This pathway is part of a major route of the degradation of L-tryptophan. It begins with 2-amino-3-carboxymuconate-6-semialdehyde which is generated from L-tryptophan degradation. The 2-amino-3-carboxymuconate-6-semialdehyde first is acted upon by a decarboxylase, forming 2-aminomuconic acid semialdehyde, which is then dehydrogenated by 2-aminomuconic semialdehyde dehydrogenase to form 2-aminomuconic acid. An unknown protein forms a 2-aminomuconate deaminase which forms (3E)-2-oxohex-3-enedioate, and a second unknown protein forms a 2-aminomuconate reductase, which forms oxoadipic acid from (3E)-2-oxohex-3-enedioate. Finally, within the mitochondria, oxoadipic acid is dehydrogenated and a coenzyme A is attached by the organelle’s oxoglutarate dehydrogenase complex, forming glutaryl-CoA. Glutaryl-CoA can then be further degraded.


ATP

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).


Alanine

Alanine is a non-essential amino acid made in the body from either the conversion of the carbohydrate pyruvate or the breakdown of DNA and the dipeptides carnosine and anserine. It is highly concentrated in muscle and is one of the most important amino acids released by muscle, functioning as a major energy source. Plasma alanine is often decreased when the BCAA (branched-chain amino acids) are deficient. This finding may relate to muscle metabolism. Alanine is highly concentrated in meat products and other high-protein foods like wheat germ and cottage cheese. Alanine is an important participant as well as a regulator of glucose metabolism. Alanine levels parallel blood sugar levels in both diabetes and hypoglycemia, and alanine reduces both severe hypoglycemia and the ketosis of diabetes. It is an important amino acid for lymphocyte reproduction and immunity. Alanine therapy has helped dissolve kidney stones in experimental animals. Normal alanine metabolism, like that of other amino acids, is highly dependent upon enzymes that contain vitamin B6. Alanine, like GABA, taurine, and glycine, is an inhibitory neurotransmitter in the brain (http://www.dcnutrition.com/AminoAcids/). L-Alanine has been found to be associated with glucagon deficiency, which is an inborn error of metabolism.

(2s)-2-aminopropanoate
(2s)-2-aminopropanoic acid
(s)-(+)-alanine
(s)-2-aminopropanoate
(s)-2-aminopropanoic acid
(s)-2-amino-propanoate
(s)-2-amino-propanoic acid
(s)-alanine
2-aminopropanoate
2-aminopropanoic acid
2-aminopropionate
2-aminopropionic acid
2-ammoniopropanoate
2-ammoniopropanoic acid
Ala
Alanine
L-(+)-alanine
L-2-aminopropanoate
L-2-aminopropanoic acid
L-2-aminopropionate
L-2-aminopropionic acid
L-a-alanine
L-a-aminopropionate
L-a-aminopropionic acid
L-alpha-alanine
L-alpha-aminopropionate
L-alpha-aminopropionic acid
A-alanine
A-aminopropionate
A-aminopropionic acid
Alpha-alanine
Alpha-aminopropanoate
Alpha-aminopropanoic acid
Alpha-aminopropionate
Alpha-aminopropionic acid
A
L-alanin
L-α-alanine


Adenosine

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.

Adenosine 5'-(dihydrogen phosphoric acid)


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

(4-)diphosphoric acid ion
(p2o74-)diphosphate
Diphosphate
Diphosphoric acid
Ppi
Pyrometaphosphate
Pyrophosphate
Pyrophosphate tetraanion
Pyrophosphate(4-) ion
[o3popo3](4-)
Diphosphat
P2o7(4-)
Pyrophosphat
Pyrophosphate ion
Phosphonato phosphoric acid
Pyrophosphoric acid
Pyrophosphoric acid ion


Velmanase alfa

Zinc is an essential element, necessary for sustaining all life.Physiologically, it exists as an ion in the body. It is estimated that 3000 of the hundreds of thousands of proteins in the human body contain zinc prosthetic groups. In addition, there are over a dozen types of cells in the human body that secrete zinc ions, and the roles of these secreted zinc signals in medicine and health are now being actively studied. Intriguingly, brain cells in the mammalian forebrain are one type of cell that secretes zinc, along with its other neuronal messenger substances. Cells in the salivary gland, prostate, immune system and intestine are other types that secrete zinc. Obtaining a sufficient zinc intake during pregnancy and in young children is a problem, especially among those who cannot afford a good and varied diet. Brain development is stunted by zinc deficiency in utero and in youth. Zinc is an activator of certain enzymes, such as carbonic anhydrase. Carbonic anhydrase is important in the transport of carbon dioxide in vertebrate blood. Even though zinc is an essential requirement for a healthy body, too much zinc can be harmful. Excessive absorption of zinc can also suppress copper and iron absorption. The free zinc ion in solution is highly toxic to plants, invertebrates, and even vertebrate fish. The Free Ion Activity Model (FIAM) is well-established in the literature, and shows that just micromolar amounts of the free ion kills some organisms.

Zinc
Zinc ion
Dietary zinc
Zinc cation
Zinc, ion (zn2+)
Zn(ii)
Zn(2+)
Zn2+


Oxogluric acid

Oxoglutaric acid, also known as alpha-ketoglutarate, alpha-ketoglutaric acid, AKG, or 2-oxoglutaric acid, is classified as a gamma-keto acid or a gamma-keto acid derivative. gamma-Keto acids are organic compounds containing an aldehyde substituted with a keto group on the C4 carbon atom. alpha-Ketoglutarate is considered to be soluble (in water) and acidic. alpha-Ketoglutarate is a key molecule in the TCA cycle, playing a fundamental role in determining the overall rate of this important metabolic process (PMID: 26759695). In the TCA cycle, AKG is decarboxylated to succinyl-CoA and carbon dioxide by AKG dehydrogenase, which functions as a key control point of the TCA cycle. Additionally, AKG can be generated from isocitrate by oxidative decarboxylation catalyzed by the enzyme known as isocitrate dehydrogenase (IDH). In addition to these routes of production, AKG can be produced from glutamate by oxidative deamination via glutamate dehydrogenase, and as a product of pyridoxal phosphate-dependent transamination reactions (mediated by branched-chain amino acid transaminases) in which glutamate is a common amino donor. AKG is a nitrogen scavenger and a source of glutamate and glutamine that stimulates protein synthesis and inhibits protein degradation in muscles. In particular, AKG can decrease protein catabolism and increase protein synthesis to enhance bone tissue formation in skeletal muscles (PMID: 26759695). Interestingly, enteric feeding of AKG supplements can significantly increase circulating plasma levels of hormones such as insulin, growth hormone, and insulin-like growth factor-1 (PMID: 26759695). It has recently been shown that AKG can extend the lifespan of adult C. elegans by inhibiting ATP synthase and TOR (PMID: 24828042). In combination with molecular oxygen, alpha-ketoglutarate is required for the hydroxylation of proline to hydroxyproline in the production of type I collagen. A recent study has shown that alpha-ketoglutarate promotes TH1 differentiation along with the depletion of glutamine thereby favouring Treg (regulatory T-cell) differentiation (PMID: 26420908). alpha-Ketoglutarate has been found to be associated with fumarase deficiency, 2-ketoglutarate dehydrogenase complex deficiency, and D-2-hydroxyglutaric aciduria, which are all inborn errors of metabolism (PMID: 8338207).

2-ketoglutarate
2-ketoglutaric acid
2-oxo-1,5-pentanedioate
2-oxo-1,5-pentanedioic acid
2-oxoglutarate
2-oxoglutaric acid
2-oxopentanedioate
2-oxopentanedioic acid
Oxoglutarate
Alpha-ketoglutaric acid
Oxoglutaric acid
A-ketoglutarate
A-ketoglutaric acid
Alpha-ketoglutarate
α-ketoglutarate
α-ketoglutaric acid


Glutamic acid

Glutamic acid (Glu), also referred to as glutamate (the anion), is one of the 20 proteinogenic amino acids. It is not among the essential amino acids. Glutamate is a key molecule in cellular metabolism. In humans, dietary proteins are broken down by digestion into amino acids, which serves as metabolic fuel or other functional roles in the body. Glutamate is the most abundant fast excitatory neurotransmitter in the mammalian nervous system. At chemical synapses, glutamate is stored in vesicles. Nerve impulses trigger release of glutamate from the pre-synaptic cell. In the opposing post-synaptic cell, glutamate receptors, such as the NMDA receptor, bind glutamate and are activated. Because of its role in synaptic plasticity, it is believed that glutamic acid is involved in cognitive functions like learning and memory in the brain. Glutamate transporters are found in neuronal and glial membranes. They rapidly remove glutamate from the extracellular space. In brain injury or disease, they can work in reverse and excess glutamate can accumulate outside cells. This process causes calcium ions to enter cells via NMDA receptor channels, leading to neuronal damage and eventual cell death, and is called excitotoxicity. The mechanisms of cell death include: * Damage to mitochondria from excessively high intracellular Ca2+. * Glu/Ca2+-mediated promotion of transcription factors for pro-apoptotic genes, or downregulation of transcription factors for anti-apoptotic genes. Excitotoxicity due to glutamate occurs as part of the ischemic cascade and is associated with stroke and diseases like amyotrophic lateral sclerosis, lathyrism, and Alzheimer's disease. glutamic acid has been implicated in epileptic seizures. Microinjection of glutamic acid into neurons produces spontaneous depolarization around one second apart, and this firing pattern is similar to what is known as paroxysmal depolarizing shift in epileptic attacks. This change in the resting membrane potential at seizure foci could cause spontaneous opening of voltage activated calcium channels, leading to glutamic acid release and further depolarization. (http://en.wikipedia.org/wiki/Glutamic_acid).

