349PathwayThreonine and 2-Oxobutanoate Degradation 2-oxobutanoate, also known as 2-Ketobutyric acid, is a 2-keto acid that is commonly produced in the metabolism of amino acids such as methionine and threonine. Like other 2-keto acids, degradation of 2-oxobutanoate occurs in the mitochondrial matrix and begins with oxidative decarboxylation to its acyl coenzyme A derivative, propionyl-CoA. This reaction is mediated by a class of large, multienzyme complexes called 2-oxo acid dehydrogenase complexes. While no 2-oxo acid dehydrogenase complex is specific to 2-oxobutanoate, numerous complexes can catalyze its reaction. In this pathway the branched-chain alpha-keto acid dehydrogenase complex is depicted. All 2-oxo acid dehydrogenase complexes consist of three main components: a 2-oxo acid dehydrogenase (E1) with a thiamine pyrophosphate cofactor, a dihydrolipoamide acyltransferase (E2) with a lipoate cofactor, and a dihydrolipoamide dehydrogenase (E3) with a flavin cofactor. E1 binds the 2-oxobutanoate to the lipoate on E2, which then transfers the propionyl group to coenzyme A, producing propionyl-CoA and reducing the lipoate. E3 then transfers protons to NAD in order to restore the lipoate. Propionyl-CoA carboxylase transforms the propionyl-CoA to S-methylmalonyl-CoA, which is then converted to R-methylmalonyl-CoA via methylmalonyl-CoA epimerase. In the final step, methylmalonyl-CoA mutase acts on the R-methylmalonyl-CoA to produce succinyl-CoA. MetabolicPW000166CenterPathwayVisualizationContext18125002200#000099PathwayVisualization111349Threonine and 2-Oxobutanoate Degradation 2-oxobutanoate, also known as 2-Ketobutyric acid, is a 2-keto acid that is commonly produced in the metabolism of amino acids such as methionine and threonine. Like other 2-keto acids, degradation of 2-oxobutanoate occurs in the mitochondrial matrix and begins with oxidative decarboxylation to its acyl coenzyme A derivative, propionyl-CoA. This reaction is mediated by a class of large, multienzyme complexes called 2-oxo acid dehydrogenase complexes. While no 2-oxo acid dehydrogenase complex is specific to 2-oxobutanoate, numerous complexes can catalyze its reaction. In this pathway the branched-chain alpha-keto acid dehydrogenase complex is depicted. All 2-oxo acid dehydrogenase complexes consist of three main components: a 2-oxo acid dehydrogenase (E1) with a thiamine pyrophosphate cofactor, a dihydrolipoamide acyltransferase (E2) with a lipoate cofactor, and a dihydrolipoamide dehydrogenase (E3) with a flavin cofactor. E1 binds the 2-oxobutanoate to the lipoate on E2, which then transfers the propionyl group to coenzyme A, producing propionyl-CoA and reducing the lipoate. E3 then transfers protons to NAD in order to restore the lipoate. Propionyl-CoA carboxylase transforms the propionyl-CoA to S-methylmalonyl-CoA, which is then converted to R-methylmalonyl-CoA via methylmalonyl-CoA epimerase. In the final step, methylmalonyl-CoA mutase acts on the R-methylmalonyl-CoA to produce succinyl-CoA. Metabolic131554SubPathway4753Compound2316102SubPathway4763Compound23172SubPathway477808Compound2148511481338Bobik TA, Rasche ME: Identification of the human methylmalonyl-CoA racemase gene based on the analysis of prokaryotic gene arrangements. Implications for decoding the human genome. J Biol Chem. 2001 Oct 5;276(40):37194-8. doi: 10.1074/jbc.M107232200. Epub 2001 Jul 31.349Pathway14869655933de Kok A, Hengeveld AF, Martin A, Westphal AH: The pyruvate dehydrogenase multi-enzyme complex from Gram-negative bacteria. Biochim Biophys Acta. 1998 Jun 29;1385(2):353-66.349Pathway148712795594Fries M, Jung HI, Perham RN: Reaction mechanism of the heterotetrameric (alpha2beta2) E1 component of 2-oxo acid dehydrogenase multienzyme complexes. Biochemistry. 2003 Jun 17;42(23):6996-7002. doi: 10.1021/bi027397z.349Pathway14882567699Jansen R, Kalousek F, Fenton WA, Rosenberg LE, Ledley FD: Cloning of full-length methylmalonyl-CoA mutase from a cDNA library using the polymerase chain reaction. Genomics. 1989 Feb;4(2):198-205.349Pathway14893718468Paxton R, Scislowski PW, Davis EJ, Harris RA: Role of branched-chain 2-oxo acid dehydrogenase and pyruvate dehydrogenase in 2-oxobutyrate metabolism. Biochem J. 1986 Mar 1;234(2):295-303.349Pathway149011752427Zhou ZH, McCarthy DB, O'Connor CM, Reed LJ, Stoops JK: The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes. Proc Natl Acad Sci U S A. 2001 Dec 18;98(26):14802-7. doi: 10.1073/pnas.011597698.349Pathway149112361482Edgar AJ: The human L-threonine 3-dehydrogenase gene is an expressed pseudogene. BMC Genet. 2002 Oct 2;3:18. Epub 2002 Oct 2.349Pathway1CellCL:00000005HepatocyteCL:00001823NeuronCL:00005406MyocyteCL:00001872Platelet CL:00002334CardiomyocyteCL:00007468Beta cellCL:00006397Epithelial CellCL:00000661Homo sapiens9606EukaryoteHuman3Escherichia coli562Prokaryote18Saccharomyces cerevisiae4932EukaryoteYeast4Arabidopsis thaliana3702EukaryoteThale cress23Pseudomonas aeruginosa287Prokaryote12Mus musculus10090EukaryoteMouse5Bos taurus9913EukaryoteCattle17Rattus norvegicus10116EukaryoteRat10Drosophila melanogaster7227EukaryoteFruit fly6Caenorhabditis elegans6239EukaryoteRoundworm24Solanum lycopersicum4081EukaryoteTomato49Bathymodiolus platifrons220390EukaryoteDeep sea mussel21Xenopus laevis8355EukaryoteAfrican clawed frog60Nitzschia sp.0001EukaryoteNitzschia42Bacteria2ProkaryoteBacteria19Schizosaccharomyces pombe4896Eukaryote25Escherichia coli (strain K12)83333Prokaryote135Felinus9685EukaryoteCat240Plasmodium falciparums121Eukaryote11Extracellular SpaceGO:00056151CytosolGO:000582931Periplasmic SpaceGO:000562035ChloroplastGO:00095075CytoplasmGO:00057372MitochondrionGO:00057393Mitochondrial MatrixGO:00057596LysosomeGO:00057644PeroxisomeGO:000577710Cell MembraneGO:000588614Mitochondrial Outer MembraneGO:000574132Inner MembraneGO:007025824Mitochondrial Intermembrane SpaceGO:00057587Endoplasmic Reticulum MembraneGO:000578913Endoplasmic ReticulumGO:000578312Mitochondrial Inner MembraneGO:000574327Peroxisome MembraneGO:00057788Smooth Endoplasmic Reticulum GO:000579025Golgi ApparatusGO:000579416Lysosomal LumenGO:004320220Endoplasmic Reticulum LumenGO:000578834Plant-Type VacuoleGO:000032539Mitochondrial membraneGO:003196615NucleusGO:000563419Sarcoplasmic ReticulumGO:00165291LiverBTO:00007597293Sympathetic Nervous SystemBTO:00018324Adrenal MedullaBTO:00000497189MuscleBTO:00008871411824BrainBTO:0000142891628StomachBTO:0001307155262Endothelium BTO:00003937Nervous SystemBTO:000148418PancreasBTO:000098825IntestineBTO:00006488Blood