27PathwayCysteine MetabolismThe semi-essential amino aid cysteine is tightly regulated in the body to ensure proper levels for metabolism but maintaining levels below toxic thresholds. Cysteine can be obtained from diet or synthesized from O-acetyl-L-serine. Cystine is the dimeric form of cysteine. Cysteine is a precursor for protein synthesis and an antioxidant. Impaired cysteine metabolism has been linked with neurodegenerative disorders. MetabolicPW000018CenterPathwayVisualizationContext1819502850#000099PathwayVisualization2527Cysteine MetabolismThe semi-essential amino aid cysteine is tightly regulated in the body to ensure proper levels for metabolism but maintaining levels below toxic thresholds. Cysteine can be obtained from diet or synthesized from O-acetyl-L-serine. Cystine is the dimeric form of cysteine. Cysteine is a precursor for protein synthesis and an antioxidant. Impaired cysteine metabolism has been linked with neurodegenerative disorders. Metabolic18287SubPathway134995Compound88297SubPathway1350826Compound8834102SubPathway1355448Compound883562SubPathway1356448Compound883698SubPathway1357448Compound883768SubPathway1358789Compound883870SubPathway1359789Compound883984SubPathway1360164Compound843Lehninger, A.L. Lehninger principles of biochemistry (4th ed.) (2005). New York: W.H Freeman.27Pathway44Salway, J.G. Metabolism at a glance (3rd ed.) (2004). Alden, Mass.: Blackwell Pub.27Pathway27962016702335Stipanuk MH, Dominy JE Jr, Lee JI, Coloso RM: Mammalian cysteine metabolism: new insights into regulation of cysteine metabolism. J Nutr. 2006 Jun;136(6 Suppl):1652S-1659S. doi: 10.1093/jn/136.6.1652S.27Pathway27962129530337 Paul BD, Sbodio JI, Snyder SH: Cysteine Metabolism in Neuronal Redox Homeostasis. Trends Pharmacol Sci. 2018 May;39(5):513-524. doi: 10.1016/j.tips.2018.02.007. Epub 2018 Mar 9.27Pathway1CellCL:00000002Platelet CL:00002335HepatocyteCL:00001823NeuronCL:00005404CardiomyocyteCL:00007468Beta cellCL:00006397Epithelial CellCL:00000666MyocyteCL:000018712AstrocyteCL:000012723T CellCL:00000841Homo sapiens9606EukaryoteHuman2Bacteria2ProkaryoteBacteria3Escherichia coli562Prokaryote12Mus musculus10090EukaryoteMouse17Rattus norvegicus10116EukaryoteRat19Schizosaccharomyces pombe4896Eukaryote24Solanum lycopersicum4081EukaryoteTomato4Arabidopsis thaliana3702EukaryoteThale cress18Saccharomyces cerevisiae4932EukaryoteYeast21Xenopus laevis8355EukaryoteAfrican clawed frog6Caenorhabditis elegans6239EukaryoteRoundworm25Escherichia coli (strain K12)83333Prokaryote49Bathymodiolus platifrons220390EukaryoteDeep sea mussel23Pseudomonas aeruginosa287Prokaryote60Nitzschia sp.0001EukaryoteNitzschia45Bos taurus9913EukaryoteCattle10Drosophila melanogaster7227EukaryoteFruit fly51Picea sitchensis3332EukaryoteSitka spruce1CytosolGO:00058293Mitochondrial MatrixGO:00057595CytoplasmGO:000573714Mitochondrial Outer MembraneGO:00057412MitochondrionGO:000573915NucleusGO:00056344PeroxisomeGO:000577713Endoplasmic ReticulumGO:00057837Endoplasmic Reticulum MembraneGO:000578910Cell MembraneGO:000588627Peroxisome MembraneGO:000577831Periplasmic SpaceGO:000562011Extracellular SpaceGO:000561535ChloroplastGO:000950712Mitochondrial Inner MembraneGO:000574332Inner MembraneGO:00702586LysosomeGO:000576424Mitochondrial Intermembrane SpaceGO:000575819Sarcoplasmic ReticulumGO:001652925Golgi ApparatusGO:000579416Lysosomal LumenGO:004320218Melanosome MembraneGO:003316236MembraneGO:001602020Endoplasmic Reticulum LumenGO:000578821SynapseGO:004520253Endoplasmic Reticulum BodyGO:001016834Plant-Type VacuoleGO:000032540PeriplasmGO:004259730Lysosomal MembraneGO:00057652Endothelium BTO:00003931LiverBTO:00007597297Nervous SystemBTO:000148418PancreasBTO:000098825IntestineBTO:00006488Blood VesselBTO:000110274119MuscleBTO:00008871411824BrainBTO:000014289164Adrenal MedullaBTO:00000497183Sympathetic