(2s)-2-aminopentanedioate
(2s)-2-aminopentanedioic acid
(s)-(+)-glutamate
(s)-(+)-glutamic acid
(s)-2-aminopentanedioate
(s)-2-aminopentanedioic acid
(s)-glutamate
(s)-glutamic acid
1-amino-propane-1,3-dicarboxylate
1-amino-propane-1,3-dicarboxylic acid
1-aminopropane-1,3-dicarboxylate
1-aminopropane-1,3-dicarboxylic acid
2-aminoglutarate
2-aminoglutaric acid
2-aminopentanedioate
2-aminopentanedioic acid
Aciglut
Aminoglutarate
Aminoglutaric acid
E
Glt
Glu
Glusate
Glut
Glutacid
Glutamicol
Glutamidex
Glutaminate
Glutaminic acid
Glutaminol
Glutaton
L-(+)-glutamate
L-(+)-glutamic acid
L-glu
L-glutamate
L-glutaminate
L-glutaminic acid
L-a-aminoglutarate
L-a-aminoglutaric acid
L-alpha-aminoglutarate
L-alpha-aminoglutaric acid
A-aminoglutarate
A-aminoglutaric acid
A-glutamate
A-glutamic acid
Alpha-aminoglutarate
Alpha-aminoglutaric acid
Alpha-glutamate
Alpha-glutamic acid
Acide glutamique
Acido glutamico
Acidum glutamicum
Glutamate
Glutamic acid
L-glutaminsaeure


Pyruvic acid

Pyruvic acid is an intermediate compound in the metabolism of carbohydrates, proteins, and fats. In thiamine deficiency, its oxidation is retarded and it accumulates in the tissues, especially in nervous structures. (From Stedman, 26th ed.) Biological Source: Intermediate in primary metabolism including fermentation processes. Present in muscle in redox equilibrium with Lactic acid. A common constituent, as a chiral cyclic acetal linked to saccharide residues, of bacterial polysaccharides. Isolated from cane sugar fermentation broth and peppermint. Constituent of Bauhinia purpurea, Cicer arietinum (chickpea), Delonix regia, Pisum sativum (pea) and Trigonella caerulea (sweet trefoil) Use/Importance: Reagent for regeneration of carbonyl compdounds from semicarbazones, phenylhydrazones and oximes. Flavoring ingredient (Dictionary of Organic Compounds).

2-oxopropanoate
2-oxopropanoic acid
2-oxopropionate
2-oxopropionic acid
Acetylformate
Acetylformic acid
Bts
Pyroracemate
Pyroracemic acid
Pyruvate
A-ketopropionate
A-ketopropionic acid
Alpha-ketopropionate
Alpha-ketopropionic acid
2-ketopropionic acid
2-oxopropansaeure
2-oxopropionsaeure
Acide pyruvique
Alpha-oxopropionsaeure
Brenztraubensaeure
Ch3cocooh
2-ketopropionate
α-ketopropionate
α-ketopropionic acid
A-oxopropionsaeure
α-oxopropionsaeure


Pyridoxal phosphate

This is the active form of vitamin B6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (pyridoxamine). -- Pubchem; Pyridoxal-phosphate (PLP, pyridoxal-5'-phosphate) is a cofactor of many enzymatic reactions. It is the active form of vitamin B6 which comprises three natural organic compounds, pyridoxal, pyridoxamine and pyridoxine. -- Wikipedia.

Phosphoric acid mono-(4-formyl-5-hydroxy-6-methyl-pyridin-3-ylmethyl) ester

Pyridoxal 5'-(dihydrogen phosphoric acid)


Bicarbonate Ion

Bicarbonate, or hydrogen carbonate, is a simple single carbon molecule that plays surprisingly important roles in diverse biological processes. Among these are photosynthesis, the Krebs cycle, whole-body and cellular pH regulation, and volume regulation. Since bicarbonate is charged it is not permeable to lipid bilayers. Mammalian membranes thus contain bicarbonate transport proteins to facilitate the specific transmembrane movement of HCO3(-). Bicarbonate ion is an anion that consists of one central carbon atom surrounded by three oxygen atoms in a trigonal planar arrangement, with a hydrogen atom attached to one of the oxygens. The bicarbonate ion carries a negative one formal charge and is the conjugate base of carbonic acid, H2CO3. The carbonate radical is an elusive and strong one-electron oxidant. Bicarbonate in equilibrium with carbon dioxide constitutes the main physiological buffer. The bicarbonate-carbon dioxide pair stimulates the oxidation, peroxidation and nitration of several biological targets. The demonstration that the carbonate radical existed as an independent species in aqueous solutions at physiological pH and temperature renewed the interest in the pathophysiological roles of this radical and related species. The carbonate radical has been proposed to be a key mediator of the oxidative damage resulting from peroxynitrite production, xanthine oxidase turnover and superoxide dismutase1 peroxidase activity. The carbonate radical has also been proposed to be responsible for the stimulatory effects of the bicarbonate-carbon dioxide pair on oxidations mediated by hydrogen peroxide/transition metal ions. The ultimate precursor of the carbonate radical anion being bicarbonate, carbon dioxide, peroxymonocarbonate or complexes of transition metal ions with bicarbonate-derived species remains a matter of debate. The carbonate radical mediates some of the pathogenic effects of peroxynitrite. The carbonate radical as the oxidant produced from superoxide dismutase (EC 1.15.1.1, SOD1) peroxidase activity. Peroxymonocarbonate is a biological oxidant, whose existence is in equilibrium with hydrogen peroxide and bicarbonate. (PMID: 17505962, 17215880).

Bicarbonate
Bicarbonate (hco3-)
Bicarbonate anion
Bicarbonate ion
Bicarbonate ion (hco31-)
Bicarbonate ions
Carbonate
Carbonate (hco31-)
Carbonate ion (hco31-)
Carbonic acid
Hydrocarbonate(1-)
Hydrogen carbonate
Hydrogen carbonate (hco3-)
Hydrogen carbonate anion
Hydrogen carbonate ion
Hydrogen carbonate ion (hco3-)
Hydrogencarbonate
Hydrogentrioxocarbonate
Monohydrogen carbonate
[co2(oh)](-)
Acid carbonate
Hco3(-)
Hydrogen carbonic acid
Acid carbonic acid
Bicarbonic acid
Bicarbonic acid ion


ADP

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. ADP is the product of ATP dephosphorylation by ATPases. ADP is converted back to ATP by ATP synthases.

Adp
Adenosindiphosphorsaeure
Adenosine 5'-pyrophosphate
Adenosine diphosphate
Adenosine pyrophosphate
Adenosine-5'-diphosphate
Adenosine-5-diphosphate
Adenosine-diphosphate
5'-adenylphosphoric acid
Adenosine 5'-diphosphate
H3adp
5'-adenylphosphate
Adenosine 5'-diphosphoric acid
Adenosine-5'-diphosphoric acid


Phosphate ion

Phosphate is a salt of phosphoric acid. In organic chemistry, a phosphate, or organophosphate, is an ester of phosphoric acid. Organic phosphates are important in biochemistry, biogeochemistry and ecology. Phosphate (Pi) is an essential component of life. In biological systems, phosphorus is found as a free phosphate ion in solution and is called inorganic phosphate, to distinguish it from phosphates bound in various phosphate esters. Inorganic phosphate is generally denoted Pi and at physiological (neutral) pH primarily consists of a mixture of HPO2-4 and H2PO-4 ions. phosphates are most commonly found in the form of adenosine phosphates, (AMP, ADP and ATP) and in DNA and RNA and can be released by the hydrolysis of ATP or ADP. Similar reactions exist for the other nucleoside diphosphates and triphosphates. Phosphoanhydride bonds in ADP and ATP, or other nucleoside diphosphates and triphosphates, contain high amounts of energy which give them their vital role in all living organisms. Phosphate must be actively transported into cells against its electrochemical gradient. In vertebrates, two unrelated families of Na+-dependent Pi transporters carry out this task. Remarkably, the two families transport different Pi species: whereas type II Na+/Pi cotransporters (SCL34) prefer divalent HPO4(2), type III Na+/Pi cotransporters (SLC20) transport monovalent H2PO4. The SCL34 family comprises both electrogenic and electroneutral members that are expressed in various epithelia and other polarized cells. Through regulated activity in apical membranes of the gut and kidney, they maintain body Pi homeostasis, and in salivary and mammary glands, liver, and testes they play a role in modulating the Pi content of luminal fluids. Phosphate levels in the blood play an important role in hormone signaling and in bone homeostasis. In classical endocrine regulation, low serum phosphate induces the renal production of the seco-steroid hormone 1,25-dihydroxyvitamin D3 (1,25(OH)2D3).This active metabolite of vitamin D acts to restore circulating mineral (i.e. phosphate and calcium) levels by increasing absorption in the intestine, reabsorption in the kidney, and mobilization of calcium and phosphate from bone. Thus, chronic renal failure is associated with hyperparathyroidism, which in turn contributes to osteomalacia (softening of the bones). Another complication of chronic renal failure is hyperphosphatemia (low levels of phosphate in the blood). Hyperphosphatemia (excess levels of phosphate in the blood) is a prevalent condition in kidney dialysis patients and is associated with increased risk of mortality. Hypophosphatemia (hungry bone syndrome) has been associated to postoperative electrolyte aberrations and after parathyroidectomy. (PMID: 17581921, 11169009, 11039261, 9159312, 17625581)Fibroblast growth factor 23 (FGF-23) has recently been recognized as a key mediator of phosphate homeostasis, its most notable effect being promotion of phosphate excretion. FGF-23 was discovered to be involved in diseases such as autosomal dominant hypophosphatemic rickets, X-linked hypophosphatemia, and tumor-induced osteomalacia in which phosphate wasting was coupled to inappropriately low levels of 1,25(OH)2D3. FGF-23 is regulated by dietary phosphate in humans. In particular it was found that phosphate restriction decreased FGF-23, and phosphate loading increased FGF-23.

Nfb orthophosphate
O-phosphoric acid
Ortho-phosphate
Orthophosphate (po43-)
Orthophosphate(3-)
Phosphate
Phosphate (po43-)
Phosphate anion(3-)
Phosphate ion (po43-)
Phosphate ion(3-)
Phosphate trianion
Phosphate(3-)
Phosphoric acid ion(3-)
Pi
[po4](3-)
Orthophosphate
Phosphate ion
Po4(3-)
Phosphoric acid
Orthophosphoric acid
Phosphoric acid ion


OXALOACETATE

Oxaloacetic acid, also known as oxosuccinic acid or oxalacetic acid, is a four-carbon dicarboxylic acid appearing as an intermediate of the citric acid cycle. In vivo, oxaloacetate (the ionized form of oxaloacetic acid) is formed by the oxidation of L-malate, catalyzed by malate dehydrogenase, and reacts with Acetyl-CoA to form citrate, catalyzed by citrate synthase.(wikipedia) A class of ketodicarboxylic acids derived from oxalic acid. Oxaloacetic acid is an intermediate in the citric acid cycle and is converted to aspartic acidD by a transamination reaction.