VesselBTO:0001102741115111PW_BS0000152111PW_BS000002107313PW_BS00010710813PW_BS000108105113PW_BS000105188118PW_BS0000241873118PW_BS0000242253541PW_BS0000243183123PW_BS000024315123PW_BS0000241321121PW_BS0001321141112PW_BS000114124151PW_BS000124409115PW_BS0001151181171PW_BS0001181371117PW_BS0001372991101PW_BS0000244831110PW_BS000115388161PW_BS000112208116PW_BS0000248511PW_BS0000083211PW_BS000003151141PW_BS0001514311PW_BS0000041115121PW_BS0001111333121PW_BS0001331122121PW_BS000112122551PW_BS000122406351PW_BS000115407251PW_BS0001151355171PW_BS0001351203171PW_BS0001201192171PW_BS0001192975101PW_BS0000244793101PW_BS0001154812101PW_BS000115205561PW_BS000024501361PW_BS000115206261PW_BS0000249611PW_BS0000095411PW_BS00000513121PW_BS00001314101PW_BS000014541315PW_BS000054221411PW_BS0000221471241PW_BS0001471601181PW_BS0001601985181PW_BS0000242771218PW_BS0000242156181PW_BS0000242916491PW_BS0000242924491PW_BS0000242941141PW_BS0000243331212PW_BS0000281136121PW_BS0001133344121PW_BS0000281151012PW_BS00011534713125PW_BS00002832914121PW_BS00002829341PW_BS000024109323PW_BS000109408451PW_BS000115126651PW_BS000126412125PW_BS000115405105PW_BS0001154251355PW_BS0001153821451PW_BS0001003744171PW_BS0000534436171PW_BS0001154461217PW_BS0001153761017PW_BS00005346013175PW_BS00011539914171PW_BS0001134824101PW_BS0001153016101PW_BS0000244781010PW_BS00011548414101PW_BS000115502461PW_BS000115207661PW_BS000024209106PW_BS0000243891461PW_BS00011211PW_BS000001193513PW_BS000019204111PW_BS000020422411PW_BS000042509516PW_BS000050261115PW_BS000026101711PW_BS00001049711PW_BS000049117131PW_BS000117103331PW_BS00010385241011PW_BS00008521217181PW_BS0000242137181PW_BS0000241613181PW_BS000161311511PW_BS000031181311PW_BS0000182892491PW_BS0000242905491PW_BS000024253541PW_BS000024224241PW_BS00002434141121PW_BS00002834695126PW_BS00002832711125PW_BS00002834524121PW_BS00002833217121PW_BS0000283317121PW_BS000028711PW_BS0000074182451PW_BS0001154239556PW_BS0001154241155PW_BS0001151231751PW_BS000123383751PW_BS00010045424171PW_BS00011545895176PW_BS00011545911175PW_BS00011544717171PW_BS0001153987171PW_BS00011348924101PW_BS00011529817101PW_BS0000244957101PW_BS0001155062461PW_BS0001155131761PW_BS000115390761PW_BS000112171211PW_BS000017592711PW_BS00005929111PW_BS000029111811PW_BS0000115811411PW_BS0000586131PW_BS0000061021231PW_BS0001021041431PW_BS000104101531PW_BS0001011553241PW_BS0001551783211PW_BS00017816212181PW_BS00016219914181PW_BS0000241632181PW_BS00016321013181PW_BS000024222341PW_BS000024226441PW_BS00002417018PW_BS0001701951318PW_BS0000242491341PW_BS00002413412121PW_BS0001343361121PW_BS00002812915121PW_BS000129350114121PW_BS00002833527121PW_BS00002813013121PW_BS0001303683601PW_BS0000282881441PW_BS0000243841251PW_BS00010043311451PW_BS0001151251351PW_BS000125429151PW_BS0001154141551PW_BS0001154222751PW_BS00011512112171PW_BS000121468114171PW_BS00011513613171PW_BS0001364641171PW_BS00011545015171PW_BS00011537527171PW_BS00005348012101PW_BS00011549127101PW_BS00011530013101PW_BS0000243911261PW_BS0001125082761PW_BS0001153951361PW_BS0001131861221PW_BS000024185321PW_BS0000248911421PW_BS000552432511PW_BS0000432811611PW_BS000028951721PW_BS000095100521PW_BS00010014117191PW_BS0001411572241PW_BS0001572164181PW_BS0000242231241PW_BS0000243221231PW_BS00002435625121PW_BS00002816611PW_BS000166943PW_BS0000944192551PW_BS00011545525171PW_BS00011549025101PW_BS0001155072561PW_BS0001153612011PW_BS00003612711651PW_BS00012715612241PW_BS00015617912211PW_BS0001792111018PW_BS0000242273441PW_BS000024302116101PW_BS000024337116121PW_BS0000283583912PW_BS00002836912601PW_BS000028448116171PW_BS0001157028511PW_BS00007016212PW_BS0000163211515PW_BS000032397113PW_BS00003927151PW_BS00002746114PW_BS0000466618518PW_BS00006672513PW_BS000072612517PW_BS0000615181PW_BS000051231511PW_BS000023918511PW_BS000091892PW_BS000089971521PW_BS00009714315191PW_BS0001431465191PW_BS0001462171518PW_BS00002421815181PW_BS0000241901118PW_BS0000242811251PW_BS0000241644PW_BS0001642851041PW_BS0000243081011PW_BS00002412815121PW_BS0001283511512PW_BS00002835325127PW_BS000028184121PW_BS0000244101551PW_BS000115435155PW_BS00011544415171PW_BS00011547225177PW_BS0001154701517PW_BS00011548515101PW_BS0001154991510PW_BS0001155161561PW_BS000115517156PW_BS000115471914PW_BS00004731323PW_BS00002470231351PW_BS000512102032401PW_BS000577109L-ThreonineHMDB0000167Threonine is an essential amino acid in humans. It is abundant in human plasma, particularly in newborns. Severe deficiency of threonine causes neurological dysfunction and lameness in experimental animals. Threonine is an immunostimulant which promotes the growth of thymus gland. It also can probably promote cell immune defense function. This amino acid has been useful in the treatment of genetic spasticity disorders and multiple sclerosis at a dose of 1 gram daily. It is highly concentrated in meat products, cottage cheese and wheat germ. (http://www.dcnutrition.com/AminoAcids/) The threonine content of most of the infant formulas currently on the market is approximately 20% higher than the threonine concentration in human milk. Due to this high threonine content the plasma threonine concentrations are up to twice as high in premature infants fed these formulas than in infants fed human milk. The whey proteins which are used for infant formulas are sweet whey proteins. Sweet whey results from cheese production. Threonine catabolism in mammals appears to be due primarily (70-80%) to the activity of threonine dehydrogenase (EC 1.1.1.103) that oxidizes threonine to 2-amino-3-oxobutyrate, which forms glycine and acetyl CoA, whereas threonine dehydratase (EC 4.2.1.16) that catabolizes threonine into 2-oxobutyrate and ammonia, is significantly less active. Increasing the threonine plasma concentrations leads to accumulation of threonine and glycine in the brain. Such accumulation affects the neurotransmitter balance which may have consequences for the brain development during early postnatal life. Thus, excessive threonine intake during infant feeding should be avoided. (PMID 9853925).72-19-5C00188628816857THR6051DB00156C[C@@H](O)[C@H](N)C(O)=OC4H9NO3InChI=1S/C4H9NO3/c1-2(6)3(5)4(7)8/h2-3,6H,5H2,1H3,(H,7,8)/t2-,3+/m1/s1AYFVYJQAPQTCCC-GBXIJSLDSA-N(2S,3R)-2-amino-3-hydroxybutanoic acid119.1192119.0582431590.603L-threonine00FDB011999Threonin;(2s,3r)-(-)-threonine;(2s,3r)-2-amino-3-hydroxybutyrate;(2s,3r)-2-amino-3-hydroxybutyric acid;(r-(r*,s*))-2-amino-3-hydroxybutanoate;(r-(r*,s*))-2-amino-3-hydroxybutanoic acid;(s)-threonine;2-amino-3-hydroxybutanoate;2-amino-3-hydroxybutanoic acid;2-amino-3-hydroxybutyrate;2-amino-3-hydroxybutyric acid;L-(-)-threonine;L-2-amino-3-hydroxybutyrate;L-2-amino-3-hydroxybutyric acid;L-alpha-amino-beta-hydroxybutyrate;L-alpha-amino-beta-hydroxybutyric acid;Threonine;[r-(r*,s*)]-2-amino-3-hydroxybutanoate;[r-(r*,s*)]-2-amino-3-hydroxybutanoic acid;[r-(r*,s*)]-2-amino-3-hydroxy-butanoate;[r-(r*,s*)]-2-amino-3-hydroxy-butanoic acid;(2s)-threonine;(2s,3r)-2-amino-3-hydroxybutanoic acid;L-threonin;T;Thr;(2s,3r)-2-amino-3-hydroxybutanoate;L-a-amino-b-hydroxybutyrate;L-a-amino-b-hydroxybutyric acid;L-α-amino-β-hydroxybutyrate;L-α-amino-β-hydroxybutyric acidPW_C000109Thr268915269025644107564510858851056908188690918783792254241431842415315790261327903811412257612412258040912514811812515213712672529912673448312831838812832820832-Ketobutyric acidHMDB00000052-Ketobutyric acid is a substance that is involved in the metabolism of many amino acids (glycine, methionine, valine, leucine, serine, threonine, isoleucine) as well as propanoate metabolism and C-5 branched dibasic acid metabolism. More specifically, alpha-ketobutyric acid is a product of the lysis of cystathionine. It is also one of the degradation products of threonine. It can be converted into propionyl-CoA (and subsequently methylmalonyl CoA, which can be converted into succinyl CoA, a citric acid cycle intermediate), and thus enter the citric acid cycle.600-18-0C0010958308312-OXOBUTANOATE57DB04553CCC(=O)C(O)=OC4H6O3InChI=1S/C4H6O3/c1-2-3(5)4(6)7/h2H2,1H3,(H,6,7)TYEYBOSBBBHJIV-UHFFFAOYSA-N2-oxobutanoic acid102.0886102.031694058-0.1112-oxobutanoic acid0-1FDB0033592-ketobutanoate;2-ketobutanoic acid;2-ketobutyrate;2-oxo-butanoate;2-oxo-butanoic acid;2-oxo-butyrate;2-oxo-butyric acid;2-oxo-n-butyrate;2-oxo-n-butyric acid;2-oxobutanoate;2-oxobutanoic acid;2-oxobutyrate;2-oxobutyric acid;3-methylpyruvate;3-methylpyruvic acid;Methyl-pyruvate;Methyl-pyruvic acid;Propionyl-formate;Propionyl-formic acid;A-keto-n-butyrate;A-keto-n-butyric acid;A-ketobutyrate;A-ketobutyric acid;A-oxo-n-butyrate;A-oxo-n-butyric acid;A-oxobutyrate;A-oxobutyric acid;Alpha-keto-n-butyrate;Alpha-keto-n-butyric acid;Alpha-ketobutric acid;Alpha-ketobutyrate;Alpha-ketobutyric acid;Alpha-oxo-n-butyrate;Alpha-oxo-n-butyric