteine remethylation. It has a role as a human metabolite, a nutrient and a mouse metabolite. It is a member of folic acids and a N-acyl-amino acid. It is functionally related to a pteroic acid. It is a conjugate acid of a folate(2-). Folic acid, also known as folate or Vitamin B9, is a member of the B vitamin family and an essential cofactor for enzymes involved in DNA and RNA synthesis. More specifically, folic acid is required by the body for the synthesis of purines, pyrimidines, and methionine before incorporation into DNA or protein. Folic acid is particularly important during phases of rapid cell division, such as infancy, pregnancy, and erythropoiesis, and plays a protective factor in the development of cancer. As humans are unable to synthesize folic acid endogenously, diet and supplementation is necessary to prevent deficiencies. For example, folic acid is present in green vegetables, beans, avocado, and some fruits. In order to function within the body, folic acid must first be reduced by the enzyme dihydrofolate reductase (DHFR) into the cofactors dihydrofolate (DHF) and tetrahydrofolate (THF). This important pathway, which is required for de novo synthesis of nucleic acids and amino acids, is disrupted by anti-metabolite therapies such as [DB00563] as they function as DHFR inhibitors to prevent DNA synthesis in rapidly dividing cells, and therefore prevent the formation of DHF and THF. When used in high doses such as for cancer therapy, or in low doses such as for Rheumatoid Arthritis or psoriasis, [DB00563] impedes the bodys ability to create folic acid. This results in a deficiency of coenzymes and a resultant buildup of toxic substances that are responsible for numerous adverse side effects. As a result, supplementation with 1-5mg of folic acid is recommended to prevent deficiency and a number of side effects associated with MTX therapy including mouth ulcers and gastrointestinal irritation. [DB00650] (also known as folinic acid) supplementation is typically used for high-dose MTX regimens for the treatment of cancer. Levoleucovorin and leucovorin are analogs of tetrahydrofolate (THF) and are able to bypass DHFR reduction to act as a cellular replacement for the co-factor THF. There are also several antiepileptic drugs (AEDs) that are associated with reduced serum and red blood cell folate, including [DB00564] (CBZ), [DB00252] (PHT), or barbiturates. Folic acid is therefore often provided as supplementation to individuals using these medications, particularly to women of child-bearing age. Inadequate folate levels can result in a number of health concerns including cardiovascular disease, megaloblastic anemias, cognitive deficiencies, and neural tube defects (NTDs). Folic acid is typically supplemented during pregnancy to prevent the development of NTDs and in individuals with alcoholism to prevent the development of neurological disorders, for example. Folic acid is a metabolite found in or produced by Escherichia coli (strain K12, MG1655). CID 6037 is a natural product found in Beta vulgaris, Angelica sinensis, and other organisms with data available. Folic Acid is a collective term for pteroylglutamic acids and their oligoglutamic acid conjugates. As a natural water-soluble substance, folic acid is involved in carbon transfer reactions of amino acid metabolism, in addition to purine and pyrimidine synthesis, and is essential for hematopoiesis and red blood cell production. (NCI05) A member of the vitamin B family that stimulates the hematopoietic system. It is present in the liver and kidney and is found in mushrooms, spinach, yeast, green leaves, and grasses (POACEAE). Folic acid is used in the treat... Folic acid or folate, is a vitamin that belongs to the class of compounds known as pterins. Chemically, folate consists of three distinct chemical moieties linked together. A pterin (2-amino-4-hydroxy-pteridine) linked by a methylene bridge to a p-aminobenzoyl group that in turn is linked through an amide linkage to glutamic acid. It is a member of the vitamin B family and is primarily known as vitamin B9. Folate is required for the body to make DNA and RNA and metabolize amino acids necessary for cell division for the hematopoietic system. As humans cannot make folate, it is required in the diet, making it an essential nutrient (i.e. a vitamin). Folate occurs naturally in many foods including mushrooms, spinach, yeast, green leaves, and grasses (poaceae). Folic acid, being biochemically inactive, is converted to tetrahydrofolic acid and methyltetrahydrofolate by the enzyme known as dihydrofolate reductase. Tetrahydrofolate and methyltetrahydrofolate are transported across cells by receptor-mediated endocytosis where they are needed to maintain normal erythropoiesis, synthesize purine and thymidylate nucleic acids, interconvert amino acids and generate formic acid. Folic acid is used in the treatment and prevention of folate deficiencies and megaloblastic anemia. Folic acid is also used as a supplement by women during pregnancy to reduce the risk of neural tube defects (NTDs) in babies. Low levels in early pregnancy are believed to be the cause of more than half of babies born with NTDs (PMID: 28097362). Folic acid is also a microbial metabolite produced by Bifidobacterium and Lactobacillus (PMID: 22254078). An N-acyl-amino acid that is a form of the water-soluble vitamin B9. Its biologically active forms (tetrahydrofolate and others) are essential for nucleotide biosynthesis and homocysteine remethylation. B - Blood and blood forming organs > B03 - Antianemic preparations > B03B - Vitamin b12 and folic acid > B03BB - Folic acid and derivatives COVID info from clinicaltrial, clinicaltrials, clinical trial, clinical trials D006401 - Hematologic Agents > D006397 - Hematinics D018977 - Micronutrients > D014815 - Vitamins V - Various > V04 - Diagnostic agents Dietary supplement Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS Formula(Parent): C19H19N7O6; Bottle Name:Folic acid ,approx; PRIME Parent Name:Folic acid; PRIME in-house No.:V0080; SubCategory_DNP: Pteridines and analogues, Pteridine alkaloids Acquisition and generation of the data is financially supported in part by CREST/JST. relative retention time with respect to 9-anthracene Carboxylic Acid is 0.543 CONFIDENCE standard compound; INTERNAL_ID 134 Folic acid (Vitamin B9) is a orally active essential nutrient from the B complex group of vitamins. Folic acid shows antidepressant-like effect. Folic acid sodium reduces the risk of neonatal neural tube defects. Folic acid can be used to the research of megaloblastic and macrocytic anemias due to folic deficiency[1][2][3][4]. Folic acid (Vitamin B9) is a orally active essential nutrient from the B complex group of vitamins. Folic acid shows antidepressant-like effect. Folic acid sodium reduces the risk of neonatal neural tube defects. Folic acid can be used to the research of megaloblastic and macrocytic anemias due to folic deficiency[1][2][3][4].