2-ketosuccinate
2-ketosuccinic acid
2-oxobutanedioate
2-oxobutanedioic acid
2-oxosuccinate
2-oxosuccinic acid
Ketosuccinate
Ketosuccinic acid
Oaa
Oxalacetate
Oxaloacetate
Oxaloacetic acid
Oxaloethanoate
Oxaloethanoic acid
Oxosuccinate
Oxosuccinic acid
A-ketosuccinate
A-ketosuccinic acid
Alpha-ketosuccinate
Alpha-ketosuccinic acid
3-carboxy-3-oxopropanoic acid
Keto-succinic acid
Oxalacetic acid
Oxobutanedioic acid
3-carboxy-3-oxopropanoate
Keto-succinate
Oxobutanedioate


Biotin

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 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 signaling. Posttranscriptional events related to ribosomal activity and protein folding may further contribute to 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 signaling and chromatin structure are consistent with the notion that biotin has a unique significance in cell biology. (PMID: 15992684, 16011464).


Manganese is an essential trace nutrient in all forms of life. Physiologically, it. exists as an ion in the body. It is concentrated in cell mitochondria, mostly in the pituitary gland, liver, pancreas, kidney, and bone, influences the synthesis of mucopolysaccharides, stimulates hepatic synthesis of cholesterol and fatty acids, and is a cofactor in many enzymes, including arginase and alkaline phosphatase in the liver.

Manganese
Manganese (ii) ion
Manganese(ii)
Manganese, ion (mn2+)
Manganous ion
Mn(2+)
Mn2+


Glyoxylic acid

Glyoxylic acid or oxoacetic acid is an organic compound that is both an aldehyde and a carboxylic acid. Glyoxylic acid is a liquid with a melting point of -93°C and a boiling point of 111°C. It is an intermediate of the glyoxylate cycle, which enables certain organisms to convert fatty acids into carbohydrates. The conjugate base of glyoxylic acid is known as glyoxylate (PMID: 16396466). In humans, glyoxylate is produced via two pathways: (1) through the oxidation of glycolate in peroxisomes and (2) through the catabolism of hydroxyproline in mitochondria. In the peroxisomes, glyoxylate is converted into glycine by glyoxylate aminotransferase (AGT1) or into oxalate by glycolate oxidase. In the mitochondria, glyoxylate is converted into glycine by mitochondrial glyoxylate aminotransferase AGT2 or into glycolate by glycolate reductase. A small amount of glyoxylate is converted into oxalate by cytoplasmic lactate dehydrogenase. Glyoxylic acid is found to be associated with primary hyperoxaluria I, which is an inborn error of metabolism. Under certain circumstances, glyoxylate can be a nephrotoxin and a metabotoxin. A nephrotoxin is a compound that causes damage to the kidney and kidney tissues. A metabotoxin is an endogenously produced metabolite that causes adverse health effects at chronically high levels. High levels of glyoxylate are involved in the development of hyperoxaluria, a key cause of nephrolithiasis (commonly known as kidney stones). Glyoxylate is both a substrate and inductor of sulfate anion transporter-1 (SAT-1), a gene responsible for oxalate transportation, allowing it to increase SAT-1 mRNA expression, and as a result oxalate efflux from the cell. The increased oxalate release allows the buildup of calcium oxalate in the urine, and thus the eventual formation of kidney stones. As an aldehyde, glyoxylate is also highly reactive and will modify proteins to form advanced glycation products (AGEs).

Formylformate
Formylformic acid
Glyoxalate
Glyoxalic acid
Glyoxylate
Glyoxylic acid
Oxalaldehydate
Oxalaldehydic acid
Oxoacetate
Oxoacetic acid
Oxoethanoate
Oxoethanoic acid
A-ketoacetate
A-ketoacetic acid
Alpha-ketoacetate
Alpha-ketoacetic acid
Glyoxalsaeure
Glyoxylsaeure
α-ketoacetate
α-ketoacetic acid
Oxaldehydate


Glycine

Glycine is a simple, nonessential amino acid, although experimental animals show reduced growth on low-glycine diets. The average adult ingests 3 to 5 grams of glycine daily. Glycine is involved in the body's production of DNA, phospholipids and collagen, and in release of energy. Glycine levels are effectively measured in plasma in both normal patients and those with inborn errors of glycine metabolism. (http://www.dcnutrition.com/AminoAcids/) Nonketotic hyperglycinaemia (OMIM 606899) is an autosomal recessive condition caused by deficient enzyme activity of the glycine cleavage enzyme system (EC 2.1.1.10). The glycine cleavage enzyme system comprises four proteins: P-, T-, H- and L-proteins (EC 1.4.4.2, EC 2.1.2.10 and EC 1.8.1.4 for P-, T- and L-proteins). Mutations have been described in the GLDC (OMIM 238300), AMT (OMIM 238310), and GCSH (OMIM 238330) genes encoding the P-, T-, and H-proteins respectively. The glycine cleavage system catalyses the oxidative conversion of glycine into carbon dioxide and ammonia, with the remaining one-carbon unit transferred to folate as methylenetetrahydrofolate. It is the main catabolic pathway for glycine and it also contributes to one-carbon metabolism. Patients with a deficiency of this enzyme system have increased glycine in plasma, urine and cerebrospinal fluid (CSF) with an increased CSF: plasma glycine ratio. (PMID 16151895).

2-aminoacetate
2-aminoacetic acid
Aciport
Amino-acetate
Amino-acetic acid
Aminoacetate
Aminoacetic acid
Aminoethanoate
Aminoethanoic acid
Glicoamin
Glycocoll
Glycolixir
Glycosthene
Gyn-hydralin
Padil
Aminoessigsaeure
G
Gly
Glycin
Glykokoll
Glyzin
H2n-ch2-cooh
Hgly
Leimzucker


cytosol

biolink:CellularComponent biolink:AnatomicalEntity biolink:PhysicalEssence biolink:OrganismalEntity biolink:SubjectOfInvestigation biolink:BiologicalEntity biolink:ThingWithTaxon biolink:NamedThing biolink:PhysicalEssenceOrOccurrent


beta-Alanine

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.

2-carboxyethylamine
3-amino-propanoate
3-amino-propanoic acid
3-aminopropanoate
3-aminopropanoic acid
3-aminopropionate
3-aminopropionic acid
Abufene
B-alanine
Omega-aminopropionate
Omega-aminopropionic acid
B-aminopropanoate
B-aminopropanoic acid
B-aminopropionate
B-aminopropionic acid
Beta alanine
Beta-alanine
Beta-aminopropanoate
Beta-aminopropanoic acid
Beta-aminopropionate
Beta-aminopropionic acid
β-alanine


Malonic semialdehyde is formed in the alternative pathway of propionate metabolism and in the catabolism of beta-alanine. Studies done on these pathways in cultured cells from a patient with mitochondrial malonyl-CoA decarboxylase deficiency show that malonic semialdehyde is directly converted into acetyl-CoA in man. (PMID: 6418146).

3-oxopropanoate
3-oxopropanoic acid
3-oxopropionic acid
Formyl acetate
Formyl acetic acid
Formylacetic acid
Malonaldehydic acid
Malonate semialdehyde
Formylacetate


Aspartic acid

Aspartic acid (Asp, D), also known as aspartate, the name of its anion, is one of the 20 natural proteinogenic amino acids which are the building blocks of proteins. As its name indicates, aspartic acid is the carboxylic acid analog of asparagine. As a neurotransmitter, aspartic acid may provide resistance to fatigue and thus lead to endurance, although the evidence to support this idea is not strong (Wikipedia). Aspartic acid is a nonessential amino acid that is made from glutamic acid by enzymes using vitamin B6. The amino acid has important roles in the urea cycle and DNA metabolism. Aspartic acid is a major excitatory neurotransmitter, which is sometimes found to be increased in epileptic and stroke patients. It is decreased in depressed patients and in patients with brain atrophy. Aspartic acid supplements are being evaluated. Five grams can raise blood levels. Magnesium and zinc may be natural inhibitors of some of the actions of aspartic acid. Aspartic acid, with the amino acid phenylalanine, is a part of a new natural sweetener, aspartame. This sweetener is an advance in artificial sweeteners, and is probably safe in normal doses to all except phenylketonurics. The jury is still out on the long-term effects it has on many brain neurohormones. Aspartic acid may be a significant immunostimulant of the thymus and can protect against some of the damaging effects of radiation. Many claims have been made for the special value of administering aspartic acid in the form of potassium and magnesium salts. Since aspartic acid is relatively nontoxic, studies are now in progress to elucidate its pharmacological and therapeutic roles (http://www.dcnutrition.com/AminoAcids).

Asp
(+)-aspartate
(+)-aspartic acid
(2s)-aspartate
(2s)-aspartic acid
(l)-aspartate
(l)-aspartic acid
(r)-2-aminosuccinate
(s)-(+)-aspartate
(s)-(+)-aspartic acid
(s)-2-aminosuccinate
(s)-2-aminosuccinic acid
(s)-aminobutanedioate
(s)-aminobutanedioic acid
(s)-aspartate
(s)-aspartic acid
(s)-amino-butanedioate
(s)-amino-butanedioic acid
2-amino-3-methylsuccinate
2-amino-3-methylsuccinic acid
2-aminosuccinate
2-aminosuccinic acid
Aminosuccinate
Asparagate
Asparagic acid
Asparaginate
Asparaginic acid
Asparatate
Aspartate
H-asp-oh
L-(+)-aspartate
L-(+)-aspartic acid
L-aminosuccinate
L-aminosuccinic acid
L-asparagate
L-asparagic acid
L-asparaginate
L-asparaginic acid
L-aspartate
Alpha-aminosuccinate
Alpha-aminosuccinic acid
(s)-2-aminobutanedioic acid
Aspartic acid
D
L-asparaginsaeure
(s)-2-aminobutanedioate


Carbon dioxide

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.