acid;Alpha-oxobutyrate;Alpha-oxobutyric acid;2-ketobutyric acid;3-methyl pyruvic acid;3-methyl pyruvate;α-ketobutyrate;α-ketobutyric acid;α-oxo-n-butyrate;α-oxo-n-butyric acidPW_C0000032KBA33781868226923827415183832254227247812613278163111786431337902711211992212212217612412227440612257740712271613512472811812482912012514911912531229712633329912643847912672648112685820512789638812800750112831920635AmmoniaHMDB0000051Ammonia 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.7664-41-7C0001422216134AMMONIA217NH3NInChI=1S/H3N/h1H3QGZKDVFQNNGYKY-UHFFFAOYSA-Nammonia17.030517.0265491011ammonia01FDB003908Ammonia 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 strongPW_C000035NH397911251338142443824791355014146854253322257235338111601614770221607177205117861981184827711885215127082911271829276966225770462947732913377343132774693337749911377539334775971157798534777993112780723297924429380650135806571191162031091199211221200494081200531261201364071203434061203634121204624051210461241211614251221193821228003741228054431229931201230104461230963761236101181237334601246713991253112971254274821254313011255024811256634791257084781261022991262744841269665021269702071270392061271585011272002091276003881278373891148Pyridoxal 5'-phosphateHMDB0001491This 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.54-47-7C00018105118405PYRIDOXAL_PHOSPHATE1022DB00114CC1=NC=C(COP(O)(O)=O)C(C=O)=C1OC8H10NO6PInChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14)NGVDGCNFYWLIFO-UHFFFAOYSA-N[(4-formyl-5-hydroxy-6-methylpyridin-3-yl)methoxy]phosphonic acid247.1419247.024573569-1.643pyridoxal phosphate0-2FDB021820Apolon b6;Biosechs;Codecarboxylase;Coenzyme b6;Hairoxal;Hexermin-p;Hi-pyridoxin;Hiadelon;Himitan;Pal-p;Plp;Phosphopyridoxal;Phosphopyridoxal coenzyme;Pidopidon;Piodel;Pydoxal;Pyridoxal 5'-phosphate;Pyridoxal 5-phosphate;Pyridoxal p;Pyridoxal phosphate;Pyridoxal-p;Pyridoxyl phosphate;Pyromijin;Sechvitan;Vitahexin-p;Vitazechs;3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-4-pyridinecarboxaldehyde;3-hydroxy-5-(hydroxymethyl)-2-methylisonicotinaldehyde 5-phosphate;Phosphoric acid mono-(4-formyl-5-hydroxy-6-methyl-pyridin-3-ylmethyl) ester;Pyridoxal 5-monophosphoric acid ester;Pyridoxal 5'-(dihydrogen phosphate);Pyridoxal-5'-phosphate;Pyridoxal 5'-phosphoric acid;3-hydroxy-5-(hydroxymethyl)-2-methylisonicotinaldehyde 5-phosphoric acid;Phosphate mono-(4-formyl-5-hydroxy-6-methyl-pyridin-3-ylmethyl) ester;Pyridoxal 5-monophosphate ester;Pyridoxal 5'-(dihydrogen phosphoric acid);Pyridoxal 5-phosphoric acid;Pyridoxal phosphoric acid;Pyridoxal-5'-phosphoric acidPW_C001148Pyr-5'P182324453518122140119696201110421450501458262120102150495325111541611754211035441118545512055671325581133653385701816071672057216212722221311858161121751511262331126281812684289126892907701725377037225770412937705222477526112777643417797334677979327782923457885533278862331806961359863071199121221200241241200294061200874071208174181211494231211554241220691231220763831228341191234024541237214581237274591246204471246273981253022971254022991254074791254584811258034891262242981262314951269423881269475011269962061272585061277865131277933901099Coenzyme AHMDB0001423Coenzyme A (CoA, CoASH, or HSCoA) is a coenzyme notable for its role in the synthesis and oxidization of fatty acids and the oxidation of pyruvate in the citric acid cycle. It is adapted from beta-mercaptoethylamine, panthothenate, and adenosine triphosphate. It is also a parent compound for other transformation products, including but not limited to, phenylglyoxylyl-CoA, tetracosanoyl-CoA, and 6-hydroxyhex-3-enoyl-CoA. Coenzyme A is synthesized in a five-step process from pantothenate and cysteine. In the first step pantothenate (vitamin B5) is phosphorylated to 4'-phosphopantothenate by the enzyme pantothenate kinase (PanK, CoaA, CoaX). In the second step, a cysteine is added to 4'-phosphopantothenate by the enzyme phosphopantothenoylcysteine synthetase (PPC-DC, CoaB) to form 4'-phospho-N-pantothenoylcysteine (PPC). In the third step, PPC is decarboxylated to 4'-phosphopantetheine by phosphopantothenoylcysteine decarboxylase (CoaC). In the fourth step, 4'-phosphopantetheine is adenylylated to form dephospho-CoA by the enzyme phosphopantetheine adenylyl transferase (CoaD). Finally, dephospho-CoA is phosphorylated using ATP to coenzyme A by the enzyme dephosphocoenzyme A kinase (CoaE). Since coenzyme A is, in chemical terms, a thiol, it can react with carboxylic acids to form thioesters, thus functioning as an acyl group carrier. CoA assists in transferring fatty acids from the cytoplasm to the mitochondria. A molecule of coenzyme A carrying an acetyl group is also referred to as acetyl-CoA. When it is not attached to an acyl group, it is usually referred to as 'CoASH' or 'HSCoA'. Coenzyme A is also the source of the phosphopantetheine group that is added as a prosthetic group to proteins such as acyl carrier proteins and formyltetrahydrofolate dehydrogenase. Acetyl-CoA is an important molecule itself. It is the precursor to HMG CoA which is a vital component in cholesterol and ketone synthesis. Furthermore, it contributes an acetyl group to choline to produce acetylcholine in a reaction catalysed by choline acetyltransferase. Its main task is conveying the carbon atoms within the acetyl group to the citric acid cycle to be oxidized for energy production (Wikipedia).85-61-0C0001068161146900CO-A6557CC(C)(COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C1N=CN=C2N)[C@@H](O)C(=O)NCCC(=O)NCCSC21H36N7O16P3SInChI=1S/C21H36N7O16P3S/c1-21(2,16(31)19(32)24-4-3-12(29)23-5-6-48)8-41-47(38,39)44-46(36,37)40-7-11-15(43-45(33,34)35)14(30)20(42-11)28-10-27-13-17(22)25-9-26-18(13)28/h9-11,14-16,20,30-31,48H,3-8H2,1-2H3,(H,23,29)(H,24,32)(H,36,37)(H,38,39)(H2,22,25,26)(H2,33,34,35)/t11-,14-,15-,16+,20-/m1/s1RGJOEKWQDUBAIZ-IBOSZNHHSA-N{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-2-({[hydroxy({hydroxy[(3R)-3-hydroxy-2,2-dimethyl-3-({2-[(2-sulfanylethyl)carbamoyl]ethyl}carbamoyl)propoxy]phosphoryl}oxy)phosphoryl]oxy}methyl)oxolan-3-yl]oxy}phosphonic acid767.534767.115208365-2.2210coenzyme A0-4FDB022614Acetoacetyl coenzyme a sodium salt;Coa;Coa hydrate;Coa-sh;Coash;Coenzyme a;Coenzyme a hydrate;Coenzyme a-sh;Coenzyme ash;Coenzymes a;Depot-zeel;Propionyl coa;Propionyl coenzyme a;S-propanoate;S-propanoate coa;S-propanoate coenzyme a;S-propanoic acid;S-propionate coa;S-propionate coenzyme a;Zeel;[(2r,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl 3-hydroxy-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)-2,2-dimethyl-4-oxobutyl dihydrogen diphosphatePW_C001099CoA2114386884538792289217240759241422459528132928623133421133511846181046295848421448655448796523210252471045280103547712457341085777101602315560751616384164681786930160696116269731997083188710816372931987347210745822282291519081226909022491241709215195130132991531824925488494261631576907293771191337722213477230329772921117755013277555334775631127763333677672129779961157804733278056350784133357856713079259333799743318000536880620118806273748063511980665376938283829383438398674288110555389110561390115842399115847398119951406120147405120231384120305122120634407120762117121406123121421433121521125121666429121682408121714414122404422122741120122904121122960135123965447123979468124079136124220464124265450124974375125341479125509478125579480125592484125634297126084481126549491126560482126746300126884501127046209127109391127301205127540206127667388128121508128133502128340395140751186140763185140767891721NADHMDB0000902NAD (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).53-84-9C00003589315846NAD5682NC(=O)C1=C[N+](=CC=C1)[C@@H]1O[C@H](COP([O-])(=O)OP(O)(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)N2C=NC3=C2N=CN=C3N)[C@@H](O)[C@H]1OC21H27N7O14P2InChI=1S/C21H27N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1-4,7-8,10-11,13-16,20-21,29-32H,5-6H2,(H5-,22,23,24,25,33,34,35,36,37)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1BAWFJGJZGIEFAR-NNYOXOHSSA-N1-[(2R,3R,4S,5R)-5-({[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphono}oxy)(hydroxy)phosphoryl]oxy}methyl)-3,4-dihydroxyoxolan-2-yl]-3-(C-hydroxycarbonimidoyl)-1lambda5-pyridin-1-ylium663.4251663.109121631-2.5281-[(2R,3R,4S,5R)-5-{[({[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphono}oxy(hydroxy)phosphoryl)oxy]methyl}-3,4-dihydroxyoxolan-2-yl]-3-(C-hydroxycarbonimidoyl)-1lambda5-pyridin-1-ylium0-1FDB0223093-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;Adenine-nicotinamide dinucleotide;Co-i;Codehydrase i;Codehydrogenase i;Coenzyme i;Cozymase;Cozymase i;Diphosphopyridine nucleotide;Diphosphopyridine nucleotide oxidized;Endopride;Nad trihydrate;Nad-oxidized;Nicotinamide adenine dinucleotide;Nicotinamide adenine dinucleotide oxidized;Nicotinamide dinucleotide;Nicotineamide adenine dinucleotide;Oxidized diphosphopyridine nucleotide;Pyridine nucleotide diphosphate;[(3s,2r,4r,5r)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl {[(3s,2r,4r,5r)-5-(3-carbamoylpyridyl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxyphosphoryl) hydrogen phosphate;[adenylate-32-p]-nad;Beta-diphosphopyridine nucleotide;Beta-nad;Beta-nicotinamide adenine dinucleotide;Beta-nicotinamide adenine dinucleotide trihydrate;Dpn;Nad;Nad+;Nadide;B-nad;β-nadPW_C000721NAD14041503353865110111421134431273514665422294927791728352931079480718481318481928490264960315167955238103533411153601125469123548212555901355610118569610057381085827141591214759421516024155607215760761616385164691786772117689016070121887097163717420571972067405198745922282412268359225908522411819216123222491300629813018300132562234240432242619315771041327712013377209134773703317765033677667334777023327770913077915113779833477840635680006368806901199382512411055238811275016611285394119929122119952406120171407120834419120984408121159425121242126121259429121817383122614384122742120123130447123141136123419455123549374123731460123812443123829464124370398125187121125319297125342479125530481125806299125825490125924482126515495126765480126885501127278507127383502128089390128360391128428395140757185988Propionyl-CoAHMDB0001275Propionyl-CoA is an intermediate in the metabolism of propanoate. Propionic aciduria is caused by an autosomal recessive disorder of propionyl coenzyme A (CoA) carboxylase deficiency (EC 6.4.1.3). In propionic aciduria, propionyl CoA accumulates within the mitochondria in massive quantities; free carnitine is then esterified, creating propionyl carnitine, which is then excreted in the urine. Because the supply of carnitine in the diet and from synthesis is limited, such patients readily develop carnitine deficiency as a result of the increased loss of acylcarnitine derivatives. This condition demands supplementation of free carnitine above the normal dietary intake to continue to remove (detoxify) the accumulating organic acids. Propionyl-CoA is a substrate for Acyl-CoA dehydrogenase (medium-chain specific, mitochondrial), Acetyl-coenzyme A synthetase 2-like (mitochondrial), Propionyl-CoA carboxylase alpha chain (mitochondrial), Methylmalonate-semialdehyde dehydrogenase (mitochondrial), Trifunctional enzyme beta subunit (mitochondrial), 3-ketoacyl-CoA thiolase (peroxisomal), Acyl-CoA dehydrogenase (long-chain specific, mitochondrial), Malonyl-CoA decarboxylase (mitochondrial), Acetyl-coenzyme A synthetase (cytoplasmic), 3-ketoacyl-CoA thiolase (mitochondrial) and Propionyl-CoA carboxylase beta chain (mitochondrial). (PMID: 10650319).317-66-8C0010043916415539PROPIONYL-COA388310CCC(=O)SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C1N=CN=C2NC24H40N7O17P3SInChI=1S/C24H40N7O17P3S/c1-4-15(33)52-8-7-26-14(32)5-6-27-22(36)19(35)24(2,3)10-45-51(42,43)48-50(40,41)44-9-13-18(47-49(37,38)39)17(34)23(46-13)31-12-30-16-20(25)28-11-29-21(16)31/h11-13,17-19,23,34-35H,4-10H2,1-3H3,(H,26,32)(H,27,36)(H,40,41)(H,42,43)(H2,25,28,29)(H2,37,38,39)/t13-,17-,18-,19?,23-/m1/s1QAQREVBBADEHPA-UXYNFSPESA-N{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-2-({[hydroxy({[hydroxy({3-hydroxy-2,2-dimethyl-3-[(2-{[2-(propanoylsulfanyl)ethyl]carbamoyl}ethyl)carbamoyl]propoxy})phosphoryl]oxy})phosphoryl]oxy}methyl)oxolan-3-yl]oxy}phosphonic acid823.597823.141423115-2.169[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-2-({[hydroxy([hydroxy(3-hydroxy-2,2-dimethyl-3-[(2-{[2-(propanoylsulfanyl)ethyl]carbamoyl}ethyl)carbamoyl]propoxy)phosphoryl]oxy)phosphoryl]oxy}methyl)oxolan-3-yl]oxyphosphonic acid0-4FDB0225292-methylacetyl-coa;2-methylacetyl-coenzyme a;Propanoyl-coa;Propanoyl-coenzyme a;Propionyl-coa;Propionyl-coenzyme a;Alpha-methylacetyl-coa;Alpha-methylacetyl-coenzyme aPW_C000988PropCoA127781694322854244554914139091224776413347843611278556111786361331209951221215764071216814081222664061235601351241331191242313741248191201259352971264304791265574821265684811273952051279975011281305021281412061144NADHHMDB0001487NADH is the reduced form of NAD+, and NAD+ is the oxidized form of NADH, A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). It forms NADP with the addition of a phosphate group to the 2' position of the adenosyl nucleotide through an ester linkage.(Dorland, 27th ed).58-68-4C0000443915316908NADH388299DB00157NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](CO[P@](O)(=O)O[P@](O)(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)N2C=NC3=C(N)N=CN=C23)[C@@H](O)[C@H]1OC21H29N7O14P2InChI=1S/C21H29N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1,3-4,7-8,10-11,13-16,20-21,29-32H,2,5-6H2,(H2,23,33)(H,34,35)(H,36,37)(H2,22,24,25)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1BOPGDPNILDQYTO-NNYOXOHSSA-N[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy]({[(2R,3S,4R,5R)-5-(3-carbamoyl-1,4-dihydropyridin-1-yl)-3,4-dihydroxyoxolan-2-yl]methoxy})phosphinic acid665.441665.124771695-2.358NADH0-2FDB0226491,4-dihydronicotinamide adenine dinucleotide;Dpnh;Dihydrocodehydrogenase i;Dihydrocozymase;Dihydronicotinamide adenine dinucleotide;Dihydronicotinamide mononucleotide;Enada;Nadh;Nadh2;Reduced codehydrogenase i;Reduced diphosphopyridine nucleotide;Reduced nicotinamide adenine diphosphate;Reduced nicotinamide-adenine dinucleotide;B-dpnh;B-nadh;Beta-dpnh;Beta-nadh;Nicotinamide adenine dinucleotide (reduced);Reduced nicotinamide adenine dinucleotidePW_C001144NADH143415334908648101115212755146954223049278117283629310994806184812184821284904649593151699552401035332111535811254661235479125559313556981005737108582914159151475945151602715560791616387164721786771117689316070111887099163717220571952067462222824422683602259086224118091981182121612320249130032981301530013255223424033224261831577107132771231337720813477371331776513367766833477700332777071307791711377986347800093688069111993822124110549388112854941158381181199554061201724071203781221209864081211624251212441261216934291218183831226163841227451201231274471231381361235513741237344601238144431242424641243713981251891211253454791255314811257622971258082991259264821265164951267674801268885011273855021280903901283623911284293951407591851060Thiamine pyrophosphateHMDB0001372Thiamine pyrophosphate is the active form of thiamine, and it serves as a cofactor for several enzymes involved primarily in carbohydrate catabolism. The enzymes are important in the biosynthesis of a number of cell constituents, including neurotransmitters, and for the production