Biotin

C10H16N2O3S (244.0881586)

Biotin (also known as vitamin B7 or vitamin H) is one of the B vitamins.[1][2][3] It is involved in a wide range of metabolic processes, both in humans and in other organisms, primarily related to the utilization of fats, carbohydrates, and amino acids.[4] The name biotin, borrowed from the German Biotin, derives from the Ancient Greek word βίοτος (bíotos; 'life') and the suffix "-in" (a suffix used in chemistry usually to indicate 'forming').[5] Biotin appears as a white, needle-like crystalline solid.[6] Biotin is an organic heterobicyclic compound that consists of 2-oxohexahydro-1H-thieno[3,4-d]imidazole having a valeric acid substituent attached to the tetrahydrothiophene ring. The parent of the class of biotins. It has a role as a prosthetic group, a coenzyme, a nutraceutical, a human metabolite, a Saccharomyces cerevisiae metabolite, an Escherichia coli metabolite, a mouse metabolite, a cofactor and a fundamental metabolite. It is a member of biotins and a vitamin B7. It is a conjugate acid of a biotinate. A water-soluble, enzyme co-factor present in minute amounts in every living cell. It occurs mainly bound to proteins or polypeptides and is abundant in liver, kidney, pancreas, yeast, and milk. Biotin is a metabolite found in or produced by Escherichia coli (strain K12, MG1655). Biotin is a natural product found in Lysinibacillus sphaericus, Aspergillus nidulans, and other organisms with data available. Biotin is hexahydro-2-oxo-1H-thieno(3,4-d)imidazole-4-pentanoic acid. Growth factor present in minute amounts in every living cell. It occurs mainly bound to proteins or polypeptides and is abundant in liver, kidney, pancreas, yeast, and milk. The biotin content of cancerous tissue is higher than that of normal tissue. Biotin is an enzyme co-factor present in minute amounts in every living cell. Biotin is also known as vitamin H or B7 or coenzyme R. It occurs mainly bound to proteins or polypeptides and is abundant in liver, kidney, pancreas, yeast, and milk. Biotin has been recognized as an essential nutrient. Our biotin requirement is fulfilled in part through diet, through endogenous reutilization of biotin and perhaps through capture of biotin generated in the intestinal flora. The utilization of biotin for covalent attachment to carboxylases and its reutilization through the release of carboxylase biotin after proteolytic degradation constitutes the biotin cycle. Biotin deficiency is associated with neurological manifestations, skin rash, hair loss and metabolic disturbances that are thought to relate to the various carboxylase deficiencies (metabolic ketoacidosis with lactic acidosis). It has also been suggested that biotin deficiency is associated with protein malnutrition, and that marginal biotin deficiency in pregnant women may be teratogenic. Biotin acts as a carboxyl carrier in carboxylation reactions. There are four biotin-dependent carboxylases in mammals: those of propionyl-CoA (PCC), 3-methylcrotonyl-CoA (MCC), pyruvate (PC) and acetyl-CoA carboxylases (isoforms ACC-1 and ACC-2). All but ACC-2 are mitochondrial enzymes. The biotin moiety is covalently bound to the epsilon amino group of a Lysine residue in each of these carboxylases in a domain 60-80 amino acids long. The domain is structurally similar among carboxylases from bacteria to mammals. There are four biotin-dependent carboxylases in mammals: those of propionyl-CoA (PCC), 3-methylcrotonyl-CoA (MCC), pyruvate (PC) and acetyl-CoA carboxylases (isoforms ACC-1 and ACC-2). All but ACC-2 are mitochondrial enzymes. The biotin moiety is covalently bound to the epsilon amino group of a Lys residue in each of these carboxylases in a domain 60-80 amino acids long. The domain is structurally similar among carboxylases from bacteria to mammals. Evidence is emerging that biotin participates in processes other than classical carboxylation reactions. Specifically, novel roles for biotin in cell signaling, gene expression, and chromatin structure have been identified in recent years. Human cells accumulate biotin by using both the sodium-dependent multivitamin transporter and monocarboxylate transporter 1. These transporters and other biotin-binding proteins partition biotin to compartments involved in biotin signaling: cytoplasm, mitochondria, and nuclei. The activity of cell signals such as biotinyl-AMP, Sp1 and Sp3, nuclear factor (NF)-kappaB, and receptor tyrosine kinases depends on biotin supply. Consistent with a role for biotin and its catabolites in ... Biotin is an enzyme co-factor present in minute amounts in every living cell. Biotin is also known as coenzyme R and vitamin H or B7. It occurs mainly bound to proteins or polypeptides and is abundant in liver, kidney, pancreas, yeast, and milk. Biotin has been recognized as an essential nutrient. Humans fulfill their biotin requirement through their diet through endogenous reutilization of biotin and perhaps through the capture of biotin generated in the intestinal flora. The utilization of biotin for covalent attachment to carboxylases and its reutilization through the release of carboxylase biotin after proteolytic degradation constitutes the biotin cycle. Biotin deficiency is associated with neurological manifestations, skin rash, hair loss, and metabolic disturbances that are thought to relate to the various carboxylase deficiencies (metabolic ketoacidosis with lactic acidosis). It has also been suggested that biotin deficiency is associated with protein malnutrition, and that marginal biotin deficiency in pregnant women may be teratogenic. Biotin acts as a carboxyl carrier in carboxylation reactions. There are four biotin-dependent carboxylases in mammals: those of propionyl-CoA (PCC), 3-methylcrotonyl-CoA (MCC), pyruvate (PC), and acetyl-CoA carboxylases (isoforms ACC-1 and ACC-2). All but ACC-2 are mitochondrial enzymes. The biotin moiety is covalently bound to the epsilon amino group of a lysine residue in each of these carboxylases in a domain 60-80 amino acids long. The domain is structurally similar among carboxylases from bacteria to mammals. Evidence is emerging that biotin participates in processes other than classical carboxylation reactions. Specifically, novel roles for biotin in cell signalling, gene expression, and chromatin structure have been identified in recent years. Human cells accumulate biotin by using both the sodium-dependent multivitamin transporter and monocarboxylate transporter 1. These transporters and other biotin-binding proteins partition biotin to compartments involved in biotin signalling: cytoplasm, mitochondria, and nuclei. The activity of cell signals such as biotinyl-AMP, Sp1 and Sp3, nuclear factor (NF)-kappaB, and receptor tyrosine kinases depends on biotin supply. Consistent with a role for biotin and its catabolites in modulating these cell signals, greater than 2000 biotin-dependent genes have been identified in various human tissues. Many biotin-dependent gene products play roles in signal transduction and localize to the cell nucleus, consistent with a role for biotin in cell signalling. Posttranscriptional events related to ribosomal activity and protein folding may further contribute to the effects of biotin on gene expression. Finally, research has shown that biotinidase and holocarboxylase synthetase mediate covalent binding of biotin to histones (DNA-binding proteins), affecting chromatin structure; at least seven biotinylation sites have been identified in human histones. Biotinylation of histones appears to play a role in cell proliferation, gene silencing, and the cellular response to DNA repair. Roles for biotin in cell signalling and chromatin structure are consistent with the notion that biotin has a unique significance in cell biology (PMID: 15992684, 16011464). Present in many foods; particularly rich sources include yeast, eggs, liver, certain fish (e.g. mackerel, salmon, sardines), soybeans, cauliflower and cow peas. Dietary supplement. Isolated from various higher plant sources, e.g. sweet corn seedlings and radish leaves An organic heterobicyclic compound that consists of 2-oxohexahydro-1H-thieno[3,4-d]imidazole having a valeric acid substituent attached to the tetrahydrothiophene ring. The parent of the class of biotins. [Raw Data] CB004_Biotin_pos_50eV_CB000006.txt [Raw Data] CB004_Biotin_pos_30eV_CB000006.txt [Raw Data] CB004_Biotin_pos_40eV_CB000006.txt [Raw Data] CB004_Biotin_pos_20eV_CB000006.txt [Raw Data] CB004_Biotin_pos_10eV_CB000006.txt [Raw Data] CB004_Biotin_neg_10eV_000006.txt [Raw Data] CB004_Biotin_neg_20eV_000006.txt Biosynthesis Biotin, synthesized in plants, is essential to plant growth and development.[22] Bacteria also synthesize biotin,[23] and it is thought that bacteria resident in the large intestine may synthesize biotin that is absorbed and utilized by the host organism.[18] Biosynthesis starts from two precursors, alanine and pimeloyl-CoA. These form 7-keto-8-aminopelargonic acid (KAPA). KAPA is transported from plant peroxisomes to mitochondria where it is converted to 7,8-diaminopelargonic acid (DAPA) with the help of the enzyme, BioA. The enzyme dethiobiotin synthetase catalyzes the formation of the ureido ring via a DAPA carbamate activated with ATP, creating dethiobiotin with the help of the enzyme, BioD, which is then converted into biotin which is catalyzed by BioB.[24] The last step is catalyzed by biotin synthase, a radical SAM enzyme. The sulfur is donated by an unusual [2Fe-2S] ferredoxin.[25] Depending on the species of bacteria, Biotin can be synthesized via multiple pathways.[24] Biotin (Vitamin B7) is a water-soluble B vitamin and serves as a coenzyme for five carboxylases in humans, involved in the synthesis of fatty acids, isoleucine, and valine, and in gluconeogenesis. Biotin is necessary for cell growth, the production of fatty acids, and the metabolism of fats and amino acids[1][2][3]. Biotin, vitamin B7 and serves as a coenzyme for five carboxylases in humans, involved in the synthesis of fatty acids, isoleucine, and valine, and in gluconeogenesis. Biotin is necessary for cell growth, the production of fatty acids, and the metabolism of fats and amino acids[1][2][3]. Biotin (Vitamin B7) is a water-soluble B vitamin and serves as a coenzyme for five carboxylases in humans, involved in the synthesis of fatty acids, isoleucine, and valine, and in gluconeogenesis. Biotin is necessary for cell growth, the production of fatty acids, and the metabolism of fats and amino acids[1][2][3].