L-Glutamine

Glutamine (Gln) is one of the 20 amino acids encoded by the standard genetic code. Its side chain is an amide; it is formed by replacing a side-chain hydroxyl of glutamic acid with an amine functional group. glutamine is found in foods high in proteins, such as fish, red meat, beans, and dairy products. glutamine is a supplement that is used in weightlifting, bodybuilding, endurance and other sports, as well as by those who suffer from muscular cramps or pain particularly elderly people. The main use of glutamine within the diet of either group is as a means of replenishing the body's stores of amino acids that have been used during exercise or everyday activities. Studies which are looking into problems with excessive consumption of glutamine thus far have proved inconclusive. However, normal supplementation is healthy mainly because glutamine is supposed to be supplemented after prolonged periods of exercise (for example, a workout or exercise in which amino acids are required for use) and replenishes amino acid stores; this being the main reason glutamine is recommended during fasting or for people who suffer from physical trauma, immune deficiencies, or cancer. There is a significant body of evidence that links glutamine-enriched diets with intestinal effects; aiding maintenance of gut barrier function, intestinal cell proliferation and differentiation, as well as generally reducing septic morbidity and the symptoms of Irritable Bowel Syndrome. The reason for such "cleansing" properties is thought to stem from the fact that the intestinal extraction rate of glutamine is higher than that for other amino acids, and is therefore thought to be the most viable option when attempting to alleviate conditions relating to the gastrointestinal tract. These conditions were discovered after comparing plasma concentration within the gut between glutamine-enriched and non glutamine-enriched diets. However, even though glutamine is thought to have "cleansing" properties and effects, it is unknown to what extent glutamine has clinical benefits, due to the varied concentrations of glutamine in varieties of food. It is also known that glutamine has various effects in reducing healing time after operations. Hospital waiting times after abdominal surgery are reduced by providing parenteral nutrition regimens containing amounts of glutamine to patients. Clinical trials have revealed that patients on supplementation regimes containing glutamine have improved nitrogen balances, generation of cysteinyl-leukotrienes from polymorphonuclear neutrophil granulocytes and improved lymphocyte recovery and intestinal permeability (in postoperative patients) - in comparison to those who had no glutamine within their dietary regime; all without any side-effects. (http://en.wikipedia.org/wiki/glutamine).

(2s)-2,5-diamino-5-oxopentanoate
(2s)-2,5-diamino-5-oxopentanoic acid
(2s)-2-amino-4-carbamoylbutanoate
(2s)-2-amino-4-carbamoylbutanoic acid
(s)-2,5-diamino-5-oxopentanoate
(s)-2,5-diamino-5-oxopentanoic acid
2-aminoglutaramic acid
Cebrogen
Glavamin
Glumin
Glutamic acid 5-amide
Glutamic acid amide
Glutamine
L-(+)-glutamine
L-2-aminoglutaramic acid
L-2-aminoglutaramidic acid
L-glutamic acid 5-amide
L-glutamic acid gamma-amide
L-glutamid
L-glutamide
L-glutamin
L-glutamine
L-glutaminsaeure-5-amid
Levoglutamid
Levoglutamida
Levoglutamide
Levoglutamidum
Levoglutamina
Polyglutamine
Stimulina
Gamma-glutamine
Q
Glutamate 5-amide
Glutamate amide


Water

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 Earth's 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 body's 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 sun's energy to split off water's 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 sun's 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).

Dihydrogen oxide
Steam
[oh2]
Acqua
Agua
Aqua
Bound water
Dihydridooxygen
Eau
H2o
Hoh
Hydrogen hydroxide
Wasser


Asparagine

Asparagine (Asn) is one of the 20 most common natural amino acids on Earth. It has carboxamide as the side chain's functional group. Asparagine is not an essential amino acid, which means that it can be synthesized from central metabolic pathway intermediates in humans and is not required in the diet. The precursor to asparagine is oxaloacetate. Oxaloacetate is converted to aspartate using a transaminase enzyme. The enzyme transfers the amino group from glutamate to oxaloacetate producing alpha-ketoglutarate and aspartate. The enzyme asparagine synthetase produces asparagine, AMP, glutamate, and pyrophosphate from aspartate, glutamine, and ATP. In the asparagine synthetase reaction, ATP is used to activate aspartate, forming beta-aspartyl-AMP. Glutamine donates an ammonium group which reacts with beta-aspartyl-AMP to form asparagine and free AMP. Since the asparagine side chain can make efficient hydrogen bond interactions with the peptide backbone, asparagines are often found near the beginning and end of alpha-helices, and in turn motifs in beta sheets. Its role can be thought as "capping" the hydrogen bond interactions which would otherwise need to be satisfied by the polypeptide backbone. Glutamines have an extra methylene group and have more conformational entropy, and thus are less useful in this regard. Asparagine also provides key sites for N-linked glycosylation, modification of the protein chain with the addition of carbohydrate chains. A reaction between asparagine and reducing sugars or reactive carbonyls produces acrylamide (acrylic amide) in food when heated to sufficient temperature (i.e. baking). These occur primarily in baked goods such as french fries, potato chips, and roasted coffee. Asparagine was first isolated in 1806 from asparagus juice, in which it is abundant--hence its name--becoming the first amino acid to be isolated. The smell observed in the urine of some individuals after their consumption of asparagus is attributed to a byproduct of the metabolic breakdown of asparagine, asparagine-amino-succinic-acid monoamide. However, some scientists disagree and implicate other substances in the smell, especially methanethiol (Wikipedia).

(-)-asparagine
(s)-2,4-diamino-4-oxobutanoate
(s)-2,4-diamino-4-oxobutanoic acid
(s)-asparagine
2-aminosuccinamate
2-aminosuccinamic acid
Agedoite
Altheine
Asn
Asparagine
Asparagine acid
Asparamide
Aspartamate
Aspartamic acid
Aspartic acid amide
Aspartic acid b-amide
Aspartic acid beta amide
B2,4-(s)-diamino-4-oxo-utanoate
B2,4-(s)-diamino-4-oxo-utanoic acid
Crystal vi
L-2,4-diamino-4-oxobutanoate
L-2,4-diamino-4-oxobutanoic acid
L-asparagine
L-aspartamine
L-b-asparagine
L-beta-asparagine
A-aminosuccinamate
A-aminosuccinamic acid
Alpha amminosuccinamate
Alpha amminosuccinamic acid
Alpha-aminosuccinamate
Alpha-aminosuccinamic acid
(2s)-2,4-diamino-4-oxobutanoic acid
(2s)-2-amino-3-carbamoylpropanoic acid
(s)-2-amino-3-carbamoylpropanoic acid
L-2-aminosuccinamic acid
L-asparagin
L-aspartic acid beta-amide
N
(2s)-2,4-diamino-4-oxobutanoate
(2s)-2-amino-3-carbamoylpropanoate
(s)-2-amino-3-carbamoylpropanoate
α-aminosuccinamate
α-aminosuccinamic acid
L-2-aminosuccinamate
L-aspartate b-amide
L-aspartate beta-amide
L-aspartate β-amide
L-aspartic acid b-amide
L-aspartic acid β-amide


Citrulline

Citrulline is an amino acid made from ornithine and carbamoyl phosphate in one of the central reactions in the urea cycle. It is also produced from arginine as a by-product of the reaction catalyzed by NOS family (NOS). In this reaction, arginine is first oxidized into N(omega)-hydroxyarginine, which is then further oxidized to citrulline concomitant with the release of nitric oxide (EC 1.14.13.39). Citrulline's name is derived from citrullus, the Latin word for watermelon, from which it was first isolated.


(N(omega)-L-arginino)succinic acid

Arginosuccinic acid is a basic amino acid. Some cells synthesize it from citrulline, aspartic acid and use it as a precursor for arginine in the urea cycle or Citrulline-NO cycle. The enzyme that catalyzes the reaction is argininosuccinate synthetase. Argininosuccinic acid is a precursor to fumarate in the citric acid cycle via argininosuccinate lyase. Defects in the arginosuccinate lyase enzyme can lead to arginosuccinate lyase deficiency. Argininosuccinate (ASA) lyase deficiency results in defective cleavage of ASA. This leads to an accumulation of ASA in cells and an excessive excretion of ASA in urine (arginosuccinic aciduria). In virtually all respects, this disorder shares the characteristics of other urea cycle defects. The most important characteristic of ASA lyase deficiency is its propensity to cause hyperammonemia in affected individuals. ASA in affected individuals is excreted by the kidney at a rate practically equivalent to the glomerular filtration rate (GFR). Whether ASA itself causes a degree of toxicity due to hepatocellular accumulation is unknown; such an effect could help explain hyperammonemia development in affected individuals. Regardless, the name of the disease is derived from the rapid clearance of ASA in urine, although elevated levels of ASA can be found in plasma. ASA lyase deficiency is associated with high mortality and morbidity rates. Symptoms of ASA lyase deficiency include anorexia, irritability rapid breathing, lethargy and vomiting. Extreme symptoms include coma and cerebral edema.