of reducing equivalents used in oxidant stress defenses and in biosyntheses and for synthesis of pentoses used as nucleic acid precursors. The chemical structure of TPP is that of an aromatic methylaminopyrimidine ring, linked via a methylene bridge to a methylthiazolium ring with a pyrophosphate group attached to a hydroxyethyl side chain. In non-enzymatic model studies it has been demonstrated that the thiazolium ring can catalyse reactions which are similar to those of TPP-dependent enzymes but several orders of magnitude slower. Using infrared and NMR spectrophotometry it has been shown that the dissociation of the proton from C2 of the thiazolium ring is necessary for catalysis; the abstraction of the proton leads to the formation of a carbanion (ylid) with the potential for a nucleophilic attack on the carbonyl group of the substrate. In all TPP-dependent enzymes the abstraction of the proton from the C2 atom is the first step in catalysis, which is followed by a nucleophilic attack of this carbanion on the substrate. Subsequent cleavage of a C-C bond releases the first product with formation of a second carbanion (2-greek small letter alpha-carbanion or enamine). The formation of this 2-greek small letter alpha-carbanion is the second feature of TPP catalysis common to all TPP-dependent enzymes. Depending on the enzyme and the substrate(s), the reaction intermediates and products differ. Methyl-branched fatty acids, as phytanic acid, undergo peroxisomal beta-oxidation in which they are shortened by 1 carbon atom. This process includes four steps: activation, 2-hydroxylation, thiamine pyrophosphate dependent cleavage and aldehyde dehydrogenation. In the third step, 2-hydroxy-3-methylacyl-CoA is cleaved in the peroxisomal matrix by 2-hydroxyphytanoyl-CoA lyase (2-HPCL), which uses thiamine pyrophosphate (TPP) as cofactor. The thiamine pyrophosphate dependence of the third step is unique in peroxisomal mammalian enzymology. Human pathology due to a deficient alpha-oxidation is mostly linked to mutations in the gene coding for the second enzyme of the sequence, phytanoyl-CoA hydroxylase (EC 1.14.11.18). (PMID: 12694175, 11899071, 9924800).154-87-0C00068113295322-(alpha-lactyl)-thpp1100CC1=C(CCOP(O)(=O)OP(O)(O)=O)SC=[N+]1CC1=CN=C(C)N=C1NC12H19N4O7P2SInChI=1S/C12H18N4O7P2S/c1-8-11(3-4-22-25(20,21)23-24(17,18)19)26-7-16(8)6-10-5-14-9(2)15-12(10)13/h5,7H,3-4,6H2,1-2H3,(H4-,13,14,15,17,18,19,20,21)/p+1AYEKOFBPNLCAJY-UHFFFAOYSA-O3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-{[hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium425.314425.044967696-3.484thiamin pyrophosphate1-1FDB022584Tpp;Thpp;Thaimine pyrophosphate;Thiamin diphosphate;Thiamin pyrophosphate;Thiamin-ppi;Thiamine diphosphate;Thiamine pyrophosphate;Thiamine-ppi;Thiamine-pyrophosphate;Thiamin diphosphoric acid;Thiamine(1+) diphosphoric acid;Thiamin pyrophosphoric acid;Thiamine diphosphoric acidPW_C001060ThiamPP205410753119781271517362536610360281556080161638816473178746322212806225771241337828511278423334790181117917513280010368119956406120802407120902122120982408121537124122746120123388119123473135123547374124095118125346479125922482126094481126802299126889501127381502127549206128400388964FADHMDB0001248FAD, 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).146-14-5C0001664397516238FAD559059DB03147CC1=CC2=C(C=C1C)N(C[C@H](O)[C@H](O)[C@H](O)COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=NC3=C1N=CN=C3N)C1=NC(=O)NC(=O)C1=N2C27H33N9O15P2InChI=1S/C27H33N9O15P2/c1-10-3-12-13(4-11(10)2)35(24-18(32-12)25(42)34-27(43)33-24)5-14(37)19(39)15(38)6-48-52(44,45)51-53(46,47)49-7-16-20(40)21(41)26(50-16)36-9-31-17-22(28)29-8-30-23(17)36/h3-4,8-9,14-16,19-21,26,37-41H,5-7H2,1-2H3,(H,44,45)(H,46,47)(H2,28,29,30)(H,34,42,43)/t14-,15+,16+,19-,20+,21+,26+/m0/s1VWWQXMAJTJZDQX-UYBVJOGSSA-N{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}[({[(2R,3S,4S)-5-{7,8-dimethyl-2,4-dioxo-2H,3H,4H,10H-benzo[g]pteridin-10-yl}-2,3,4-trihydroxypentyl]oxy}(hydroxy)phosphoryl)oxy]phosphinic acid785.5497785.157134455-2.279flavine-adenine dinucleotide0-3FDB0225111h-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;AdeflavinPW_C000964FAD9991145186819232164253176282882518840211881414894216122916224921335825362237232646023646883147411347581048816526810352851025335111549612655111275613118603015560541566082161611616263901647517864991796666107703916371752057321213746522274872239076224118182161188721511899211122962251232824912443151125192271259522612710291127202921302930113041302436233187708029377126133771521347750111377507112775181157754133477615132777263377805432978375345789303317922233679272358800123688003436980714119119958406119999384120051408120107407120432405120453122120490124121278429121298418121417382121489383122748120122776121122802374122823443123066376123087135123166448123849464123868454123976399124047398125348479125378480125429482125474481125697297125979489126107299126277484126891501126920391126968502126987207127011206127310209127432506127602388127840389140790185140799186463Hydrogen carbonateHMDB0000595Bicarbonate, 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).71-52-3C0028876917544HCO3749OC(O)=OCH2O3InChI=1S/CH2O3/c2-1(3)4/h(H2,2,3,4)BVKZGUZCCUSVTD-UHFFFAOYSA-Ncarbonic acid62.024862.000393930.572carbonic acid0-1FDB022134Bicarbonate;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 ionPW_C000463HCO32241687823933239722613153145705391103544512055711336049155611016164941787482222909222477959112786301327876211180029368119993406121209407121436122121557124123779119123994135124115118125372479126059297126360299126541481126914501127511205127922388128114206414Adenosine triphosphateHMDB0000538Adenosine 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).56-65-5C00002595715422ATP5742DB00171NC1=NC=NC2=C1N=CN2[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1OC10H16N5O13P3InChI=1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1ZKHQWZAMYRWXGA-KQYNXXCUSA-N({[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)phosphonic acid507.181506.995745159-2.057adenosine triphosphate0-3FDB0218135'-(tetrahydrogen triphosphate) adenosine;5'-atp;Atp;Adenosine 5'-triphosphate;Adenosine 5'-triphosphorate;Adenosine 5'-triphosphoric acid;Adenosine triphosphate;Adenylpyrophosphorate;Adenylpyrophosphoric acid;Adephos;Adetol;Adynol;Atipi;Atriphos;Cardenosine;Fosfobion;Glucobasin;Myotriphos;Phosphobion;Striadyne;Triadenyl;Triphosphaden;Triphosphoric acid adenosine ester;Adenosine-5'-triphosphate;H4atp;Adenosine triphosphoric acid;Adenosine-5'-triphosphoric acidPW_C000414ATP922146082661641422478137333279959343997632105182112102146492156142160582405592434272726462812293029663163723616613617514399234474314768914864545032895035265155752059752151005250104529110153131115346112539010354061175430118544312055421295556132556913356031355621108584614358541465876107589714759241516048155610916162301666493178683918868701606976199715720571842067209210722521372292117298198730221673902177408218743216374812227499190818622511847277119031701201028112039164121782851257822612691290132642231532730842326315426213224269431877028253772181347723332977468333776323367803733278041350781681287821435178240353784113357849411578850130788653317891933480028368800461848067411985629194826124113234941132823881162801091199141221199924061201544071202453821203624121212464291213921231213974331214714081219744101220651251220793831220834051224024221224444351229193991230094461238164641239514471239564681240293741245274441246161361246303981246343761249434721249723751250114701253042971253714791253922991255154811255954841261234851262203001262344951262404781265474911265964991269135011271233891277315161277813951277963901278012091281195081281675171407708911560S-Methylmalonyl-CoAHMDB0002310S-Methylmalonyl-CoA