Pyridoxal

C8H9NO3 (167.0582404)

Pyridoxal is a pyridinecarbaldehyde that is pyridine-4-carbaldehyde bearing methyl, hydroxy and hydroxymethyl substituents at positions 2, 3 and 5 respectively. Pyridoxal, also known as pyridoxaldehyde, belongs to the class of organic compounds known as pyridoxals and derivatives. Pyridoxals and derivatives are compounds containing a pyridoxal moiety, which consists of a pyridine ring substituted at positions 2, 3, 4, and 5 by a methyl group, a hydroxyl group, a carbaldehyde group, and a hydroxymethyl group, respectively. Pyridoxal is one form of vitamin B6. Pyridoxal exists in all living species, ranging from bacteria to humans. In humans, pyridoxal is involved in glycine and serine metabolism. Pyridoxal has been detected, but not quantified in several different foods, such as sourdoughs, lichee, arctic blackberries, watercress, and cottonseeds. Some medically relevant bacteria, such as those in the genera Granulicatella and Abiotrophia, require pyridoxal for growth. This nutritional requirement can lead to the culture phenomenon of satellite growth. In in vitro culture, these pyridoxal-dependent bacteria may only grow in areas surrounding colonies of bacteria from other genera ("satellitism") that are capable of producing pyridoxal. Pridoxal has a role as a cofactor, a human metabolite, a Saccharomyces cerevisiae metabolite, an Escherichia coli metabolite and a mouse metabolite.

Pyridoxamine

C8H12N2O2 (168.0898732)

Pyridoxamine is one form of vitamin B6. Chemically it is based on a pyridine ring structure, with hydroxyl, methyl, aminomethyl, and hydroxymethyl substituents. It differs from pyridoxine by the substituent at the 4-position. The hydroxyl at position 3 and aminomethyl group at position 4 of its ring endow pyridoxamine with a variety of chemical properties, including the scavenging of free radical species and carbonyl species formed in sugar and lipid degradation and chelation of metal ions that catalyze Amadori reactions. Pyridoxamine, also known as PM, belongs to the class of organic compounds known as pyridoxamine 5-phosphates. These are heterocyclic aromatic compounds containing a pyridoxamine that carries a phosphate group at the 5-position. Within humans, pyridoxamine participates in a number of enzymatic reactions. In particular, pyridoxamine can be converted into pyridoxal; which is mediated by the enzyme pyridoxine-5-phosphate oxidase. In addition, pyridoxamine can be converted into pyridoxamine 5-phosphate; which is catalyzed by the enzyme pyridoxal kinase. Pyridoxamine also inhibits the formation of advanced lipoxidation endproducts during lipid peroxidation reactions by reaction with dicarbonyl intermediates. In humans, pyridoxamine is involved in vitamin B6 metabolism. Outside of the human body, pyridoxamine has been detected, but not quantified in several different foods, such as nutmegs, sparkleberries, fennels, turmerics, and swiss chards. Pyridoxamine inhibits the Maillard reaction and can block the formation of advanced glycation endproducts, which are associated with medical complications of diabetes. Pyridoxamine is hypothesized to trap intermediates in the formation of Amadori products released from glycated proteins, possibly preventing the breakdown of glycated proteins by disrupting the catalysis of this process through disruptive interactions with the metal ions crucial to the redox reaction. One research study found that pyridoxamine specifically reacts with the carbonyl group in Amadori products, but inhibition of post-Amadori reactions (that can lead to advanced glycation endproducts) is due in much greater part to the metal chelation effects of pyridoxamine. The 4-aminomethyl form of vitamin B6. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate. -- Pubchem; Pyridoxamine is one of the compounds that can be called vitamin B6, along with Pyridoxal and Pyridoxine. -- Wikipedia [HMDB]. Pyridoxamine is found in many foods, some of which are cucumber, fox grape, millet, and teff. Acquisition and generation of the data is financially supported in part by CREST/JST. D018977 - Micronutrients > D014815 - Vitamins KEIO_ID P116 Pyridoxylamine is an advanced glycation end production (AGEs) and lipoxidation end products (ALEs) inhibitor, to protect against diabetes-induced retinal vascular lesions.