Nervous 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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-N507.181506.995745159FDB0218135'-(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_C000414ATP9221460826616414224781373332799593439976321051821121021464921561421605824055924342727264628122930296631637236166136175143992344743147689148645450328950352651557520597521510052501045291101531311153461125390103540611754301185443120554212955561325569133560313556211085846143585414658761075897147592415160481556109161623016664931786839188687016069761997157205718420672092107225213722921172981987302216739021774082187432163748122274991908186225118472771190317012010281120391641217828512578226126912901326422315327308423263154262132242694318770282537721813477233329774683337763233678037332780413507816812878214351782403537841133578494115788501307886533178919334800283688004618480674119856291948261241132349411328238811628010911991412211999240612015440712024538212036241212124642912139212312139743312147140812197441012206512512207938312208340512240242212244443512291939912300944612381646412395144712395646812402937412452744412461613612463039812463437612494347212497237512501147012530429712537147912539229912551548112559548412612348512622030012623449512624047812654749112659649912691350112712338912773151612778139512779639012780120912811950812816751714077089195L-Glutamic acidHMDB0000148Glutamic 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).56-86-0C000253303216015GLT30572DB00142N[C@@H](CCC(O)=O)C(O)=OC5H9NO4InChI=1S/C5H9NO4/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H,7,8)(H,9,10)/t3-/m0/s1WHUUTDBJXJRKMK-VKHMYHEASA-N147.1293147.053157781FDB012535(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-glutaminsaeurePW_C000095Glu16244365811911384164149699110542144850145626146254532311153441135415117543911855651325631107563210858591056006147607115761919465318568381876844188709272709371716520571822077514224751815182082258373220117921981185516112004222126213112683289126972904234831542349318428453207702025377332133775251127797134677977327779813477829134580649135120023124120040122120086407120347406120692126120816418121147423121153424121157425122833119122997120123299443123401454123719458123725459123729460125401299125418297125457481125667479125769301125802489126941388126995206127162501127257506140738841407395971034Adenosine 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-N427.2011427.029414749FDB021817Adp;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_C001034ADP2341348415224821380159631597831061141518219014921041821131021615824085924352727284727364628552931657236356144002344763147709150362651577520897521710053151115349112539210354461205544129557213356241085741117576410158491435856146587810758991475926151605015561111616231166649517867009468411886872160715920571872067208210722621372312117300198730321673912177410218743316374832228187225118512771190517012013281121802851326222315329308423283154239831342622322426963187702925377087132772161347730632977472333776633367803933278043350781701287821535178244353784143357849511578705331788491307892033480030368806221188065113580676119948271241132833881162041091199441221199944061201564071203183821203664121212484291213941231213994331214724081218993831219764101220641251220854051224054221224454351229733991230134461238184641239534471239584681240303741244523981245294441246151361246363761249474721249753751250124701253342971253734791254922991255174811256454841261254851262193001262354951262424781265504911265974991269155011277335161277803951277973901278032091281225081281685171283133891441Phosphoric acidHMDB0002142Phosphoric 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.7664-38-2C00009100426078979OP(O)(O)=OH3O4PInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)NBIIXXVUZAFLBC-UHFFFAOYSA-N97.995297.976895096FDB013380Acide