Ammonia

Ammonia is a colourless alkaline gas and is one of the most abundant nitrogen-containing compounds in the atmosphere. It is an irritant with a characteristic pungent odor that is widely used in industry. Inasmuch as ammonia is highly soluble in water and, upon inhalation, is deposited in the upper airways, occupational exposures to ammonia have commonly been associated with sinusitis, upper airway irritation, and eye irritation. Acute exposures to high levels of ammonia have also been associated with diseases of the lower airways and interstitial lung. Small amounts of ammonia are naturally formed in nearly all tissues and organs of the vertebrate organism. Ammonia is both a neurotoxin and a metabotoxin. In fact, it is the most common endogenous neurotoxin. A neurotoxin is a compound that causes damage to neural tissue and neural cells. A metabotoxin is an endogenously produced metabolite that causes adverse health effects at chronically high levels. Ammonia is recognized to be central in the pathogenesis of a brain condition known as hepatic encephalopathy, which arises from various liver diseases and leads to a build up ammonia in the blood (hyperammonemia). More than 40% of people with cirrhosis develop hepatic encephalopathy. Part of the neurotoxicity of ammonia arises from the fact that it easily crosses the blood-brain barrier and is absorbed and metabolized by the astrocytes, a population of cells in the brain that constitutes 30% of the cerebral cortex. Astrocytes use ammonia when synthesizing glutamine from glutamate. The increased levels of glutamine lead to an increase in osmotic pressure in the astrocytes, which become swollen. There is increased activity of the inhibitory gamma-aminobutyric acid (GABA) system, and the energy supply to other brain cells is decreased. This can be thought of as an example of brain edema. The source of the ammonia leading to hepatic encephalopathy is not entirely clear. The gut produces ammonia, which is metabolized in the liver, and almost all organ systems are involved in ammonia metabolism. Colonic bacteria produce ammonia by splitting urea and other amino acids, however this does not fully explain hyperammonemia and hepatic encephalopathy. The alternative explanation is that hyperammonemia is the result of the intestinal breakdown of amino acids, especially glutamine. The intestines have significant glutaminase activity, predominantly located in the enterocytes. On the other hand, intestinal tissues only have a little glutamine synthetase activity, making it a major glutamine-consuming organ. In addition to the intestine, the kidney is an important source of blood ammonia in patients with liver disease. Ammonia is also taken up by the muscle and brain in hepatic coma, and there is confirmation that ammonia is metabolized in muscle. Excessive formation of ammonia in the brains of Alzheimer's disease patients has also been demonstrated, and it has been shown that some Alzheimer's disease patients exhibit elevated blood ammonia concentrations. Ammonia is the most important natural modulator of lysosomal protein processing. Indeed, there is strong evidence for the involvement of aberrant lysosomal processing of beta-amyloid precursor protein (beta-APP) in the formation of amyloid deposits. Inflammatory processes and activation of microglia are widely believed to be implicated in the pathology of Alzheimer's disease. Ammonia is able to affect the characteristic functions of microglia, such as endocytosis, and cytokine production. Based on these facts, an ammonia-based hypothesis for Alzheimer's disease has been suggested (PMID: 17006913, 16167195, 15377862, 15369278). Chronically high levels of ammonia in the blood are associated with nearly twenty different inborn errors of metabolism including: 3-hydroxy-3-methylglutaryl-CoA lyase deficiency, 3-methyl-crotonylglycinuria, argininemia, argininosuccinic aciduria, beta-ketothiolase deficiency, biotinidase deficiency, carbamoyl phosphate synthetase deficiency, carnitine-acylcarnitine translocase deficiency, citrullinemia type I, hyperinsulinism-hyperammonemia syndrome, hyperornithinemia-hyperammonemia-homocitrullinuria syndrome, isovaleric aciduria, lysinuric protein intolerance, malonic aciduria, methylmalonic aciduria, methylmalonic aciduria due to cobalamin-related disorders, propionic acidemia, pyruvate carboxylase deficiency, and short chain acyl CoA dehydrogenase deficiency (SCAD deficiency). Many of these inborn errors of metabolism are associated with urea cycle disorders or impairment of amino acid metabolism. High levels of ammonia in the blood (hyperammonemia) lead to the activation of NMDA receptors in the brain. This results in the depletion of brain ATP, which in turn leads to the release of glutamate. Ammonia also leads to the impairment of mitochondrial function and calcium homeostasis, thereby decreasing ATP synthesis. Excess ammonia also increases the formation of nitric oxide (NO), which in turn reduces the activity of glutamine synthetase, and thereby decreases the elimination of ammonia in the brain (PMID: 12020609). As a neurotoxin, ammonia predominantly affects astrocytes. Disturbed mitochondrial function and oxidative stress, factors implicated in the induction of the mitochondrial permeability transition, appear to be involved in the mechanism of ammonia neurotoxicity. Ammonia can also affect the glutamatergic and GABAergic neuronal systems, the two prevailing neuronal systems of the cortical structures. All of these effects can lead to irreversible brain damage, coma, and/or death. Infants with urea cycle disorders and hyperammonemia initially exhibit vomiting and increasing lethargy. If untreated, seizures, hypotonia (poor muscle tone, floppiness), respiratory distress (respiratory alkalosis), and coma can occur. Adults with urea cycle disorders and hyperammonemia will exhibit episodes of disorientation, confusion, slurred speech, unusual and extreme combativeness or agitation, stroke-like symptoms, lethargy, and delirium. Ammonia also has toxic effects when an individual is exposed to ammonia solutions. Acute exposure to high levels of ammonia in air may be irritating to skin, eyes, throat, and lungs and cause coughing and burns. Lung damage and death may occur after exposure to very high concentrations of ammonia. Swallowing concentrated solutions of ammonia can cause burns in the mouth, throat, and stomach. Splashing ammonia into eyes can cause burns and even blindness.

Ammonia anhydrous
Ammonia inhalant
Ammonia solution strong [usan]
Ammonia water
Ammoniak
Liquid ammonia
Am-fol
Ammonia
Ammonia (conc 20% or greater)
Ammonia gas
Ammonia solution
Ammonia solution strong (nf)
Ammonia water (jp15)
Ammoniac [french]
Ammoniaca [italian]
Ammoniacum gummi
Ammoniak [german]
Ammoniak kconzentrierter
Ammoniakgas
Ammonium ion
Amoniak [polish]
Anhydrous ammonia
Aromatic ammonia vaporole
Azane
Nh(3)
Nh3
Nitro-sil
Primaeres amin
Sekundaeres amin
Spirit of hartshorn
Tertiaeres amin
[nh3]
Ammoniac
Amoniaco
R-717
Ammonia solution strong


Hioxyl

Hydrogen peroxide (H2O2) is a very pale blue liquid which appears colourless in a dilute solution, slightly more viscous than water. It is a weak acid. It has strong oxidizing properties and is therefore a powerful bleaching agent that is mostly used for bleaching paper, but has also found use as a disinfectant and as an oxidizer. Hydrogen peroxide in the form of carbamide peroxide is widely used for tooth whitening (bleaching), both in professionally- and in self-administered products. Hydrogen peroxide (H2O2) is a well-documented component of living cells. It plays important roles in host defense and oxidative biosynthetic reactions. In addition there is growing evidence that at low levels, H2O2 also functions as a signaling agent, particularly in higher organisms. H2O2 has increasingly been viewed as an important cellular signaling agent in its own right, capable of modulating both contractile and growth-promoting pathways with more far-reaching effects. Due to the accumulation of hydrogen peroxide in the skin of patients with the depigmentation disorder vitiligo, the human epidermis cannot have the normal capacity for autocrine synthesis, transport and degradation of acetylcholine as well as the muscarinic (m1-m5) and nicotinic signal transduction in keratinocytes and melanocytes. Accumulating evidence suggests that hydrogen peroxide (H(2)O(2)) plays an important role in cancer development. Experimental data have shown that cancer cells produce high amounts of H(2)O(2). An increase in the cellular levels of H(2)O(2) has been linked to several key alterations in cancer, including DNA alterations, cell proliferation, apoptosis resistance, metastasis, angiogenesis and hypoxia-inducible factor 1 (HIF-1) activation. (PMID: 17150302, 17335854, 16677071, 16607324, 16514169).

Adeka super el
Albone
Albone 35
Albone ds
Anti-keim 50
Asepticper
Baquashock
Cix
Clarigel gold
Crestal whitestrips
Crystacide
Dentasept
Deslime lp
Hioxyl
Hipox
Hybrite
Hydrogen dioxide
Hydrogen peroxide
Inhibine
Lase peroxide
Lensan a
Magic bleaching
Metrokur
Mirasept
Nite white excel 2
Odosat d
Opalescence xtra
Oxigenal
Oxydol
Oxyfull
Oxysept
Oxysept i
Pegasyl
Perhydrol
Perone
Peroxaan
Peroxclean
Quasar brite
Select bleach
Superoxol
T-stuff
Whiteness hp
Whitespeed
Xtra white
[oh(oh)]
Dihydrogen dioxide
H2o2
Hooh


Adenylsuccinic acid, also known as adenylosuccinate or aspartyl adenylate, belongs to the class of organic compounds known as purine ribonucleoside monophosphates. These are nucleotides consisting of a purine base linked to a ribose to which one monophosphate group is attached. Adenylsuccinic acid is slightly soluble (in water) and a moderately acidic compound (based on its pKa). Within the cell, adenylsuccinic acid is primarily located in the cytoplasm and mitochondria. In humans, adenylsuccinic acid is involved in the aspartate metabolism pathway, the azathioprine action pathway, the mercaptopurine action pathway, and the purine metabolism pathway. Adenylsuccinic acid is also involved in several metabolic disorders, some of which include myoadenylate deaminase deficiency, the lesch-nyhan syndrome (LNS) pathway, adenylosuccinate lyase deficiency, and the hypoacetylaspartia pathway. Adenylsuccinic acid is a substrate of the enzyme adenylosuccinase [EC 4.3.2.2] in purine metabolism pathway. The accumulation of adenylsuccinic acid in body fluids occurs due to a deficiency of adenylosuccinase. (KEGG; PMID 8412002).

D-ribofuranosyl-9h-purin-6-yl) mono(dihydrogen phosphate) (ester)


Fumaric acid

Fumaric acid is a precursor to L-malate in the Krebs tricarboxylic acid cycle. It is formed by the oxidation of succinate by succinate dehydrogenase. Fumarate is converted by fumarase to malate. A fumarate is a salt or ester of the organic compound fumaric acid, a dicarboxylic acid. (wikipedia).