Pyridoxamine 5'-phosphate

C8H13N2O5P (248.05620580000001)

Pyridoxamine 5-phosphate belongs to the class of organic compounds known as pyridoxamine 5-phosphates. These are heterocyclic aromatic compounds containing a pyridoxamine that carries a phosphate group at the 5-position. Vitamin B6 is a water-soluble compound that was discovered in 1930s during nutrition studies on rats. The vitamin was named pyridoxine to indicate its structural homology to pyridine. Later it was shown that vitamin B6 could exist in two other, slightly different, chemical forms, termed pyridoxal and pyridoxamine. All three forms of vitamin B6 are precursors of an activated compound known as pyridoxal 5-phosphate (PLP), which plays a vital role as the cofactor of a large number of essential enzymes in the human body. Vitamin B6 is a water-soluble vitamin. The three major forms of vitamin B6 are pyridoxine (also known as pyridoxol), pyridoxal, and pyridoxamine, which are all converted in the liver to pyridoxal 5-phosphate (PLP) a cofactor in many reactions of amino acid metabolism. PLP also is necessary for the enzymatic reaction governing the release of glucose from glycogen. Vitamin B6 is a water-soluble compound that was discovered in 1930s during nutrition studies on rats. The vitamin was named pyridoxine to indicate its structural homology to pyridine. Later it was shown that vitamin B6 could exist in two other, slightly different, chemical forms, termed pyridoxal and pyridoxamine. All three forms of vitamin B6 are precursors of an activated compound known as pyridoxal 5-phosphate (PLP), which plays a vital role as the cofactor of a large number of essential enzymes in the human body. KEIO_ID P113; [MS3] KO009146 KEIO_ID P113; [MS2] KO009143 KEIO_ID P113

Pyridoxine

C8H11NO3 (169.0738896)

Pyridoxine, also known vitamin B6, is commonly found in food and is used as a dietary supplement. Pyridoxine is an essential nutrient, meaning the body cannot synthesize it, and it must be obtained from the diet. Sources in the diet include fruit, vegetables, and grain. Although pyridoxine and vitamin B6 are still frequently used as synonyms, especially by medical researchers, this practice is sometimes misleading (PMID: 2192605). Technically, pyridoxine is one of the compounds that can be called vitamin B6 or it is a member of the family of B6 vitamins. Healthy human blood levels of pyridoxine are 2.1 - 21.7 ng/mL. Pyridoxine is readily converted to pyridoxal phosphate which is a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids and aminolevulinic acid. Pyridoxine assists in the balancing of sodium and potassium as well as promoting red blood cell production. Therefore pyridoxine is required by the body to make amino acids, carbohydrates, and lipids. It is linked to cancer immunity and helps fight the formation of homocysteine. It has been suggested that pyridoxine might help children with learning difficulties, and may also prevent dandruff, eczema, and psoriasis. In addition, pyridoxine can help balance hormonal changes in women and aid in immune system. Lack of pyridoxine may cause anemia, nerve damage, seizures, skin problems, and sores in the mouth (Wikipedia). Deficiency of pyridoxine, though rare because of widespread distribution in foods, leads to the development of peripheral neuritis in adults and affects the central nervous system in children (DOSE - 3rd edition). As a supplement pyridoxine is used to treat and prevent pyridoxine deficiency, sideroblastic anaemia, pyridoxine-dependent epilepsy, certain metabolic disorders, problems from isoniazid, and certain types of mushroom poisoning. Pyridoxine in combination with doxylamine is used as a treatment for morning sickness in pregnant women. Found in rice husks, cane molasses, yeast, wheat germ and cod liver oils. Vitamin, dietary supplement, nutrient. Pyridoxine is one of the compounds that can be called vitamin B6, along with pyridoxal and pyridoxamine. It differs from pyridoxamine by the substituent at the 4 position. It is often used as pyridoxine hydrochloride. Pyridoxine in the urine is a biomarker for the consumption of soy products. Acquisition and generation of the data is financially supported in part by CREST/JST. A - Alimentary tract and metabolism > A11 - Vitamins D018977 - Micronutrients > D014815 - Vitamins COVID info from COVID-19 Disease Map KEIO_ID P053 Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS Pyridoxine (Pyridoxol) is a pyridine derivative. Pyridoxine exerts antioxidant effects in cell model of Alzheimer's disease via the Nrf-2/HO-1 pathway. Pyridoxine (Pyridoxol) is a pyridine derivative. Pyridoxine exerts antioxidant effects in cell model of Alzheimer's disease via the Nrf-2/HO-1 pathway.

Nicotinamide adenine dinucleotide phosphate

C21H30N7O17P3 (745.0911)

NADPH is the reduced form of NADP+, and NADP+ is the oxidized form of NADPH. Nicotinamide adenine dinucleotide phosphate (NADP) is a coenzyme composed of ribosylnicotinamide 5-phosphate (NMN) coupled with a pyrophosphate linkage to 5-phosphate adenosine 2,5-bisphosphate. NADP serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). NADP is formed through the addition of a phosphate group to the 2 position of the adenosyl nucleotide through an ester linkage (Dorland, 27th ed). This extra phosphate is added by the enzyme NAD+ kinase and removed via NADP+ phosphatase. NADP is also known as TPN (triphosphopyridine nucleotide) and it is an important cofactor used in anabolic reactions in all forms of cellular life. Examples include the Calvin cycle, cholesterol synthesis, fatty acid elongation, and nucleic acid synthesis (Wikipedia). Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5-phosphate (NMN) coupled by pyrophosphate linkage to the 5-phosphate adenosine 2,5-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed.) [HMDB]. NADPH is found in many foods, some of which are american pokeweed, rice, ginseng, and ostrich fern. COVID info from COVID-19 Disease Map Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS

Thiamine

[C12H17N4OS]+ (265.1123012)

Thiamine, also known as aneurin or vitamin B1, belongs to the class of organic compounds known as thiamines. Thiamines are compounds containing a thiamine moiety, which is structurally characterized by a 3-[(4-Amino-2-methyl-pyrimidin-5-yl)methyl]-4-methyl-thiazol-5-yl backbone. Thiamine exists in all living species, ranging from bacteria to plants to humans. Thiamine biosynthesis occurs in bacteria, some protozoans, plants, and fungi. Thiamine is a vitamin and an essential nutrient meaning the body cannot synthesize it, and it must be obtained from the diet. It is soluble in water and insoluble in alcohol. Thiamine decomposes if heated. Thiamine was first discovered in 1897 by Umetaro Suzuki in Japan when researching how rice bran cured patients of Beriberi. Thiamine was the first B vitamin to be isolated in 1926 and was first made in 1936. Thiamine plays a key role in intracellular glucose metabolism and it is thought that thiamine inhibits the effect of glucose and insulin on arterial smooth muscle cell proliferation. Thiamine plays an important role in helping the body convert carbohydrates and fat into energy. It is essential for normal growth and development and helps to maintain proper functioning of the heart and the nervous and digestive systems. Thiamine cannot be stored in the body; however, once absorbed, the vitamin is concentrated in muscle tissue. Thiamine has antioxidant, erythropoietic, cognition-and mood-modulatory, antiatherosclerotic, putative ergogenic, and detoxification activities. Natural derivatives of thiamine, such as thiamine monophosphate (ThMP), thiamine diphosphate (ThDP), also sometimes called thiamine pyrophosphate (TPP), thiamine triphosphate (ThTP), and adenosine thiamine triphosphate (AThTP), act as coenzymes in addition to performing unique biological functions. Thiamine deficiency can lead to beriberi, Wernicke–Korsakoff syndrome, optic neuropathy, Leighs disease, African seasonal ataxia (or Nigerian seasonal ataxia), and central pontine myelinolysis. In Western countries, thiamine deficiency is seen mainly in chronic alcoholism. Thiamine supplements or thiamine therapy can be used for the treatment of a number of disorders including thiamine and niacin deficiency states, Korsakovs alcoholic psychosis, Wernicke-Korsakov syndrome, delirium, and peripheral neuritis. In humans, thiamine is involved in the metabolic disorder called 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency. Outside of the human body, Thiamine is found in high quantities in whole grains, legumes, pork, fruits, and yeast and fish. Grain processing removes much of the thiamine content in grains, so in many countries cereals and flours are enriched with thiamine. Thiamine is an essential vitamin. It is found in many foods, some of which are atlantic croaker, wonton wrapper, cereals and cereal products, and turmeric. A - Alimentary tract and metabolism > A11 - Vitamins > A11D - Vitamin b1, plain and in combination with vitamin b6 and b12 > A11DA - Vitamin b1, plain Acquisition and generation of the data is financially supported in part by CREST/JST. D018977 - Micronutrients > D014815 - Vitamins KEIO_ID T056; [MS2] KO009294 KEIO_ID T056