belongs to the class of organic compounds known as acyl coas. These are organic compounds containing a coenzyme A substructure linked to an acyl chain. S-Methylmalonyl-CoA is slightly soluble (in water) and an extremely strong acidic compound (based on its pKa). S-Methylmalonyl-CoA has been primarily detected in urine. Within the cell, S-methylmalonyl-CoA is primarily located in the cytoplasm, mitochondria and peroxisome. In humans, S-methylmalonyl-CoA is involved in the threonine and 2-oxobutanoate degradation pathway, the propanoate metabolism pathway, and the valine, leucine and isoleucine degradation pathway. S-Methylmalonyl-CoA is also involved in several metabolic disorders, some of which include the isovaleric aciduria pathway, the maple syrup urine disease pathway, isobutyryl-CoA dehydrogenase deficiency, and the 3-methylglutaconic aciduria type III pathway. Methylmalonyl-CoA is an intermediate in the metabolism of Propanoate. It is a substrate for Malonyl-CoA decarboxylase (mitochondrial), Methylmalonyl-CoA mutase (mitochondrial) and Methylmalonyl-CoA epimerase (mitochondrial).73173-91-8C0068321252287D-METHYL-MALONYL-COA13628334C[C@@H](C(O)=O)C(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP(O)(=O)OP(O)(=O)OCC1OC([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C(N)N=CN=C12C25H40N7O19P3SInChI=1S/C25H40N7O19P3S/c1-12(23(37)38)24(39)55-7-6-27-14(33)4-5-28-21(36)18(35)25(2,3)9-48-54(45,46)51-53(43,44)47-8-13-17(50-52(40,41)42)16(34)22(49-13)32-11-31-15-19(26)29-10-30-20(15)32/h10-13,16-18,22,34-35H,4-9H2,1-3H3,(H,27,33)(H,28,36)(H,37,38)(H,43,44)(H,45,46)(H2,26,29,30)(H2,40,41,42)/t12-,13?,16+,17+,18-,22?/m0/s1MZFOKIKEPGUZEN-JDVCRUKVSA-N(2S)-3-[(2-{3-[(2R)-3-[({[({[(3S,4R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)methyl]-2-hydroxy-3-methylbutanamido]propanamido}ethyl)sulfanyl]-2-methyl-3-oxopropanoic acid867.607867.131252359-2.3910(2S)-3-[(2-{3-[(2R)-3-{[({[(3S,4R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methoxy(hydroxy)phosphoryl}oxy(hydroxy)phosphoryl)oxy]methyl}-2-hydroxy-3-methylbutanamido]propanamido}ethyl)sulfanyl]-2-methyl-3-oxopropanoic acid0-5FDB022959(s)-methylmalonyl-coa;(s)-methylmalonyl-coenzyme aPW_C001560S-MmCoA228642695378623133790321121215784071222514061241351191248041201264144791267304811279795011283222061034Adenosine diphosphateHMDB0001341Adenosine 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.58-64-0C00008602216761ADP5800NC1=NC=NC2=C1N=CN2[C@@H]1O[C@H](COP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1OC10H15N5O10P2InChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1XTWYTFMLZFPYCI-KQYNXXCUSA-N[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy]phosphonic acid427.2011427.029414749-2.126adenosine-diphosphate0-2FDB021817Adp;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 acidPW_C001034ADP2341348415224821380159631597831061141518219014921041821131021615824085924352727284727364628552931657236356144002344763147709150362651577520897521710053151115349112539210354461205544129557213356241085741117576410158491435856146587810758991475926151605015561111616231166649517867009468411886872160715920571872067208210722621372312117300198730321673912177410218743316374832228187225118512771190517012013281121802851326222315329308423283154239831342622322426963187702925377087132772161347730632977472333776633367803933278043350781701287821535178244353784143357849511578705331788491307892033480030368806221188065113580676119948271241132833881162041091199441221199944061201564071203183821203664121212484291213941231213994331214724081218993831219764101220641251220854051224054221224454351229733991230134461238184641239534471239584681240303741244523981245294441246151361246363761249474721249753751250124701253342971253734791254922991255174811256454841261254851262193001262354951262424781265504911265974991269155011277335161277803951277973901278032091281225081281685171283133891051HydrogenHMDB0001362Hydrogen is a colorless, odorless, nonmetallic, tasteless, highly flammable diatomic gas with the molecular formula H2. With an atomic weight of 1.00794, hydrogen is the lightest element. Besides the common H1 isotope, hydrogen exists as the stable isotope Deuterium and the unstable, radioactive isotope Tritium. Hydrogen is the most abundant of the chemical elements, constituting roughly 75% of the universe's elemental mass. Hydrogen can form compounds with most elements and is present in water and most organic compounds. It plays a particularly important role in acid-base chemistry, in which many reactions involve the exchange of protons between soluble molecules. Oxidation of hydrogen, in the sense of removing its electron, formally gives H+, containing no electrons and a nucleus which is usually composed of one proton. That is why H+ is often called a proton. This species is central to discussion of acids. Under the Bronsted-Lowry theory, acids are proton donors, while bases are proton acceptors. A bare proton H+ cannot exist in solution because of its strong tendency to attach itself to atoms or molecules with electrons. However, the term 'proton' is used loosely to refer to positively charged or cationic hydrogen, denoted H+. H2 is a product of some types of anaerobic metabolism and is produced by several microorganisms, usually via reactions catalyzed by iron- or nickel-containing enzymes called hydrogenases. These enzymes catalyze the reversible redox reaction between H2 and its component two protons and two electrons. Creation of hydrogen gas occurs in the transfer of reducing equivalents produced during pyruvate fermentation to water.1333-74-0C002825883867318276ALPHA-GLUCOSE-16-BISPHOSPHATE762[H][H]H2InChI=1S/H2/h1HUFHFLCQGNIYNRP-UHFFFAOYSA-Ndihydrogen2.01592.0156500640dihydrogen00FDB016247Dihydrogen;Hydrogen;Hydrogen cation;Hydrogen gas;Hydrogen ion;Hydronium;Proton;E 949;E-949;E949;H2;Molecular hydrogenPW_C001051H21756823882269633146704952107033163704516012774151132702257859411278603132787721111131639412144812212203240712203712412400613512458611912459111812607329712618248112618829912752920512800538812832320620BiotinHMDB0000030Biotin 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).58-85-5C0012017154815956BIOTIN149962DB00121[H][C@]12CS[C@@H](CCCCC(O)=O)[C@@]1([H])NC(=O)N2C10H16N2O3SInChI=1S/C10H16N2O3S/c13-8(14)4-2-1-3-7-9-6(5-16-7)11-10(15)12-9/h6-7,9H,1-5H2,(H,13,14)(H2,11,12,15)/t6-,7-,9-/m0/s1YBJHBAHKTGYVGT-ZKWXMUAHSA-N5-[(3aS,4S,6aR)-2-oxo-hexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoic acid244.311244.088163078-2.3035-[(3aS,4S,6aR)-2-oxo-hexahydrothieno[3,4-d]imidazol-4-yl]pentanoic acid0-1FDB014510(+)-biotin;(+)-cis-hexahydro-2-oxo-1h-thieno[3,4]imidazole-4-valerate;(+)-cis-hexahydro-2-oxo-1h-thieno[3,4]imidazole-4-valeric acid;(3as,4s,6ar)-hexahydro-2-oxo-1h-thieno[3,4-d]imidazole-4-valerate;(3as,4s,6ar)-hexahydro-2-oxo-1h-thieno[3,4-d]imidazole-4-valeric acid;-(+)-biotin;1swk;1swn;1swr;5-(2-oxohexahydro-1h-thieno[3,4-d]imidazol-4-yl)pentanoate;5-(2-oxohexahydro-1h-thieno[3,4-d]imidazol-4-yl)pentanoic acid;Biodermatin;Bioepiderm;Bios ii;Bios h;Biotin;Coenzyme r;D(+)-biotin;D-(+)-biotin;D-biotin;D-biotin factor s;Factor s;Factor s (vitamin);Hexahydro-2-oxo-1h-thieno(3,4-d)imidazole-4-pentanoate;Hexahydro-2-oxo-1h-thieno(3,4-d)imidazole-4-pentanoic acid;Hexahydro-2-oxo-[3as-(3aa,4b,6aa)]-1h-thieno[3,4-d]imidazole-4-pentanoate;Hexahydro-2-oxo-[3as-(3aa,4b,6aa)]-1h-thieno[3,4-d]imidazole-4-pentanoic acid;Hexahydro-2-oxo-[3as-(3alpha,4beta,6alpha)]-1h-thieno[3,4-d]imidazole-4-pentanoate;Hexahydro-2-oxo-[3as-(3alpha,4beta,6alpha)]-1h-thieno[3,4-d]imidazole-4-pentanoic