(2e)-but-2-enedioate
(2e)-but-2-enedioic acid
(e)-2-butenedioate
(e)-2-butenedioic acid
2-(e)-butenedioate
2-(e)-butenedioic acid
Allomaleate
Allomaleic acid
Boletate
Boletic acid
Fc 33
Fumarate
Fumaric acid
Lichenate
Lichenic acid
Sodium fumarate
Trans-1,2-ethylenedicarboxylate
Trans-1,2-ethylenedicarboxylic acid
Trans-2-butenedioate
Trans-2-butenedioic acid
Trans-butenedioate
Trans-butenedioic acid
(2e)-2-butenedioic acid
E297
Fumarsaeure
Trans-but-2-enedioic acid
(2e)-2-butenedioate
Trans-but-2-enedioate


D-Aspartic Acid

D-Aspartic acid is the D-isomer of aspartic acid. Since its discovery in invertebrates, free D-aspartate (D-Asp) has been identified in a variety of organisms, including microorganisms, plants, and lower animals, mammals and humans. D-Asp in mammalian tissues is present in specific cells, indicating the existence of specific molecular components that regulate D-Asp levels and localization in tissues. In the rat adrenal medulla, D-Asp is closely associated with adrenaline-cells (A-cells), which account for approximately 80% of the total number of chromaffin cells in the tissue, and which make and store adrenaline. D-Asp appears to be absent from noradrenaline-cells (NA-cells), which comprise approximately 20% of the total number of chromaffin cells in the adrenal medulla, and which make and store noradrenaline. D-aspartate oxidase (EC 1.4.3.1, D-AspO), which catalyzes oxidative deamination of D-Asp, appears to be present only in NA-cells, suggesting that the lack of D-Asp in these cells is due to D-Asp oxidase-mediated metabolism of D-Asp. In the rat adrenal cortex, the distribution of D-Asp changes during development. It has been suggested that developmental changes in the localization of D-Asp reflects the participation of D-Asp in the development and maturation of steroidogenesis in rat adrenal cortical cells. D-Asp is involved in steroid hormone synthesis and secretion in mammals as well. D-Asp is synthesized intracellularly, most likely by Asp racemase (EC 5.1.1.13). Endogenous D-Asp apparently has two different intracellular localization patterns: cytoplasmic and vesicular. D-Asp release can occur through three distinct pathways: 1) spontaneous, continuous release of cytoplasmic D-Asp, which is not associated with a specific stimulus; 2) release of cytoplasmic D-Asp via a volume-sensitive organic anion channel that connects the cytoplasm and extracellular space; 3) exocytotic discharge of vesicular D-Asp. D-Asp can be released via a mechanism that involves the L-Glu transporter. D-Asp is thus apparently in dynamic flux at the cellular level to carry out its physiological function(s) in mammals. (PMID: 16755369).

(-)-aspartic acid
(2r)-2-aminobutanedioate
(2r)-2-aminobutanedioic acid
(r)-2-aminobutanedioate
(r)-2-aminobutanedioic acid
(r)-2-aminosuccinic acid
(r)-aspartic acid
1-amino-1,2-carboxyethane
Aspartic acid
D-(-)-aspartic acid
D-asparaginsaeure
D-aspartate
D-aspartic acid
Lopac-alpha-9256
Tocris-0213
Delta-(-)-aspartic acid
Delta-asparaginsaeure
Delta-aspartate
Delta-aspartic acid


Oxygen

Oxygen is the third most abundant element in the universe after hydrogen and helium and the most abundant element by mass in the Earth's 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).

Dioxygen
Molecular oxygen
O2
Oxygen
Oxygen molecule
[oo]
Dioxygene
Disauerstoff
E 948
E-948
E948


FAD

FAD, also known as flavitan or adeflavin, belongs to the class of organic compounds known as flavin nucleotides. These are nucleotides containing a flavin moiety. Flavin is a compound that contains the tricyclic isoalloxazine ring system, which bears 2 oxo groups at the 2- and 4-positions. FAD is a drug which is used to treat eye diseases caused by vitamin b2 deficiency, such as keratitis and blepharitis. FAD is slightly soluble (in water) and a moderately acidic compound (based on its pKa). FAD has been found in human liver and muscle tissues, and has also been detected in multiple biofluids, such as feces and blood. Within the cell, FAD is primarily located in the cytoplasm, mitochondria, endoplasmic reticulum and peroxisome. FAD exists in all living organisms, ranging from bacteria to humans. In humans, FAD is involved in the risedronate action pathway, the ibandronate action pathway, the valine, leucine and isoleucine degradation pathway, and the pyrimidine metabolism pathway. FAD is also involved in several metabolic disorders, some of which include the oncogenic action OF L-2-hydroxyglutarate in hydroxygluaricaciduria pathway, gaba-transaminase deficiency, 4-hydroxybutyric aciduria/succinic semialdehyde dehydrogenase deficiency, and the saccharopinuria/hyperlysinemia II pathway. FAD is a condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972).

1h-purin-6-amine flavin dinucleotide
1h-purin-6-amine flavine dinucleotide
Adenine-flavin dinucleotide
Adenine-flavine dinucleotide
Adenine-riboflavin dinuceotide
Adenine-riboflavin dinucleotide
Adenine-riboflavine dinucleotide
Fad
Flamitajin b
Flanin f
Flavin adenine dinucleotide
Flavin adenine dinucleotide oxidized
Flavin-adenine dinucleotide
Flavine adenosine diphosphate
Flavine-adenine dinucleotide
Flavitan
Flaziren
Isoalloxazine-adenine dinucleotide
Riboflavin 5'-adenosine diphosphate
Riboflavin-adenine dinucleotide
Riboflavine-adenine dinucleotide
Adeflavin


N-acetyl-L-aspartic acid

N-Acetylaspartic acid is a derivative of aspartic acid. It is the second most concentrated molecule in the brain after the amino acid glutamate. It is synthesized in neurons from the amino acid aspartate and acetyl coenzyme A (acetyl CoA). The various functions served by N-acetylaspartic acid are still under investigation, but the primary proposed functions include (1) acting as a neuronal osmolyte that is involved in fluid balance in the brain, (2) serving as a source of acetate for lipid and myelin synthesis in oligodendrocytes (the glial cells that myelinate neuronal axons), (3) serving as a precursor for the synthesis of the important dipeptide neurotransmitter N-acetylaspartylglutamate (NAAG), and (4) playing a potential role in energy production from the amino acid glutamate in neuronal mitochondria. High neurotransmitter levels can lead to abnormal neural signaling, delayed or arrested intellectual development, and difficulties with general motor skills. When present in sufficiently high levels, N-acetylaspartic acid can be a neurotoxin, an acidogen, and a metabotoxin. A neurotoxin is a compound that disrupts or attacks neural tissue. An acidogen is an acidic compound that induces acidosis, which has multiple adverse effects on many organ systems. A metabotoxin is an endogenously produced metabolite that causes adverse health effects at chronically high levels. Chronically high levels of N-acetylaspartic acid are associated with Canavan disease. N-acetylaspartic acid is an organic acid. Abnormally high levels of organic acids in the blood (organic acidemia), urine (organic aciduria), the brain, and other tissues lead to general metabolic acidosis. Acidosis typically occurs when arterial pH falls below 7.35. Infants with acidosis have symptoms that include poor feeding, vomiting, loss of appetite, weak muscle tone (hypotonia), and lack of energy (lethargy). These can progress to heart abnormalities, seizures, coma, and possibly death. Many affected children with organic acidemias experience intellectual disability or delayed development. In adults, acidosis or acidemia is characterized by headaches, confusion, feeling tired, tremors, sleepiness, and flapping tremors.

(2s)-2-acetamidobutanedioate
(2s)-2-acetamidobutanedioic acid
(s)-2-(acetylamino)butanedioate
(s)-2-(acetylamino)butanedioic acid
(s)-2-(acetylamino)succinic acid
Acetyl-l-aspartate
Acetyl-l-aspartic acid
Acetylaspartate
Acetylaspartic acid
L-n-acetylaspartate
L-n-acetylaspartic acid
N-acetyl-l-aspartate
N-acetyl-l-aspartic acid
N-acetyl-s-aspartate
N-acetyl-s-aspartic acid
N-acetylaspartate
N-acetylaspartic acid
Naa
(s)-2-(acetylamino)succinate


Acetic acid

Acetic acid is one of the simplest carboxylic acids. It is an important chemical reagent and industrial chemical that is used in the production of plastic soft drink bottles, photographic film; and polyvinyl acetate for wood glue, as well as many synthetic fibres and fabrics. In households diluted acetic acid is often used as a cleaning agent. In the food industry acetic acid is used as an acidity regulator. The acetyl group, derived from acetic acid, is fundamental to the biochemistry of virtually all forms of life. When bound to coenzyme A it is central to the metabolism of carbohydrates and fats. However, the concentration of free acetic acid in cells is kept at a low level to avoid disrupting the control of the pH of the cell contents. Acetic acid is produced and excreted by certain bacteria, notably the Acetobacter genus and Clostridium acetobutylicum. These bacteria are found universally in foodstuffs, water, and soil, and acetic acid is produced naturally as fruits and some other foods spoil. Acetic acid is also a component of the vaginal lubrication of humans and other primates, where it appears to serve as a mild antibacterial agent.

Acetate
Ethanoate
Ethanoic acid
Ethylate
Ethylic acid
Glacial acetate
Glacial acetic acid
Kyselina octova
Methanecarboxylate
Methanecarboxylic acid
Vinegar
Vinegar acid
Acide acetique
Acoh
Ch3-cooh
Ch3co2h
E 260
E-260
E260
Essigsaeure
Ethoic acid
Hoac
Ins no. 260
Meco2h
Mecooh
Ethoate


GTP

Guanosine triphosphate (GTP) is a guanine nucleotide containing three phosphate groups esterified to the sugar moiety. GTP functions as a carrier of phosphates and pyrophosphates involved in channeling chemical energy into specific biosynthetic pathways. GTP activates the signal transducing G proteins which are involved in various cellular processes including proliferation, differentiation, and activation of several intracellular kinase cascades. Proliferation and apoptosis are regulated in part by the hydrolysis of GTP by small GTPases Ras and Rho. Another type of small GTPase, Rab, plays a role in the docking and fusion of vesicles and may also be involved in vesicle formation. In addition to its role in signal transduction, GTP also serves as an energy-rich precursor of mononucleotide units in the enzymatic biosynthesis of DNA and RNA.

Guanosine mono(tetrahydrogen triphosphate) (ester)


Inosinic Acid

Inosinic acid is a purine nucleotide which has hypoxanthine as the base and one phosphate group esterified to the sugar moiety. Inosinic acid is a nucleotide present in muscle and other tissues. It is formed by the deamination of AMP and when hydrolysed produces inosine. Inosinic acid is the ribonucleotide of hypoxanthine and is the first compound formed during the synthesis of purine. (Wikipedia).