Nicotinic acid mononucleotide

[C11H15NO9P]+ (336.048441)

Nicotinic acid mononucleotide, also known as nicotinate ribonucleotide, belongs to the class of organic compounds known as nicotinic acid nucleotides. These are pyridine nucleotides in which the pyridine base is nicotinic acid or a derivative thereof. Nicotinic acid mononucleotide is an extremely weak basic (essentially neutral) compound (based on its pKa). Nicotinic acid mononucleotide an intermediate in the cofactor biosynthesis and the nicotinate and nicotinamide metabolism pathways. It is a substrate for nicotinamide riboside kinase, ectonucleotide pyrophosphatase/phosphodiesterase, nicotinamide mononucleotide adenylyltransferase, 5-nucleotidase, nicotinate-nucleotide pyrophosphorylase, and 5(3)-deoxyribonucleotidase. Nicotinic acid mononucleotide is an intermediate in the metabolism of Nicotinate and nicotinamide. It is a substrate for Ectonucleotide pyrophosphatase/phosphodiesterase 2, Ectonucleotide pyrophosphatase/phosphodiesterase 1, Nicotinamide mononucleotide adenylyltransferase 3, Cytosolic 5-nucleotidase IA, Cytosolic 5-nucleotidase IB, Nicotinate-nucleotide pyrophosphorylase, 5(3)-deoxyribonucleotidase (cytosolic type), Cytosolic purine 5-nucleotidase, Nicotinamide mononucleotide adenylyltransferase 2, Ectonucleotide pyrophosphatase/phosphodiesterase 3, 5-nucleotidase, 5(3)-deoxyribonucleotidase (mitochondrial) and Nicotinamide mononucleotide adenylyltransferase 1. [HMDB] NaMN is the most common mononucleotide intermediate (a hub) in NAD biogenesis. For example, in E. coli all three pyridine precursors are converted into NaMN (Table 1 and Figure 3(a)). Qa produced by the de novo Asp–DHAP pathway (genes nadB and nadA) is converted into NaMN by QAPRT (gene nadC). Salvage of both forms of niacin proceeds via NAPRT (gene pncB) either directly upon or after deamidation by NMDSE (gene pncA). Overall, more than 90\% of approximately 680 analyzed bacterial genomes contain at least one of the pathways leading to the formation of NaMN. Most of them (∼480 genomes) have the entire set of nadBAC genes for NaMN de novo synthesis from Asp that are often clustered on the chromosome and/or are co-regulated by the same transcription factors (see Section 7.08.3.1.2). Among the examples provided in Table 1, F. tularensis (Figure 4(c)) has all three genes of this de novo pathway forming a single operon-like cluster and supporting the growth of this organism in the absence of any pyridine precursors in the medium. More than half the genomes with the Asp–DHAP pathway also contain a deamidating niacin salvage pathway (genes pncAB) as do many representatives of the α-, β-, and γ-Proteobacteria, Actinobacteria, and Bacillus/Clostridium group. As already emphasized, the genomic reconstruction approach provides an assessment of the metabolic potential of an organism, which may or may not be realized under given conditions. For example, E. coli and B. subtilis can utilize both de novo and PncAB Nm salvage pathways under the same growth conditions, whereas in M. tuberculosis (having the same gene pattern) the latter pathway was considered nonfunctional, so that the entire NAD pool is generated by the de novo NadABC route. However, a recent study demonstrated the functional activity of the Nm salvage pathway in vivo, under hypoxic conditions in infected macrophages.221 This study also implicated the two downstream enzymes of NAD synthesis (NAMNAT and NADSYN) as attractive chemotherapeutic targets to treat acute and latent forms of tuberculosis. In approximately 100 species, including many Cyanobacteria (e.g., Synechococcus spp.), Bacteroidetes (e.g., Chlorobium spp.) and Proteobacteria (e.g., Caulobacter crescentus, Zymomonas mobilis, Desulfovibrio spp., and Shewanella spp. representing α-, β-, δ-, and γ-groups, respectively) the Asp–DHAP pathway is the only route to NAD biogenesis. Among them, nearly all Helicobacter spp. (except H. hepaticus), contain only the two genes nadA and nadC but lack the first gene of the pathway (nadB), which is a likely subject of nonorthologous gene replacement. One case of NadB (ASPOX) replacement by the ASPDH enzyme in T. maritima (and methanogenic archaea) was discussed in Section 7.08.2.1. However, no orthologues of the established ASPDH could be identified in Helicobacter spp. as well as in approximately 15 other diverse bacterial species that have the nadAC but lack the nadB gene (e.g., all analyzed Corynebacterium spp. except for C. diphtheriae). Therefore, the identity of the ASPOX or ASPDH enzyme in these species is still unknown, representing one of the few remaining cases of ‘locally missing genes’220 in the NAD subsystem. All other bacterial species contain either both the nadA and nadB genes (plus nadC) or none. In a limited number of bacteria (∼20 species), mostly in the two distant groups of Xanthomonadales (within γ-Proteobacteria) and Flavobacteriales (within Bacteroidetes), the Asp–DHAP pathway of Qa synthesis is replaced by the Kyn pathway. As described in Section 7.08.2.1.2, four out of five enzymes (TRDOX, KYNOX, KYNSE, and HADOX) in the bacterial version of this pathway are close homologues of the respective eukaryotic enzymes, whereas the KYNFA gene is a subject of multiple nonorthologous replacements. Although the identity of one alternative form of KYNFA (gene kynB) was established in a group of bacteria that have a partial Kyn pathway for Trp degradation to anthranilate (e.g., in P. aeruginosa or B. cereus57), none of the known KYNFA homologues are present in Xanthomonadales or Flavobacteriales. In a few species (e.g., Salinispora spp.) a complete gene set of the Kyn pathway genes co-occurs with a complete Asp–DHAP pathway. Further experiments would be required to establish to what extent and under what conditions these two pathways contribute to Qa formation. As discussed, the QAPRT enzyme is shared by both de novo pathways, and a respective gene, nadC is always found in the genomes containing one or the other pathway. Similarly, gene nadC always co-occurs with Qa de novo biosynthetic genes with one notable exception of two groups of Streptococci, S. pneumonaie and S. pyogenes. Although all other members of the Lactobacillales group also lack the Qa de novo biosynthetic machinery and rely entirely on niacin salvage, only these two human pathogens contain a nadC gene. The functional significance of this ‘out of context’ gene is unknown, but it is tempting to speculate that it may be involved in a yet-unknown pathway of Qa salvage from the human host. Among approximately 150 bacterial species that lack