acid;Lutavit h2;Meribin;Rovimix h 2;Vitamin b7;Vitamin h;Vitamin-h;Cis-(+)-tetrahydro-2-oxothieno[3,4]imidazoline-4-valerate;Cis-(+)-tetrahydro-2-oxothieno[3,4]imidazoline-4-valeric acid;Cis-hexahydro-2-oxo-1h-thieno(3,4)imidazole-4-valeric acid;Cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid;Delta-(+)-biotin;Delta-biotin;Delta-biotin factor s;Biotina;Biotine;BiotinumPW_C000020Biotin2641358579151699322702529210152981055393103544912055461115551114557513360511556112161649617869251607484222778311327796011280031368806531351199954061201341221205034091212104071215591241231091371237801191241171181253744791255012971257184831264212991265424811269165011270382051279893881281152061523R-Methylmalonyl-CoAHMDB0002255R-Methylmalonyl-CoA belongs to the class of organic compounds known as acyl coas. These are organic compounds containing a coenzyme A substructure linked to an acyl chain. R-Methylmalonyl-CoA is slightly soluble (in water) and an extremely strong acidic compound (based on its pKa). R-Methylmalonyl-CoA has been primarily detected in urine. Within the cell, R-methylmalonyl-CoA is primarily located in the cytoplasm. In humans, R-methylmalonyl-CoA is involved in the threonine and 2-oxobutanoate degradation pathway, the valine, leucine and isoleucine degradation pathway, and the propanoate metabolism pathway. R-Methylmalonyl-CoA is also involved in several metabolic disorders, some of which include the maple syrup urine disease pathway, the 3-methylglutaconic aciduria type IV pathway, 3-methylcrotonyl CoA carboxylase deficiency type I, and 3-hydroxyisobutyric acid dehydrogenase deficiency. Methylmalonyl-CoA is an intermediate in the metabolism of Propanoate. It is a substrate for Malonyl-CoA decarboxylase (mitochondrial), Methylmalonyl-CoA mutase (mitochondrial) and Methylmalonyl-CoA epimerase (mitochondrial).73173-92-9 C01213 22833590METHYL-MALONYL-COA17216177C[C@H](C(O)=O)C(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP(O)(=O)OP(O)(=O)OCC1OC(C(O)C1OP(O)(O)=O)N1C=NC2=C(N)N=CN=C12C25H40N7O19P3SInChI=1S/C25H40N7O19P3S/c1-12(23(37)38)24(39)55-7-6-27-14(33)4-5-28-21(36)18(35)25(2,3)9-48-54(45,46)51-53(43,44)47-8-13-17(50-52(40,41)42)16(34)22(49-13)32-11-31-15-19(26)29-10-30-20(15)32/h10-13,16-18,22,34-35H,4-9H2,1-3H3,(H,27,33)(H,28,36)(H,37,38)(H,43,44)(H,45,46)(H2,26,29,30)(H2,40,41,42)/t12-,13?,16?,17?,18+,22?/m1/s1MZFOKIKEPGUZEN-YLYUOEEYSA-N(2R)-3-[(2-{3-[(2R)-3-[({[({[5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)methyl]-2-hydroxy-3-methylbutanamido]propanamido}ethyl)sulfanyl]-2-methyl-3-oxopropanoic acid867.607867.131252359-2.3910(2R)-3-[(2-{3-[(2R)-3-{[({[5-(6-aminopurin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methoxy(hydroxy)phosphoryl}oxy(hydroxy)phosphoryl)oxy]methyl}-2-hydroxy-3-methylbutanamido]propanamido}ethyl)sulfanyl]-2-methyl-3-oxopropanoic acid0-5FDB022930PW_C001523R-MmCoA229042697243873786241337903513279204112121580407122252406122578124124138119124805120125150118126415479126733299127980501128326388808Succinyl-CoAHMDB0001022Succinyl-CoA is an important intermediate in the citric acid cycle, where it is synthesized from α-Ketoglutarate by α-ketoglutarate dehydrogenase (EC 1.2.4.2) through decarboxylation, and is converted into succinate through the hydrolytic release of coenzyme A by succinyl-CoA synthetase (EC 6.2.1.5). Succinyl-CoA may be an end product of peroxisomal beta-oxidation of dicarboxylic fatty acids; the identification of an apparently specific succinyl-CoA thioesterase (ACOT4, EC 3.1.2.3, hydrolyzes succinyl-CoA) in peroxisomes strongly suggests that succinyl-CoA is formed in peroxisomes. Acyl-CoA thioesterases (ACOTs) are a family of enzymes that catalyze the hydrolysis of the CoA esters of various lipids to the free acids and coenzyme A, thereby regulating levels of these compounds. (PMID: 16141203).604-98-8C00091439161153803-METHYLBENZYLSUCCINYL-COA388307CC(C)(COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C1N=CN=C2N)C(O)C(=O)NCCC(=O)NCCSC(=O)CCC(O)=OC25H40N7O19P3SInChI=1S/C25H40N7O19P3S/c1-25(2,20(38)23(39)28-6-5-14(33)27-7-8-55-16(36)4-3-15(34)35)10-48-54(45,46)51-53(43,44)47-9-13-19(50-52(40,41)42)18(37)24(49-13)32-12-31-17-21(26)29-11-30-22(17)32/h11-13,18-20,24,37-38H,3-10H2,1-2H3,(H,27,33)(H,28,39)(H,34,35)(H,43,44)(H,45,46)(H2,26,29,30)(H2,40,41,42)/t13-,18-,19-,20?,24-/m1/s1VNOYUJKHFWYWIR-FZEDXVDRSA-N4-{[2-(3-{3-[({[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)methyl]-2-hydroxy-3-methylbutanamido}propanamido)ethyl]sulfanyl}-4-oxobutanoic acid867.607867.131252359-2.19104-({2-[3-(3-{[({[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methoxy(hydroxy)phosphoryl}oxy(hydroxy)phosphoryl)oxy]methyl}-2-hydroxy-3-methylbutanamido)propanamido]ethyl}sulfanyl)-4-oxobutanoic acid0-5FDB022375Coa s-(hydrogen succinate);Coa s-succinate;Coenzyme a s-(hydrogen succinate);Coenzyme a s-succinate;S-(hydrogen butanedioate;S-(hydrogen butanedioate) coa;S-(hydrogen butanedioate) coenzyme a;S-(hydrogen butanedioic acid;S-succinoylcoenzyme a;Suc-co-a;Suc-coa;Succ-coa;Succ-coenzyme a;Succ-s-coa;Succ-s-coenzyme a;Succ-s-coenzyme-a;Succ-coenzyme-a;Succino-1-yl-coenzyme a;Succinyl coa;Succinyl coenzyme a;Succinyl-s-coa;Succinyl-s-coenzyme a;Succinyl-s-coenzyme-a;Succinylcoenzyme-a;Succinylcoenzyme aPW_C000808Suc-CoA233410553366925378103603915560971616485178701516073611637474222771401337810111278576132800213681199784061207694071220141241227631201233651191245681181253584791261642991263064811269015011278682061401AdenosylcobalaminHMDB0002086Adenosylcobalamin is one of two metabolically active forms synthesized upon ingestion of vitamin B12 and is the predominant form in the liver; it acts as a coenzyme in the reaction catalyzed by methylmalonyl-CoA mutase. A cobalamin (cbl) derivative in which the substituent is deoxyadenosyl. It is one of two metabolically active forms synthesized upon ingestion of vitamin B12 and is the predominant form in the liver; it acts as a coenzyme in the reaction catalyzed by methylmalonyl-CoA mutase (MCM; E.C. 5.4.99.2). Inborn errors of vitamin B12 metabolism are autosomal recessive disorders and have been classified into nine distinct complementation classes. Disorders affecting adenosylcobalamin cause methylmalonic acidemia and metabolic acidosis. Methylmalonyl-CoA mutase catalyzes the conversion of L-methylmalonyl-CoA to succinyl-CoA and uses adenosylcobalamin (AdoCbl) as a cofactor. Cbl must be transported into mitochondria, reduced and adenosylated before it can be utilized by MCM. (PMID: 