5'-imp
5'-inosinate
5'-inosine monophosphate
5'-inosinic acid
Imp
Inosine 5'-monophosphate
Inosine 5'-phosphate
Inosine monophosphate
Inosine-5'-monophosphate
2'-inosine-5'-monophosphate
Hypoxanthosine 5'-monophosphate
Inosinic acid
Ribosylhypoxanthine monophosphate
2'-inosine-5'-monophosphoric acid
5'-inosine monophosphoric acid
Hypoxanthosine 5'-monophosphoric acid
Inosine 5'-monophosphoric acid
Inosine 5'-phosphoric acid
Inosine monophosphoric acid
Inosinate
Ribosylhypoxanthine monophosphoric acid


GDP

Guanosine 5'-(trihydrogen diphosphate). A guanine nucleotide containing two phosphate groups esterified to the sugar moiety. It is an ester of pyrophosphoric acid with the nucleoside guanosine. GDP consists of the pyrophosphate group, the pentose sugar ribose, and the nucleobase guanine. GDP is the product of GTP dephosphorylation by GTPases, e.g. the G-proteins that are involved in signal transduction.


Magnesium salts are essential in nutrition, being required for the activity of many enzymes, especially those concerned with oxidative phosphorylation. Physiologically, it exists as an ion in the body. It is a component of both intra- and extracellular fluids and is excreted in the urine and feces. Deficiency causes irritability of the nervous system with tetany, vasodilatation, convulsions, tremors, depression, and psychotic behavior. Magnesium ion in large amounts is an ionic laxative, and magnesium sulfate (Epsom salts) is sometimes used for this purpose. So-called "milk of magnesia" is a water suspension of one of the few insoluble magnesium compounds, magnesium hydroxide; the undissolved particles give rise to its appearance and name. Milk of magnesia is a mild base, and is commonly used as an antacid.

Magnesium
Magnesium ions
Magnesium ion
Magnesium, doubly charged positive ion
Magnesium, ion (mg(2+))
Mg(2+)
Mg2+


carbamoyl phosphate

Carbamoyl phosphate is a precursor of both arginine and pyrimidine biosynthesis. It is a labile and potentially toxic intermediate. Carbamoyl phosphate is a molecule that is involved in ridding the body of excess nitrogen in the urea cycle, and also in the synthesis of pyrimidines. It is produced from carbon dioxide, ammonia, and phosphate (from ATP) by the enzyme carbamoyl phosphate synthase. -- Wikipedia.

Carbamic acid monoanhydride with phosphorate

Carbamic acid monoanhydride with phosphoric acid

Aminocarbonyl dihydrogen phosphoric acid


N-Carbamoylaspartic acid

Ureidosuccinic acid, also known as L-ureidosuccinate or carbamyl-L-aspartate, belongs to the class of organic compounds known as aspartic acid and derivatives. Aspartic acid and derivatives are compounds containing an aspartic acid or a derivative thereof resulting from reaction of aspartic acid at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom. Ureidosuccinic acid exists as a solid, soluble (in water), and a weakly acidic compound (based on its pKa). Ureidosuccinic acid has been found in human prostate tissue, and has also been primarily detected in saliva. Within the cell, ureidosuccinic acid is primarily located in the cytoplasm. Ureidosuccinic acid exists in all living organisms, ranging from bacteria to humans. In humans, ureidosuccinic acid is involved in the aspartate metabolism pathway and the pyrimidine metabolism pathway. Ureidosuccinic acid is also involved in several metabolic disorders, some of which include the canavan disease pathway, UMP synthase deficiency (orotic aciduria), dihydropyrimidinase deficiency, and Beta ureidopropionase deficiency. Outside of the human body, ureidosuccinic acid can be found in a number of food items such as green vegetables, celeriac, pepper (c. frutescens), and italian sweet red pepper. This makes ureidosuccinic acid a potential biomarker for the consumption of these food products. Ureidosuccinic acid is an intermediary product in pyrimidine biosynthesis.

2-ureidobutanedioate
2-ureidobutanedioic acid
Carbamoylaspartic acid
Carbamyl-l-aspartic acid
Carbamylaspartic acid
L-n-carbamoylaspartic acid
L-ureidosuccinate
L-ureidosuccinic acid
N-(aminocarbonyl)-l-aspartic acid
N-carbamoyl-l-aspartate
N-carbamoyl-l-aspartic acid
N-carbamoyl-s-aspartic acid
N-carbamoylaspartate
N-carbamoylaspartic acid
Ncd
Ureidosuccinate
Carbamyl-l-aspartate
(2s)-2-(carbamoylamino)butanedioate
N-(aminocarbonyl)-l-aspartate
N-carbamoyl-s-aspartate


Arginine

Arginine is an essential amino acid that is physiologically active in the L-form. In mammals, arginine is formally classified as a semi-essential or conditionally essential amino acid, depending on the developmental stage and health status of the individual. Infants are unable to effectively synthesize arginine, making it nutritionally essential for infants. Adults, however, are able to synthesize arginine in the urea cycle. Arginine can be considered to be a basic amino acid as the part of the side chain nearest to the backbone is long, carbon-containing, and hydrophobic, whereas the end of the side chain is a complex guanidinium group. With a pKa of 12.48, the guanidinium group is positively charged in neutral, acidic, and even most basic environments. Because of the conjugation between the double bond and the nitrogen lone pairs, the positive charge is delocalized. This group is able to form multiple H-bonds. L-Arginine is an amino acid that has numerous functions in the body. It helps dispose of ammonia, is used to make compounds such as nitric oxide, creatine, L-glutamate, and L-proline, and it can be converted into glucose and glycogen if needed. In large doses, L-arginine also stimulates the release of the hormones growth hormone and prolactin. Arginine is a known inducer of mTOR (mammalian target of rapamycin) and is responsible for inducing protein synthesis through the mTOR pathway. mTOR inhibition by rapamycin partially reduces arginine-induced protein synthesis (PMID: 20841502). Catabolic disease states such as sepsis, injury, and cancer cause an increase in arginine utilization, which can exceed normal body production, leading to arginine depletion. Arginine also activates AMP kinase (AMPK) which then stimulates skeletal muscle fatty acid oxidation and muscle glucose uptake, thereby increasing insulin secretion by pancreatic beta-cells (PMID: 21311355). Arginine is found in plant and animal proteins, such as dairy products, meat, poultry, fish, and nuts. The ratio of L-arginine to lysine is also important: soy and other plant proteins have more L-arginine than animal sources of protein.


Fructose 6-phosphate is an important intermediate in the Carbohydrates pathway. The interconversion of glucose-6-phosphate and fructose-6-phosphate, the second step of the Embden-Meyerhof glycolytic pathway, is catalyzed by the enzyme phosphoglucose isomerase (PGI). In gluconeogenesis, fructose-6-phosphate is the immediate precursor of glucose-6-phosphate (wikipedia).


Glucosamine 6-Phosphate

Glucosamine 6-phosphate is normally produced in endothelial cells via the de novo glucosamine synthesis by the enzyme fructose-6-phosphate amidotransferase and the modulation of this pathway by hyperglycemia and glutamine. glutamine-fructose-6-phosphate amidotransferase (GFAT) catalyzes the first committed step in the pathway for biosynthesis of hexosamines in mammals. A member of the N-terminal nucleophile class of amidotransferases, GFAT transfers the amino group from the L-glutamine amide to D-fructose 6-phosphate, producing glutamic acid and glucosamine 6-phosphate. As glucosamine inhibits endothelial nitric oxide synthesis it has important implications for impaired endothelium-dependent relaxation and vascular dysfunction in diabetes mellitus. (PMID 11270676, 11842094).

Phosphoric acid mono-((2r,3s,4r,5r)-5-amino-2,3,4-trihydroxy-6-oxo-hexyl) ester


acetyl-CoA

The main function of coenzyme A is to carry acyl groups (such as the acetyl group) or thioesters. Acetyl-CoA is an important molecule itself. It is the precursor to HMG CoA, which is a vital component in cholesterol and ketone synthesis. (wikipedia). acetyl CoA participates in the biosynthesis of fatty acids and sterols, in the oxidation of fatty acids and in the metabolism of many amino acids. It also acts as a biological acetylating agent.

Ac-coa
Ac-coenzyme a
Ac-s-coa
Ac-s-coenzyme a
Acetyl coenzyme-a
Acetyl-coa
Acetyl-coenzyme a
Acetyl-s-coa
Acetyl-s-coenzyme a
Acetylcoenzyme-a
S-acetate coa
S-acetate coenzyme a
S-acetyl coenzyme a
Accoa
Acetyl coenzyme a
S-acetyl-coa
S-acetyl-coenzyme a
Acetylcoenzyme a


N-Acetyl-D-glucosamine 6-phosphate, also known as N-acetyl-D-glucosamine-6-p or GLCNAC6P, belongs to the class of organic compounds known as acylaminosugars. These are organic compounds containing a sugar linked to a chain through N-acyl group. N-Acetyl-D-glucosamine 6-phosphate is soluble (in water) and a moderately acidic compound (based on its pKa). N-Acetyl-D-glucosamine 6-phosphate has been primarily detected in saliva. Within the cell, N-acetyl-D-glucosamine 6-phosphate is primarily located in the cytoplasm. In humans, N-acetyl-D-glucosamine 6-phosphate is involved in the amino sugar metabolism pathway, the homocarnosinosis pathway, and the glutamate metabolism pathway. N-Acetyl-D-glucosamine 6-phosphate is also involved in several metabolic disorders, some of which include the 2-hydroxyglutric aciduria (D and L form) pathway, the tay-sachs disease pathway, the hyperinsulinism-hyperammonemia syndrome pathway, and the sialuria or french type sialuria pathway. N-Acetyl-D-Glucosamine 6-Phosphate is an intermediate in the metabolism of Aminosugars. It is a substrate for Glucosamine 6-phosphate N-acetyltransferase.


ADP-D-ribose

Adenosine diphosphate ribose is a molecule formed into poly(ADP-ribose) or PAR chains by the enzyme poly ADP ribose polymerase or PARP. PARP is found in every cell nucleus. Its main role is to detect and signal single-strand DNA breaks (SSB) to the enzymatic machinery involved in the SSB repair. PARP activation is an immediate cellular response to metabolic, chemical, or radiation-induced DNA SSB damage. Once PARP detects a SSB, it binds to the DNA, and, after a structural change, begins the synthesis of a poly (ADP-ribose) chain (PAR) as a signal for the other DNA-repairing enzymes such as DNA ligase III (LigIII), DNA polymerase beta, and scaffolding proteins such as X-ray cross-complementing gene 1 (XRCC1). After repairing, the PAR chains are degraded via PAR glycohydrolase (PARG). ADP-ribose binds to and activates the TRPM2 ion channel. Adenosine diphosphate ribose is an intermediate in NAD metabolism. The enzyme NAD(P)+ nucleosidase [EC:3.2.2.6] catalyzes the production of this metabolite from nicotinamide adenine dinucleotide phosphate. This reaction is irreversible and occurs in the cytosol.