phosphorique (french);Acido fosforico [italian];Acidum phosphoricum;Diphosphate tetrasodium;Fosforzuuroplossingen [dutch];Marphos;Nfb;Ortho- phosphoric acid;Orthophosphoric acid;Phosphoric acid (acd/name 4.0);Phosphorsaeure;Phosphorsaeureloesungen [german];Sodium pyrophosphate;Sodium pyrophosphate decahydrate;Sodium pyrophosphate decahydrate biochemica;Sonac;Tetra-sodium pyrophosphate;Tetrasodium pyrophosphate decahydrate;Tetrasodium pyrophosphate 10-hydrate;White phosphoric acid;[po(oh)3];Acide phosphorique;H3po4;Phosphate;Phosphorsaeureloesungen;OrthophosphatePW_C001441PhosfrA171844044831315924316782190249191054856359131475943151689116011782198118282131182921611852277126383177105132773301337747333377779111780001127827235678706331787073348067113580677119119918122120126124120157407120344406120367412121383419121900383121902408122858118122994120123014446123942455124453398124455374125308297125493299125518481125664479126056490126855205127030388127053206127159501127508507826γ-GlutamylcysteineHMDB0001049gamma-Glutamylcysteine is a dipeptide composed of gamma-glutamate and cysteine, and is a proteolytic breakdown product of larger proteins. It belongs to the family of N-acyl-alpha Amino Acids and Derivatives. These are compounds containing an alpha amino acid which bears an acyl group at its terminal nitrogen atom. gamma-Glutamylcysteine is an incomplete breakdown product of protein digestion or protein catabolism. Some dipeptides are known to have physiological or cell-signaling effects although most are simply short-lived intermediates on their way to specific amino acid degradation pathways following further proteolysis. gamma-Glutamylcysteine is a product of enzyme glutamate-cysteine ligase [EC 6.3.2.2] and a substrate of enzyme glutathione synthase [EC 6.3.2.3] in the glutamate metabolism pathway (KEGG).636-58-8C0066912393817515L-GAMMA-GLUTAMYLCYSTEINE110467DB03408N[C@@H](CCC(=O)N[C@@H](CS)C(O)=O)C(O)=OC8H14N2O5SInChI=1S/C8H14N2O5S/c9-4(7(12)13)1-2-6(11)10-5(3-16)8(14)15/h4-5,16H,1-3,9H2,(H,10,11)(H,12,13)(H,14,15)/t4-,5-/m0/s1RITKHVBHSGLULN-WHFBIAKZSA-N250.272250.062342258FDB003603(des-gly)-Glutathione;3gc;5-L-Glutamyl-L-cysteine;5-L-Glutamylcysteine;H-Glu(Cys-OH)-OH;H-gamma-Glu-Cys-OH;L-g-Glutamyl-L-cysteine;L-gamma-Glutamyl-L-cysteine;L-gamma-Glutamylcysteine;N-(1-Carboxy-2-mercaptoethyl)-L-glutamine;N-L-gamma-Glutamyl-L-cysteine;Xn-L-g-glutamyl-glutamine;Xn-L-gamma-glutamyl-glutamine;g-Glutamylcysteine;g-L-Glutamyl-L-cysteine;gamma-Glu-Cys;gamma-Glutamylcysteine;gamma-L-Glutamyl-L-cysteine;Gammaglucys;Glu(-Cys);L-γ-Glutamyl-L-cysteine;G-Glu-Cys;γ-Glu-Cys;γ-Glutamylcysteine;γ-L-Glutamyl-L-cysteine;L-g-Glutamylcysteine;L-γ-Glutamylcysteine;γ-L-Glu-L-Cys;N-γ-Glutamylcysteine;N-L-γ-Glutamyl-cysteine;N-L-γ-Glutamyl-L-cysteine;gamma-L-Glu-L-Cys;N-L-gamma-Glutamyl-cysteine;N-γ-L-Glutamyl-L-cysteinePW_C000826γGluCys17584662277780111807051351200961221254652971270022051065OxygenHMDB0001377Oxygen 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).7782-44-7C0000797715379CPD-6641952O=OO2InChI=1S/O2/c1-2MYMOFIZGZYHOMD-UHFFFAOYSA-N31.998831.989829244FDB022589Dioxygen;Molecular oxygen;O2;Oxygen;Oxygen molecule;[oo];Dioxygene;Disauerstoff;E 948;E-948;E948PW_C001065O2959110524516500185058549146252863836491067431688207541576347693383621375492016242531222803294260424747135467123548012554931265508127580910859731476129159700618870321637050160731921375332107560212839515111816216118641981188321511894211120572251206316412247286122792261232524912706291127162921300429813016300130263011303830213260223422761742657315769102937704429477214134773501117736313077377331773953327749711377512115775373347762633677723337777361127774712977756341778051147781213378070329781511327838134578805343791113601200474081203831221204264051205424071205534141205944091206014061208834151210451241211043831216054341216564291221173821225734181226893841227983741228224431230271351230603761231284471231391361231634481231761191231874501232191371232261201234594511236091181236693981241634691242144641246693991251454541252751211254254821257064781257314831257372971257404791258844811261002991262724841265224951267214891268254801269645021269862071271982091272142081272192051272225011273055041273452061275573881275745151278353891280813951280953901283125061284323917893-SulfinoalanineHMDB00009963-Sulfinoalanine