de novo biosynthesis genes and rely on deamidating salvage of niacin (via NAPRT), the majority (∼100) are from the group of Firmicutes. Such a functional variant (illustrated for Staphylococcus aureus in Figure 4(b)) is characteristic of many bacterial pathogens, both Gram-positive and Gram-negative (e.g., Brucella, Bordetella, and Campylobacter spp. from α-, β-, and δ-Proteobacteria, Borrelia, and Treponema spp. from Spirochaetes). Most of the genomes in this group contain both pncA and pncB genes that are often clustered on the chromosome and/or are co-regulated (see Section 7.08.3.1.2). In some cases (e.g., within Mollicutes and Spirochaetales), only the pncB, but not the pncA gene, can be reliably identified, suggesting that either of these species can utilize only the deamidated form of niacin (Na) or that some of them contain an alternative (yet-unknown) NMASE. Although the nondeamidating conversion of Nm into NMN (via NMPRT) appears to be present in approximately 50 bacterial species (mostly in β- and γ-Proteobacteria), it is hardly ever the only route of NAD biogenesis in these organisms. The only possible exception is observed in Mycoplasma genitalium and M. pneumoniae that contain the nadV gene as the only component of pyridine mononucleotide biosynthetic machinery. In some species (e.g., in Synechocystes spp.), the NMPRT–NMNAT route is committed primarily to the recycling of endogenous Nm. On the other hand, in F. tularensis (Figure 4(c)), NMPRT (gene nadV) together with NMNAT (of the nadM family) constitute the functional nondeamidating Nm salvage pathway as it supports the growth of the nadE′-mutant on Nm but not on Na (L. Sorci et al., unpublished). A similar nondeamidating Nm salvage pathway implemented by NMPRT and NMNAT (of the nadR family) is present in some (but not all) species of Pasteurellaceae in addition to (but never instead of) the RNm salvage pathway (see below), as initially demonstrated for H. ducreyi.128 A two-step conversion of NaMN into NAD via a NaAD intermediate (Route I in Figure 2) is present in the overwhelming majority of bacteria. The signature enzyme of Route I, NAMNAT of the NadD family is present in nearly all approximately 650 bacterial species that are expected to generate NaMN via de novo or salvage pathways (as illustrated by Figures 3(a) and 3(b)). All these species, without a single exception, also contain NADSYN (encoded by either a short or a long form of the nadE gene), which is required for this route. The species that lack the NadD/NadE signature represent several relatively rare functional variants, including: 1. Route I of NAD synthesis (NaMN → NaAD → NAD) variant via a bifunctional NAMNAT/NMNAT enzyme of the NadM family is common for archaea (see Section 7.08.3.2), but it appears to be present in only a handful of bacteria, such as Acinetobacter, Deinococcus, and Thermus groups. Another unusual feature of the latter two groups is the absence of the classical NADKIN, a likely subject of a nonorthologous replacement that remains to be elucidated. 2. Route II of NAD synthesis (NaMN → NMN → NAD). This route is implemented by a combination of the NMNAT of either the NadM family (as in F. tularensis) or the NadR family (as in M. succinoproducens and A. succinogenes) with NMNSYN of the NadE′ family. The case of F. tularensis described in Section 7.08.2.4 is illustrated in Figure 3(b). The rest of the NAD biosynthetic machinery in both species from the Pasteurellaceae group, beyond the shared Route II, is remarkably different from that in F. tularensis. Instead of de novo biosynthesis, they harbor a Na salvage pathway via NAPRT encoded by a pncB gene that is present in a chromosomal cluster with nadE′. Neither of these two genes are present in other Pasteurellaceae that lack the pyridine carboxylate amidation machinery (see below). 3. Salvage of RNm (RNm → NMN → NAD). A genomic signature of this pathway, a combination of the PnuC-like transporter and a bifunctional NMNAT/RNMKIN of the NadR family, is present in many Enterobacteriaceae and in several other diverse species (e.g., in M. tuberculosis). However, in H. influenzae (Figure 3(d)) and related members of Pasteurellaceae, it is the only route of NAD biogenesis. As shown in Table 1, H. influenzae as well as many other members of this group have lost nearly all components of the rich NAD biosynthetic machinery that are present in their close phylogenetic neighbors (such as E. coli and many other Enterobacteriaceae). This pathway is an ultimate route for utilization of the so called V-factors (NADP, NAD, NMN, or RNm) that are required to support growth of H. influenzae. It was established that all other V-factors are degraded to RNm by a combination of periplasmic- and membrane-associated hydrolytic enzymes.222 Although PnuC was initially considered an NMN transporter,223 its recent detailed analysis in both H. influenzae and Salmonella confirmed that its actual physiological function is in the uptake of RNm coupled with the phosphorylation of RNM to NMN by RNMKIN.17,148,224 As already mentioned, H. ducreyi and several other V-factor-independent members of the Pasteurellaceae group (H. somnus, Actinobacillus pleuropneumoniae, and Actinomycetemcomitans) harbor the NMNAT enzyme (NadV) that allows them to grow in the presence of Nm (but not Na) in the medium (Section 7.08.2.2). 4. Uptake of the intact NAD. Several groups of phylogenetically distant intracellular endosymbionts with extremely truncated genomes contain only a single enzyme, NADKIN, from the entire subsystem. Among them are all analyzed species of the Wolbachia, Rickettsia, and Blochmannia groups. These species are expected to uptake and utilize the intact NAD from their host while retaining the ability to convert it into NADP. Among all analyzed bacteria, only the group of Chlamydia does not have NADKIN and depends on the salvage of both NAD and NADP via a unique uptake system.157 A comprehensive genomic reconstruction of the metabolic potential (gene annotations and asserted pathways) across approximately 680 diverse bacterial genomes sets the stage for the accurate cross-genome projection and prediction of regulatory mechanisms that control the realization of this potential in a variety of species and growth conditions. In the next section, we summarize the recent accomplishments in the genomic reconstruction of NAD-related regulons in bacteria. Nicotinic acid mononucleotide. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=321-02-8 (retrieved 2024-06-29) (CAS RN: 321-02-8). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0).