17011224).13870-90-1C0019418408ADENOSYLCOBALAMIN-5-P30791458[C@H]1(C[Co-3]2345[N+]6=C7C(C)=C8N2[C@]([H])([C@H](CC(=O)N)[C@]8(CCC(=O)NC[C@@H](C)OP([O-])(=O)O[C@@H]2[C@@H](CO)O[C@H](N8C=[N+]3C3=CC(C)=C(C)C=C83)[C@@H]2O)C)[C@@]2(C)[C@@](CC(=O)N)([C@H](CCC(=O)N)C(C(C)=C3[N+]4=C(C=C6C([C@@H]7CCC(=O)N)(C)C)[C@@H](CCC(=O)N)[C@@]3(CC(=O)N)C)=[N+]52)C)O[C@@H](N2C3=NC=NC(=C3N=C2)N)[C@H](O)[C@@H]1OC72H100CoN18O17PInChI=1S/C62H90N13O14P.C10H12N5O3.Co/c1-29-20-39-40(21-30(29)2)75(28-70-39)57-52(84)53(41(27-76)87-57)89-90(85,86)88-31(3)26-69-49(83)18-19-59(8)37(22-46(66)80)56-62(11)61(10,25-48(68)82)36(14-17-45(65)79)51(74-62)33(5)55-60(9,24-47(67)81)34(12-15-43(63)77)38(71-55)23-42-58(6,7)35(13-16-44(64)78)50(72-42)32(4)54(59)73-56;1-4-6(16)7(17)10(18-4)15-3-14-5-8(11)12-2-13-9(5)15;/h20-21,23,28,31,34-37,41,52-53,56-57,76,84H,12-19,22,24-27H2,1-11H3,(H15,63,64,65,66,67,68,69,71,72,73,74,77,78,79,80,81,82,83,85,86);2-4,6-7,10,16-17H,1H2,(H2,11,12,13);/q;;+2/p-2/t31-,34-,35-,36-,37+,41-,52-,53-,56-,57+,59-,60+,61+,62+;4-,6-,7-,10-;/m11./s1ZIHHMGTYZOSFRC-OUCXYWSSSA-L(10S,12R,13S,17R,23R,24R,25R,30S,35S,36S,40S,41S,42R,46R)-1-{[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl}-30,35,40-tris(2-carbamoylethyl)-24,36,41-tris(carbamoylmethyl)-46-hydroxy-12-(hydroxymethyl)-5,6,17,23,28,31,31,36,38,41,42-undecamethyl-15,20-dioxo-11,14,16-trioxa-2lambda5,9,19,26,43lambda5,44lambda5,45lambda5-heptaaza-15lambda5-phospha-1-cobaltadodecacyclo[27.14.1.1^{1,34}.1^{2,9}.1^{10,13}.0^{1,26}.0^{3,8}.0^{23,27}.0^{25,42}.0^{32,44}.0^{39,43}.0^{37,45}]heptatetraconta-2(47),3,5,7,27,29(44),32,34(45),37,39(43)-decaene-2,43,44,45-tetrakis(ylium)-1,1,1-triuid-15-olate1579.58181578.6583455712(10S,12R,13S,17R,23R,24R,25R,30S,35S,36S,40S,41S,42R,46R)-1-{[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl}-30,35,40-tris(2-carbamoylethyl)-24,36,41-tris(carbamoylmethyl)-46-hydroxy-12-(hydroxymethyl)-5,6,17,23,28,31,31,36,38,41,42-undecamethyl-15,20-dioxo-11,14,16-trioxa-2lambda5,9,19,26,43lambda5,44lambda5,45lambda5-heptaaza-15lambda5-phospha-1-cobaltadodecacyclo[27.14.1.1^{1,34}.1^{2,9}.1^{10,13}.0^{1,26}.0^{3,8}.0^{23,27}.0^{25,42}.0^{32,44}.0^{39,43}.0^{37,45}]heptatetraconta-2(47),3,5,7,27,29(44),32,34(45),37,39(43)-decaene-2,43,44,45-tetrakis(ylium)-1,1,1-triuid-15-olate00FDB022837(5'-deoxy-5'-adenosyl)cobamide coenzyme;5'-deoxy-5'-adenosyl vitamin b12;5'-deoxy-5'-adenosylcobalamin;Adenosylcobalamin 5'-phosphate;Calomide;Cobalamin coenzyme;Cobamamide;Cobamamide 5'-phosphate;Cobamide coenzyme;Coenzyme b12;Deoxyadenosylcobalamin;Dibencozide;Funacomide;Vitamin b12 coenzyme;Vitamin b12 coenzymes;Adenosylcob(iii)alamin;5,6-dimethylbenzimidazolyl-5-deoxyadenosyl-cobamide;(5,6-dimethylbenzimidazolyl)cobamide coenzyme;Alpha-(5,6-dimethylbenzimidazolyl)cobamide coenzyme;5'-deoxy-5'-adenosyl-5,6-dimethylbenzimidazolylcobamide;5,6-dimethylbenzimidazolyl-co-5'-deoxy-5'-adenosylcobamide;Dmbc coenzyme;A-(5,6-dimethylbenzimidazolyl)cobamide coenzyme;α-(5,6-dimethylbenzimidazolyl)cobamide coenzymePW_C001401Adnscbn2401378628112121582407124140119126419481127985206635L-serine dehydratase/L-threonine deaminaseP20132HMDBP00671SDS12q24.13CH47105414.3.1.17; 4.3.1.194328269122232Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrialP11182The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
HMDBP03078DBT1p31J0320812.3.1.16815974174834359252Dihydrolipoyl dehydrogenase, mitochondrialP09622Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction.
HMDBP00054DLD7q31-q32L1375711.8.1.421741080346708639411369657021421265414252510201425961202932-oxoisovalerate dehydrogenase subunit beta, mitochondrialP21953
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
HMDBP00299BCKDHB6q14.1X5244611.2.4.41589417382269332942-oxoisovalerate dehydrogenase subunit alpha, mitochondrialP12694The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
HMDBP00300BCKDHA19q13.1-q13.2Z1409311.2.4.4158841737226943253Propionyl-CoA carboxylase alpha chain, mitochondrialP05165HMDBP00259PCCA13q32AY03579516.4.1.3170032287446142252Propionyl-CoA carboxylase beta chain, mitochondrialP05166HMDBP00258PCCB3q21-q22M3116716.4.1.317013461521428474250Methylmalonyl-CoA epimerase, mitochondrialQ96PE7HMDBP00256MCEE2p13.3AF36454715.1.99.1171432291426982251Methylmalonyl-CoA mutase, mitochondrialP22033Involved in the degradation of several amino acids, odd-chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle. MCM has different functions in other species.
HMDBP00257MUT6p12.3M3750015.4.99.21715424023109L-serine dehydratase/L-threonine deaminase1PW_P000109124635254114814318683branched-chain alpha-keto dehydrogenase complex1PW_P000683767223217685217692931770294130710601308964130910601684Propionyl-CoA carboxylase1PW_P00068477125317722521310201465Methylmalonyl-CoA epimerase, mitochondrial1PW_P000465488250468Methylmalonyl-CoA mutase, mitochondrial1PW_P0004684912512286140111482falsePW_R001482Right56211091Compoundfalse562231Compoundfalse5623351Compoundtrue12031091483falsePW_R001483Right562431Compoundfalse562510991Compoundtrue56267211Compoundtrue56279881Compoundfalse562811441Compoundtrue12046832.3.1.1681484falsePW_R001484Right56299881Compoundfalse56304631Compoundtrue56314141Compoundtrue563215601Compoundfalse563310341Compoundtrue563410511Compoundtrue12056846.4.1.31263falsePW_R001263Right482915601Compoundfalse483015231Compoundfalse9764655.1.99.11486falsePW_R001486Right563715231Compoundfalse56388081Compoundfalse12074685.4.99.2117PW_T0001171351091Compound152Right118PW_T00011813631Compound23Right52511091581false47510510regular2001905252109281false47549510regular20019052633281false47389510regular200190526435263false39483110regular78785265114829false52571220regular1003552663381false96890510regular20019052711099385false1178108010regular50305272721359false114884010regular50305273988381false154890510regular20019052741144360false146884510regular50305275106039false1298103510regular10035527696439false135393510regular100255277106039false122893510regular100355282463347false1748108510regular78785283414342false1528111510regular503052841560381false1551146010regular20019052851034343false1531138010regular503052861051355false1747136110regular787852872039false1593120210regular1002552881523281false1551190010regular2001905289808381false996190010regular2001905290140139false1336194510regular10025216563522false5007378subunitregular150702171223232true12589708noneregular150702172523113true12438908noneregular1608021732933167true12439358noneregular1408521742943136false12639208proteinregular17515521802533136false158311878noneregular17515521812523136false155811878proteinregular175155218225022false157617408subunitregular15070218325132false131619608subunitregular15070194510911122158216588852657996Cofactor194868311132164217121652172216621732167217488952758008Cofactor89052768009Cofactor89152778010Cofactor19516841113217321802174218189252878021Cofactor1952465111221752182195346811132176218389352908026Cofactor7981M575 295 C575 325 126 118 150 135 5true187982M575 495 C575 465 577 412 575 295 83false18trueM 467.5 552.0096189432334 L 475 565 L 482.5 552.0096189432334false7993M575 685 C575 715 575 707 575 737 5false187994M573 895 C573 865 575 837 575 807 5false18trueM 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345false7995M472 870 C520 870 571 851 575 807 5false18trueM 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345false7996M250 110 L250 160 L300 110 z10true187997M673 990 C703 990 674 953 698 970 5true187998M968 1000 C938 1000 819 989 673 990 83false18trueM 885.0096189432334 1017.5 L 898 1010 L 885.0096189432334 1002.5false8003M1168 1000 C1198 1000 1238 1000 1268 1000 5false188004M1203 1080 C1206 1017 1225 999 1268 1000 5false188005M1173 870 C1173 902 1189 1000 1268 1000 5false188006M1548 1000 C1518 1000 1468 1000 1438 1000 5false18trueM 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345false8007M1493 875 C1497 919 1468 1000 1438 1000 5false18trueM 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345false8008M1323 975 L1323 1025 L1373 975 z10true188009M1323 975 L1323 1025 L1373 975 z10true188010M1323 975 L1323 1025 L1373 975 z10true188015M1648 1095 C1648 1125 1648 1164 1648 1194 5false188016M1748 1124 C1708 1121 1656 1139 1648 1194 5false188017M1578 1130 C1648 1134 1648 1164 1648 1194 5false188018M1651 1460 C1651 1430 1648 1372 1648 1342 5false18trueM 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345false8019M1581 1395 C1614 1395 1648 1372 1648 1342 5false18trueM 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345false8020M1747 1400 C1688 1401 1648 1372 1648 1342 5false18trueM 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345false8021M1558 1202.5 L1558 1252.5 L1608 1202.5 z10true188022M1651 1650 C1651 1680 1651 1710 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