or cysteinesulfinic acid is a N-methyl-D-aspartate agonist. It is a product of cysteine dioxygenase or CDO [EC 1.13.11.20]. In humans cysteine catabolism is tightly regulated via regulation of cysteine dioxygenase (CDO) levels in the liver, with the turnover of CDO protein being dramatically decreased when intracellular cysteine levels increase. This occurs in response to changes in the intracellular cysteine concentration via changes in the rate of CDO ubiquitination and degradation. Expressed at high levels in the liver with lower levels in the kidney, brain, and lung, cysteine dioxygenase catalyzes the addition of molecular oxygen to the sulfhydryl group of cysteine, yielding cysteinesulfinic acid. The oxidative catabolism of cysteine to cysteinesulfinate by CDO represents an irreversible loss of cysteine from the free amino acid pool. Once generated, cysteinesulfinate is shuttled into several pathways including hypotaurine/taurine synthesis, sulfite/sulfate production, and the generation of pyruvate.1115-65-7C00606439270417213-SULFINOALANINE16743745N[C@@H](CS(O)=O)C(O)=OC3H7NO4SInChI=1S/C3H7NO4S/c4-2(3(5)6)1-9(7)8/h2H,1,4H2,(H,5,6)(H,7,8)/t2-/m0/s1ADVPTQAUNPRNPO-REOHCLBHSA-N153.157153.009578407FDB0223583-sulfino- alanine;3-sulfino-l-alanine;3-sulphino-l-alanine;Alanine 3-sulfinic acid;Cysteine hydrogen sulfite ester;Cysteine sulfinate;Cysteine sulfinic acid;L-cysteine sulfinic acid;L-cysteinesulfinic acid;2-amino-3-sulfino-propionic acid;Cysteine-s,s-dioxide;Cysteine-s-dioxide;L-cysteine-s,s-dioxide;2-amino-3-sulfino-propionate;2-amino-3-sulphino-propionate;2-amino-3-sulphino-propionic acidPW_C0007893S-Ala708877781111120560122123194135544Fe2+HMDB0000692Iron is a chemical element with the symbol Fe and atomic number 26. Iron makes up 5% of the Earth's crust and is second in abundance to aluminium among the metals and fourth in abundance among the elements. Physiologically, it. exists as an ion in the body. Iron (as Fe2+, ferrous ion) is a necessary trace element used by all known living organisms. Iron-containing enzymes, usually containing heme prosthetic groups, participate in catalysis of oxidation reactions in biology, and in transport of a number of soluble gases. Iron is an essential constituent of hemoglobin, cytochrome, and other components of respiratory enzyme systems. Its chief functions are in the transport of oxygen to tissue (hemoglobin) and in cellular oxidation mechanisms. Inorganic iron involved in redox reactions is also found in the iron-sulfur clusters of many enzymes, such as nitrogenase (involved in the synthesis of ammonia from nitrogen and hydrogen) and hydrogenase. A class of non-heme iron proteins is responsible for a wide range of functions such as ribonucleotide reductase (reduces ribose to deoxyribose; DNA biosynthesis) and purple acid phosphatase (hydrolysis of phosphate esters). When the body is fighting a bacterial infection, the body sequesters iron inside of cells (mostly stored in the storage molecule ferritin) so that it cannot be used by bacteria. Depletion of iron stores may result in iron-deficiency anemia. Iron is used to build up the blood in anemia. Humans experience iron toxicity above 20 milligrams of iron for every kilogram of weight, and 60 milligrams per kilogram is a lethal dose. Over-consumption of