Nicotinic acid adenine dinucleotide

[C21H27N6O15P2]+ (665.1009592)

Nicotinic acid adenine dinucleotide, also known as deamido-NAD or NAAD, belongs to the class of organic compounds known as (5->5)-dinucleotides. These are dinucleotides where the two bases are connected via a (5->5)-phosphodiester linkage. NAAD is possibly soluble (in water) and a strong basic compound (based on its pKa). NAAD exists in all living species, ranging from bacteria to humans. L-Glutamine and NAAD can be converted into L-glutamic acid and NAD; which is catalyzed by the enzyme glutamine-dependent nad(+) synthetase. In humans, NAAD is involved in the nicotinate and nicotinamide metabolism pathway. NAAD is also involved in the metabolic disorder called succinic semialdehyde dehydrogenase deficiency. Outside of the human body, NAAD has been detected, but not quantified in, several different foods, such as japanese walnuts, cauliflowers, sparkleberries, komatsuna, and macadamia nut (m. tetraphylla). This could make NAAD a potential biomarker for the consumption of these foods. NAAD is the product of the degradation of Nicotinic acid adenine dinucleotide phosphate (NAADP) by a Ca2+-sensitive phosphatase. NAADP is a Ca2+-mobilizing second messenger which is synthesized, in response to extracellular stimuli, via the base-exchange reaction by an ADP-ribosyl cyclase (ARC) family members (such as CD38). NAADP binds to and opens Ca2+ channels on intracellular organelles, thereby increasing the intracellular Ca2+ concentration which, in turn, modulates a variety of cellular processes. Structurally, NAADP it is a dinucleotide that only differs from the house-keeping enzyme cofactor, NADP, by a hydroxyl group (replacing the nicotinamide amino group) and yet this minor modification converts it into the most potent Ca2+-mobilizing second messenger yet described. NAADP may also be broken down to 2-phosphoadenosine diphosphoribose (ADPRP) by CD38 or reduced to NAADPH. Deamido-nad(+), also known as deamidonicotinamide adenine dinucleoetide, is a member of the class of compounds known as (5->5)-dinucleotides (5->5)-dinucleotides are dinucleotides where the two bases are connected via a (5->5)-phosphodiester linkage. Deamido-nad(+) is slightly soluble (in water) and a moderately acidic compound (based on its pKa). Deamido-nad(+) can be found in a number of food items such as garden tomato, sea-buckthornberry, pitanga, and japanese walnut, which makes deamido-nad(+) a potential biomarker for the consumption of these food products. Deamido-nad(+) exists in all living species, ranging from bacteria to humans. In humans, deamido-nad(+) is involved in few metabolic pathways, which include glutamate metabolism, homocarnosinosis, and nicotinate and nicotinamide metabolism. Deamido-nad(+) is also involved in few metabolic disorders, which include 2-hydroxyglutric aciduria (D and L form), 4-hydroxybutyric aciduria/succinic semialdehyde dehydrogenase deficiency, hyperinsulinism-hyperammonemia syndrome, and succinic semialdehyde dehydrogenase deficiency.

Pantetheine

C11H22N2O4S (278.1300212)

Pantetheine is the mercaptoethyl conjugated amide analogue of pantothenic acid (Vitamin B5). The dimer of this compound, pantethine is more commonly known, and is considered to be a more potent form of vitamin B5 than pantothenic acid. Pantetheine is an intermediate in the production of Coenzyme A by the body. An intermediate in the pathway of coenzyme A formation in mammalian liver and some microorganisms. Pantetheine is the mercaptoethyl conjugated amide analogue of pantothenic acid (Vitamin B5). The dimer of this compound, pantethine is more commonly known, and is considered to be a more potent form of vitamin B5 than pantothenic acid. Pantetheine is an intermediate in the production of Coenzyme A by the body. COVID info from COVID-19 Disease Map Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS

Water

H2O (18.0105642)

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

Oxygen

O2 (31.98983)

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

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

zinc ion

Zn+2 (63.929145)

A - Alimentary tract and metabolism > A16 - Other alimentary tract and metabolism products > A16A - Other alimentary tract and metabolism products > A16AB - Enzymes D000970 - Antineoplastic Agents > D059003 - Topoisomerase Inhibitors > D059004 - Topoisomerase I Inhibitors C307 - Biological Agent > C29726 - Enzyme Replacement or Supplement Agent D004791 - Enzyme Inhibitors

Tetrahydrofolic acid

C19H23N7O6 (445.1709738)

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

Pyridoxine 5'-phosphate

C8H12NO6P (249.0402222)

Pyridoxine phosphate, also known as pyridoxine 5-phosphoric acid or pyridoxine 5-(dihydrogen phosphate), is a member of the class of compounds known as pyridoxine-5-phosphates. Pyridoxine-5-phosphates are pyridoxines that carry a phosphate group at the 5-position. Pyridoxine phosphate is slightly soluble (in water) and a moderately acidic compound (based on its pKa). Pyridoxine phosphate can be found primarily in blood. Within the cell, pyridoxine phosphate is primarily located in the cytoplasm (predicted from logP). Pyridoxine phosphate exists in all living species, ranging from bacteria to humans. In humans, pyridoxine phosphate is involved in the vitamin B6 metabolism. Pyridoxine phosphate is also involved in hypophosphatasia, which is a metabolic disorder. Moreover, pyridoxine phosphate is found to be associated with obesity. Pyridoxine 5-phosphate is a substrate for Pyridoxine-5-phosphate oxidase and Pyridoxal kinase.

5-Methyltetrahydropteroyltri-L-glutamic acid

C30H39N9O12 (717.2718054)

5-Methyltetrahydropteroyltri-L-glutamic acid (CAS: 13061-55-7) is formed during the reaction between the carbonyl group of 5-methyltetrahydropteroate and the amine group on one end of three replicates of glutamate. It is involved in several pathways as a product of enzymatic reduction such as in tetrahydrofolate biosynthesis II and methionine biosynthesis I, II, and III. It is also involved in several pathways as a product of enzymatic oxidation such as in the pathways folate polyglutamylation I and carbon tetrachloride degradation II. In humans, this compound is produced by the bacteria in the gut and may be found in feces or urine. 5-Methyltetrahydropteroyltri-L-glutamate is formed under reaction between carbonyl group of 5-Methyltetrahydropteroate and amine group on one end of three replicates of glutamate. It is involved in several pathways such as tetrahydrofolate biosynthesis II, methionine biosynthesis I,II,III as a product of enzymatic reduction; while in pathways folate polyglutamylation I and carbon tetrachloride degradation II as a product of enzymatic oxidation. [HMDB]. 5-Methyltetrahydropteroyltri-L-glutamate is found in many foods, some of which are common cabbage, chives, lime, and garden rhubarb.

(S)-Nadphx

C21H32N7O18P3 (763.1016642000001)

A tetrahydronicotinamide adenine dinucleotide obtained by formal stereo- and regioselective hydration across the 2,3-double bond in the nicotinyl ring of NADPH, with the hydroxy group located at position 2, having (S)-configuration.