Chitin

Chitin is one of the main components in the cell walls of fungi, the exoskeletons of insects and other arthropods (such as crustaceans) as well as fish and frogs. It is a polysaccharide that is constructed from units of acetylglucosamine (more completely, N-acetyl-D-glucose-2-amine). These are linked together in beta-1,4 fashion (in a similar manner to the glucose units which form cellulose). In effect, chitin may be described as cellulose with one hydroxyl group on each monomer replaced by an acetylamine group. This allows for increased hydrogen bonding between adjacent polymers, giving the polymer increased strength. Chitin is the second most abundant polysaccharide in the world (after cellulose). Chitinases break down chitin and are a part of the defence mechanism of mammals against chitin-containing parasites in lower life forms. Under certain circumstances, chitin can act as an allergen. Research using murine models has shown that chitin is a size-dependent microbial-associated molecular pattern (MAMP) that can induce an immunological response via pattern recognition receptors. Medium-sized chitin micro-particles (CMPs) have been shown to induce inflammation, while small-sized CMPs reduce inflammation. Additionally, mammalian chitinases may play a key role in mediating the T-helper 2 cell-driven inflammatory response that is commonly associated with asthma. The high prevalence of asthma among people working with chitinous substances, such as crabs and fungi, suggests that chitin might be an allergen playing a significant role in the development of asthma.


carbonic acid

Carbonic acid (ancient name acid of air or aerial acid) is the only inorganic carbon acid, and has the formula H2CO3. It is also a name sometimes given to solutions of carbon dioxide in water, which contain small amounts of H2CO3. The salts of carbonic acids are called bicarbonates (or hydrogencarbonates) and carbonates. (wikipedia).

Acid of air
Aerial acid
Bisodium carbonate
Calcined
Carbonic acid sodium salt
Consal
Crystol carbonate
Dihydrogen carbonate
Disodium carbonate
Mild alkali
Na-x
Oxyper
Sal soda
Salt of soda
Scotch soda
Soda
Soda ash
Sodium carbonate
Sodium carbonate anhydrous
Sodium carbonate hydrated
Sodium carbonate peroxyhydrate
Solvay soda
Trona soda ash
Tronalight light soda ash
[co(oh)2]
H2co3
Koehlensaeure
Carbonate
Dihydrogen carbonic acid


Phosphoric acid

Phosphoric acid, also known as orthophosphoric acid or phosphoric(V) acid, is a mineral acid with the chemical formula H3PO4. Alternatively, orthophosphoric acid molecules can combine with themselves to form a variety of compounds referred to as phosphoric acids in a more general way. For a discussion of these, see Phosphoric acids and Phosphates. Appears to exist only as a food additive and produced synthetically. --Wikipedia.

Sodium pyrophosphate decahydrate biochemica


5-Phosphoribosylamine, also known as 5-p-beta-D-ribosyl-amine or PRA, 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. 5-Phosphoribosylamine is soluble (in water) and a moderately acidic compound (based on its pKa). In humans, 5-phosphoribosylamine is involved in the purine metabolism pathway, the azathioprine action pathway, the mercaptopurine action pathway, and the homocarnosinosis pathway. 5-Phosphoribosylamine is also involved in several metabolic disorders, some of which include the AICA-ribosiduria pathway, xanthine dehydrogenase deficiency (xanthinuria), the hyperinsulinism-hyperammonemia syndrome pathway, and 4-hydroxybutyric aciduria/succinic semialdehyde dehydrogenase deficiency. Outside of the human body, 5-phosphoribosylamine can be found in a number of food items such as red bell pepper, apple, chinese chestnut, and wild leek. This makes 5-phosphoribosylamine a potential biomarker for the consumption of these food products. 5-Phosphoribosylamine is a substrate for Amidophosphoribosyltransferase and Trifunctional purine biosynthetic protein adenosine-3.


Phosphoribosyl pyrophosphate (PRPP) is a pentosephosphate. The key substance in the biosynthesis of histidine, tryptophan, and purine and pyrimidine nucleotides. It is formed from ribose 5-phosphate by the enzyme ribose-phosphate diphosphokinase. It plays a role in transferring phosphate groups in several reactions. (Wikipedia).

A-d-5-(dihydrogen phosphate) 1-(trihydrogen pyrophosphate) ribofuranose

A-d-ribofuranose, 5-(dihydrogen phosphate) 1-(trihydrogen diphosphate)

Alpha-d-5-(dihydrogen phosphate) 1-(trihydrogen pyrophosphate) ribofuranose

Alpha-d-ribofuranose, 5-(dihydrogen phosphate) 1-(trihydrogen diphosphate)

Alpha-delta-5-(dihydrogen phosphate) 1-(trihydrogen pyrophosphate) ribofuranose

Alpha-d-ribofuranose 5-(dihydrogen phosphate) 1-(trihydrogen diphosphate)

A-d-ribofuranose 5-(dihydrogen phosphate) 1-(trihydrogen diphosphate)

A-d-ribofuranose 5-(dihydrogen phosphoric acid) 1-(trihydrogen diphosphoric acid)

Alpha-d-ribofuranose 5-(dihydrogen phosphoric acid) 1-(trihydrogen diphosphoric acid)

α-d-ribofuranose 5-(dihydrogen phosphate) 1-(trihydrogen diphosphate)

α-d-ribofuranose 5-(dihydrogen phosphoric acid) 1-(trihydrogen diphosphoric acid)


Tetrakis(λ¹-iron(1+) ion) tetrasulfane tetrasulfanide belongs to the class of inorganic compounds known as transition metal sulfides. These are inorganic compounds containing a sulfur atom of an oxidation state of -2, in which the heaviest atom bonded to the oxygen is a transition metal.


Xanthylic acid

Xanthylic acid is an important metabolic intermediate in the Purine Metabolism, and is a product or substrate of the enzymes Inosine monophosphate dehydrogenase (EC 1.1.1.205), Hypoxanthine phosphoribosyltransferase (EC 2.4.2.8), Xanthine phosphoribosyltransferase (EC 2.4.2.22), 5'-Ribonucleotide phosphohydrolase (EC 3.1.3.5), Ap4A hydrolase (EC 3.6.1.17), Nucleoside-triphosphate diphosphatase (EC 3.6.1.19), Phosphoribosylamine-glycine ligase (EC 6.3.4.1), and glutamine amidotransferase (EC 6.3.5.2). (KEGG) Xanthylic acid can also be used in quantitative measurements of the Inosine monophosphate dehydrogenase enzyme activities in purine metabolism. This measurement is important for optimal thiopurine therapy for children with acute lymphoblastic leukaemia (ALL). (PMID: 16725387).


Guanosine monophosphate, also known as guanylic acid or 5'-GMP, belongs to the class of organic compounds known as purine ribonucleoside monophosphates. These are nucleotides consisting of a purine base linked to a ribose to which one monophosphate group is attached. Guanosine monophosphate is slightly soluble (in water) and a moderately acidic compound (based on its pKa). Guanosine monophosphate has been found throughout most human tissues, and has also been detected in multiple biofluids, such as saliva and blood. Guanosine monophosphate can be found anywhere throughout the human cell, such as in mitochondria, golgi, lysosome, and nucleus. Guanosine monophosphate exists in all living organisms, ranging from bacteria to humans. In humans, guanosine monophosphate is involved in the tigecycline action pathway, the homocarnosinosis pathway, the chloramphenicol action pathway, and the azithromycin action pathway. Guanosine monophosphate is also involved in several metabolic disorders, some of which include adenylosuccinate lyase deficiency, xanthine dehydrogenase deficiency (xanthinuria), adenine phosphoribosyltransferase deficiency (aprt), and myoadenylate deaminase deficiency. Outside of the human body, guanosine monophosphate can be found in a number of food items such as black salsify, oyster mushroom, endive, and redcurrant. This makes guanosine monophosphate a potential biomarker for the consumption of these food products. Guanosine 5\'-monophosphate. A guanine nucleotide containing one phosphate group esterified to the sugar moiety and found widely in nature.

5'-gmp
E 626
Gmp
Guanidine monophosphate
Guanosine 5'-monophosphate
Guanosine 5'-phosphate
Guanosine 5'-phosphorate
Guanosine 5'-phosphoric acid
Guanosine monophosphate
Guanosine-5'-monophosphate
Guanosine-5'-phosphate
Guanosine-phosphate
Guanylate
Guanylic acid
Pg
Guanosine 5'-monophosphoric acid
Guanosine monophosphoric acid
Guanosine-5'-monophosphoric acid


Deamido-Nad+

Nicotinic acid adenine dinucleotide phosphate, (NAADP), is a Ca2+-mobilizing second messenger synthesized in response to extracellular stimuli. 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, 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.


NAD(+)

NAD (or Nicotinamide adenine dinucleotide) is used extensively in glycolysis and the citric acid cycle of cellular respiration. The reducing potential stored in NADH can be converted to ATP through the electron transport chain or used for anabolic metabolism. ATP "energy" is necessary for an organism to live. Green plants obtain ATP through photosynthesis, while other organisms obtain it by cellular respiration. (wikipedia). Nicotinamide adenine dinucleotide is a A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed).

3-carbamoyl-1-d-ribofuranosylpyridinium hydroxide 5'-ester with adenosine 5'-pyrophosphate

3-carbamoyl-1-beta-d-ribofuranosylpyridinium hydroxide 5'-ester with adenosine 5'-pyrophosphate inner salt

3-carbamoyl-1-beta-delta-ribofuranosylpyridinium hydroxide 5'-ester with adenosine 5'-pyrophosphate inner salt

3-carbamoyl-1-delta-ribofuranosylpyridinium hydroxide 5'-ester with adenosine 5'-pyrophosphate

Nicotinamide adenine dinucleotide oxidized

Beta-nicotinamide adenine dinucleotide trihydrate