iron, often the result of children eating large quantities of ferrous sulfate tablets intended for adult consumption, is the most common toxicological cause of death in children under six. The DRI lists the Tolerable Upper Intake Level (UL) for adults as 45 mg/day. For children under fourteen years old the UL is 40 mg/day. Iron is a metal extracted from iron ore, and is almost never found in the free elemental state.15438-31-0C148182728429033Ferric-Hydroxamate-Complexes25394DB01592[Fe++]FeInChI=1S/Fe/q+2CWYNVVGOOAEACU-UHFFFAOYSA-N55.84555.934942133FDB016251Armco iron;Carbonyl iron;Fe;Ferrovac e;Hematite;Infed;Loha;Limonite;Magnetite;Malleable iron;Metopirone;Metyrapone;Pzho;Pzh2m;Remko;Suy-b 2;Taconite;Venofer;Wrought iron;Fe (ii) ion;Fe(ii);Fe2+;Fe(2+);Ferrous ion;Iron ion(2+)PW_C000544Fe2+398196413678316922070981777270411637052160120602251214315177179132777401127775112977760341777821111205444071205574141205701221217651241231781191231914501232041351243161181261432991261854811276503881407104914071618134Oxoglutaric acidHMDB0000208Oxoglutaric 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).328-50-7C0002651309152-KETOGLUTARATE50DB02926OC(=O)CCC(=O)C(O)=OC5H6O5InChI=1S/C5H6O5/c6-3(5(9)10)1-2-4(7)8/h1-2H2,(H,7,8)(H,9,10)KPGXRSRHYNQIFN-UHFFFAOYSA-N146.0981146.021523302FDB0033612-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 acidPW_C000134AKG152423141414684991867331110842126351447501455261467545375103541411754381185564132600814760361556069157609216164821786530857471222751522475191518209225837422011863198126812897705425377135133774811117752311277746129779673457797034677976327779843477842533480018368806941351131629411997240612002212412008440712017412212055241412081441812098940812114642312115242412116042512275712012283111912318645012339945412355437412371845812372445912373246012535747912540029912545548112553329712580048912592948212690050112694038812699320612706620512725550612738850210853-Sulfinylpyruvic acidHMDB0001405This compound is found in the mammalian cysteine metobolic pathway. It is the deaminated form of Cysteine sulfinic acid (PMID: 3925121), which subsequently spontaneously reacts to form pyruvate while releasing sulfur dioxide. It is the byproduct of oxidoreductases (EC 1.4.1.-), and aspartate transaminase (EC 2.6.1.1). It is also often associated with hepatic disease, and the presence of aspartate transaminase is used in diagnostic biochemical assays of such ailments. (PMID: 17310554).C05527575176673-SULFINYL-PYRUVATE4911362OC(=O)C(=O)CS(O)=OC3H4O5SInChI=1S/C3H4O5S/c4-2(3(5)6)1-9(7)8/h1H2,(H,5,6)(H,7,8)JXYLQEMXCAAMOL-UHFFFAOYSA-N152.126151.977943928FDB0226033-sulfinopyruvate;3-sulfinyl-pyruvate;3-sulfinylpyruvate;3-sulphinyl-pyruvate;Beta-sulfinylpyruvatePW_C0010853Sulfpa7118777831111205611221231951351148Pyridoxal 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-N247.1419247.024573569FDB021820Apolon 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'P182324453518122140119696201110421450501458262120102150495325111541611754211035441118545512055671325581133653385701816071672057216212722221311858161121751511262331126281812684289126892907701725377037225770412937705222477526112777643417797334677979327782923457885533278862331806961359863071199121221200241241200294061200874071208174181211494231211554241220691231220763831228341191234024541237214581237274591246204471246273981253022971254022991254074791254584811258034891262242981262314951269423881269475011269962061272585061277865131277933901420WaterHMDB0002111Water 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).7732-18-5C0000196215377937OH2OInChI=1S/H2O/h1H2XLYOFNOQVPJJNP-UHFFFAOYSA-N18.015318.010564686FDB013390Dihydrogen oxide;Steam;[oh2];Acqua;Agua;Aqua;Bound water;Dihydridooxygen;Eau;H2o;Hoh;Hydrogen