Tetrahydrofolyl-[Glu](2)

C24H30N8O9 (574.213565)

Tetrahydrofolyl-[Glu](n) is involved in the folate biosynthesis pathway. Tetrahydrofolyl-[Glu](n) can be reversibly converted into Tetrahydrofolyl-[Glu](2) by folylpolyglutamate synthase [EC:6.3.2.17]. Tetrahydrofolyl-[Glu](n) can be irreversibly converted into tetrahydrofolate by gamma-glutamyl hydrolase [EC:3.4.19.9]. [HMDB] Tetrahydrofolyl-[Glu](n) is involved in the folate biosynthesis pathway. Tetrahydrofolyl-[Glu](n) can be reversibly converted into Tetrahydrofolyl-[Glu](2) by folylpolyglutamate synthase [EC:6.3.2.17]. Tetrahydrofolyl-[Glu](n) can be irreversibly converted into tetrahydrofolate by gamma-glutamyl hydrolase [EC:3.4.19.9].

Manganous cation

Mn+2 (54.938046)

Ammonium

H4N+ (18.0343724)

Ammonium, also known as ammonium(1+) or nh4+, 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. Ammonium can be found in a number of food items such as irish moss, sago palm, sorghum, and malabar spinach, which makes ammonium a potential biomarker for the consumption of these food products. Ammonium can be found primarily in blood and sweat. Ammonium exists in all living species, ranging from bacteria to humans. In humans, ammonium is involved in the the oncogenic action of 2-hydroxyglutarate. Ammonium is also involved in a couple of metabolic disorders, which include the oncogenic action of d-2-hydroxyglutarate in hydroxygluaricaciduria and the oncogenic action of l-2-hydroxyglutarate in hydroxygluaricaciduria. Moreover, ammonium is found to be associated with n-acetylglutamate synthetase deficiency. The ammonium cation is a positively charged polyatomic ion with the chemical formula NH+ 4. It is formed by the protonation of ammonia (NH3). Ammonium is also a general name for positively charged or protonated substituted amines and quaternary ammonium cations (NR+ 4), where one or more hydrogen atoms are replaced by organic groups (indicated by R) . Ammonium is an important source of nitrogen for many plant species, especially those growing on hypoxic soils. However, it is also toxic to most crop species and is rarely applied as a sole nitrogen source. The ammonium (more obscurely: aminium) cation is a positively charged polyatomic cation with the chemical formula NH4+. It is formed by the protonation of ammonia (NH3). Ammonium is also a general name for positively charged or protonated substituted amines and quaternary ammonium cations (NR4+), where one or more hydrogen atoms are replaced by organic radical groups (indicated by R). Ammonium is found to be associated with N-acetylglutamate synthetase deficiency, which is an inborn error of metabolism.

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])

(R)-Nadphx

C21H32N7O18P3 (763.1016642000001)

A tetrahydronicotinamide adenine dinucleotide obtained by formal stero- and regioselective hydration across the 2,3-double bond in the nicotinyl ring of NADPH, with the hydroxy group located at position 2, having (R)-configuration.

(2S)-2-[[(4S)-4-[[(4S)-4-[[4-[[(6R)-2-amino-4-oxo-5,6,7,8-tetrahydro-3H-pteridin-6-yl]methyl-formylamino]benzoyl]amino]-4-carboxybutanoyl]amino]-4-carboxybutanoyl]amino]pentanedioic acid

C30H37N9O13 (731.2510712)

formate

CHO2- (44.997654600000004)

Formate, also known as formic acid or methanoic acid, is a member of the class of compounds known as carboxylic acids. Carboxylic acids are compounds containing a carboxylic acid group with the formula -C(=O)OH. Formate is soluble (in water) and a weakly acidic compound (based on its pKa). Formate can be found in a number of food items such as mammee apple, chicory roots, malabar spinach, and grapefruit, which makes formate a potential biomarker for the consumption of these food products. Formate (IUPAC name: methanoate) is the anion derived from formic acid. Its formula is represented in various equivalent ways: CHOO‚àí or HCOO‚àí or HCO2‚àí. It is the product of deprotonation of formic acid. It is the simplest carboxylate anion. A formate (compound) is a salt or ester of formic acid . Formate, also known as formic acid or methanoic acid, is a member of the class of compounds known as carboxylic acids. Carboxylic acids are compounds containing a carboxylic acid group with the formula -C(=O)OH. Formate is soluble (in water) and a weakly acidic compound (based on its pKa). Formate can be found in a number of food items such as mammee apple, chicory roots, malabar spinach, and grapefruit, which makes formate a potential biomarker for the consumption of these food products. Formate (IUPAC name: methanoate) is the anion derived from formic acid. Its formula is represented in various equivalent ways: CHOO− or HCOO− or HCO2−. It is the product of deprotonation of formic acid. It is the simplest carboxylate anion. A formate (compound) is a salt or ester of formic acid .

Nicotinamide adenine dinucleotide

C21H26N7O14P2- (662.1012936000001)

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Coenzyme II

C21H25N7O17P3-3 (740.051977)

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5-Phosphoribosyl 1-pyrophosphate

C5H8O14P3-5 (384.9126958)

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Hydrogen phosphate

HO4P-2 (95.96124760000001)

Pyridoxal 5-phosphate(2-)

C8H8NO6P-2 (245.0089238)

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[Hydroxy(oxido)phosphoryl] phosphate

HO7P2-3 (174.9197556)

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(2S)-2-azaniumylpropanoate

C3H7NO2 (89.0476762)

D,L-Cysteine

C3H7NO2S (121.0197482)

NADPH(4-)

C21H26N7O17P3-4 (741.0598016)

[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-oxidophosphoryl]oxy-oxidophosphoryl] phosphate

C10H12N5O13P3-4 (502.9644492)

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Adenosine-diphosphate

C10H12N5O10P2-3 (424.0059412)

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Adenosine-5-monophosphate(2-)

C10H12N5O7P-2 (345.0474332)

Thiamine(1+) diphosphate(3-)

C12H16N4O7P2S-2 (422.0214926)

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L-glutamate(1-)

C5H8NO4- (146.0453308)

An alpha-amino-acid anion that is the conjugate base of L-glutamic acid, having anionic carboxy groups and a cationic amino group

7,8-Dihydrofolate

C19H19N7O6-2 (441.1396754)

D-pantetheine 4-phosphate(2-)

C11H21N2O7PS-2 (356.08070460000005)

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5-Methyltetrahydrofolate(2-)

C20H23N7O6-2 (457.1709738)

(2S)-5-amino-2-ammonio-5-oxopentanoate

C5H10N2O3 (146.069139)

10-Formyltetrahydrofolate dianion

C20H21N7O7-2 (471.1502396)

5,10-methenyltetrahydrofolate tri-L-glutamate

C30H32N9O12-3 (710.2170332)

2-[[4-(3-Amino-1-oxo-2,5,6,6a,7,9-hexahydroimidazo[1,5-f]pteridin-8-yl)benzoyl]amino]pentanedioate

C20H21N7O6-2 (455.15532460000003)