hydroxide;WasserPW_C001420H2O5589491095139415131621448113526156242865210691207703382318838210943113774914655415904320182425322226786027274627781728052931437031647236346145983647273749419350302751567519597521410052279452361035297105531911153431135355112540211054701235483125549212655071275534130553711455411295591135560811856221085691657591405778101584114358531465877107589095591014759401516032155605915760871616123163613315962151621816664771786507180660015267131176840188688816071622057181207719320672112117228213723821472432157295198735021673882107401212746722274922247500190758817082012258237226841416292652611850277119221641201128112213285122502861226428712327249125202271263265126932901270529112715292130072981301930013025301130373021326122313327294153403084232731542695318436913227691429377019253771021327713113377215134773783317739733277471333775161157753633477628336777223377775934177816343779823477807132978235352782423537827035679113360800143688003937080591228806561199383038394794384110557390110639391115844398119879232119915122119963406120008407120046408120113124120365412120430405120438409120606415120794414121158425121240429121351121121381419121607434122118382122384436122753120122797374122804443123012446123064376123072137123131447123142136123162448123231451123384450123730460123810464123940455124165469124670399124938471124945472125305297125353479125386481125424482125480299125682483125707478125745487126054490126238495126273484126764480126896501126963502127017388127177208127199209127227504127506507127576515127836389128082395128176513140674790140675834140755185164Pyruvic acidHMDB0000243Pyruvic 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).127-17-3C00022106032816PYRUVATE1031DB00119CC(=O)C(O)=OC3H4O3InChI=1S/C3H4O3/c1-2(4)3(5)6/h1H3,(H,5,6)LCTONWCANYUPML-UHFFFAOYSA-N88.062188.016043994FDB0082932-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-oxopropionsaeurePW_C000164Pyr172204422811813144950145726536510354051175440118544412055661325570133589395592014759511516022155606715660741616126160638316467178651017765328574572227495220820022512622311529224915349187731011177972346779783277809011280004368800423678069513511287994115683121119950406120011124120175122120878407121148423121154424123454119123720458123726459125340479125390299125534297125854481126883501126931388127067205127858206162SulfiteHMDB0000240Endogenous sulfite is generated as a consequence of the body's normal processing of sulfur-containing amino acids. Sulfites occur as a consequence of fermentation and also occur naturally in a number of foods and beverages. As food additives, sulfiting agents were first used in 1664 and have been approved in the United States since the 1800s. Sulfite is an allergen, a neurotoxin, and a metabotoxin. An allergen is a compound that causes allergic reactions such as wheezing, rash, or rhinitis. A neurotoxin is a substance that causes damage to nerves or brain tissues. A metabotoxin is an endogenously produced metabolite that causes adverse health effects at chronically high levels. As an allergen, sulfite is known to induce asthmatic reactions. Sulfite sensitivity occurs most often in asthmatic adults (predominantly women), but it is also occasionally reported in preschool children. Adverse reactions to sulfites in nonasthmatics are extremely rare. Asthmatics who are steroid-dependent or who have a higher degree of airway hyperreactivity may be at greater risk of experiencing a reaction to sulfite-containing foods. Sulfite sensitivity reactions vary widely, ranging from no reaction to severe. The majority of reactions are mild. These manifestations may include dermatologic, respiratory, or gastrointestinal signs and symptoms. The precise mechanisms of the sensitivity responses have not been completely elucidated: inhalation of sulfur dioxide (SO2) generated in the stomach following ingestion of sulfite-containing foods or beverages, a deficiency in a mitochondrial enzyme, and an IgE-mediated immune response have all been implicated. Exogenously supplied sulfite is detoxified by the enzyme sulfite oxidase. Sulfite oxidase (EC 1.8.3.1) is 1 of 3 enzymes in humans that require molybdenum as a cofactor. Under certain circumstances, chronically high levels of sulfite can lead to serious neurotoxicity. Sulfite oxidase deficiency (also called molybdenum cofactor deficiency) is a rare autosomal inherited disease that is typified by high concentrations of sulfite in the blood and urine. It is characterized by severe neurological symptoms such as untreatable seizures, attenuated growth of the brain, and mental retardation. It results from defects in the enzyme sulfite oxidase, which is responsible for the oxidation of sulfite to sulfate. This sulfite to sulfate reaction is the final step in the degradation of sulfur-containing metabolites (including the amino acids cysteine and methionine). The term "isolated sulfite oxidase deficiency" is used to define the deficiency caused by mutations in the sulfite oxidase gene. This differentiates it from another version of sulfite oxidase deficiency that is due to defects in the molybdenum cofactor biosynthetic pathway (with mutations in the MOCS1 or MOCS2 genes). Isolated sulfite oxidase deficiency is a rare but devastating neurologic disease that usually presents in early infancy with seizures and alterations in muscle tone (PMID: 16234925, 16140720, 8586770). Sulfite oxidase deficiency (as caused by MOCS1 or MOCS2) may be treated with cPMP, a precursor of the molybdenum cofactor (PMID: 20385644). The mechanism behind sulfite neurotoxicity appears to be related to its ability to bind and inhibit glutamate dehydrogenase (GDH). Inhibition of GDH leads to a decrease in alpha-ketoglutarate and a diminished flux through the tricarboxylic acid cycle. This is accompanied by a decrease in NADH through the mitochondrial electron transport chain, which leads to a decrease in mitochondrial membrane potential and in ATP synthesis. Since glutamate is a major metabolite in the brain, inhibition of GDH by sulfite appears to contribute to neural damage characteristic of sulfite oxidase deficiency in human infants (PMID: 15273247).14265-45-3C00094109917359SO31068OS(O)=OH2O3SInChI=1S/H2O3S/c1-4(2)3/h(H2,1,2,3)LSNNMFCWUKXFEE-UHFFFAOYSA-N82.07981.97246462FDB021915Bisulfite;Sulfite dianion;Sulfite ion;Sulfite ions;Sulfonate;Sulfur trioxide;Sulfuric anhydride;Sulphite;Trioxosulfate(2-);Trioxosulfate(iv);Trioxosulphate(2-);Trioxosulphate(iv);[so3](2-);So3(2-);Sulphite ionPW_C000162Sulfite71381241377784111790001121205631221209524071231971351235181191258934811273542061827Hydrogen sulfideHMDB0003276Hydrogen sulfide is a highly toxic and flammable gas. Because it is heavier than air it tends to accumulate at the bottom of poorly ventilated spaces. Although very pungent at first, it quickly deadens the sense of smell, so potential victims may be unaware of its presence until it is too late. H2S arises from virtually anywhere where elemental sulfur comes into contact with organic material, especially at high temperatures. Hydrogen sulfide is a covalent hydride chemically related to water (H2O) since oxygen and sulfur occur in the same periodic table group. It often results when bacteria break down organic matter in the absence of oxygen, such as in swamps, and sewers (alongside the process of anaerobic digestion). It also occurs in volcanic gases, natural gas and some well waters. It is also important to note that Hydrogen sulfide is a central participant in the sulfur cycle, the biogeochemical cycle of sulfur on Earth. As mentioned above, sulfur-reducing and sulfate-reducing bacteria derive energy from oxidizing hydrogen or organic molecules in the absence of oxygen by reducing sulfur or sulfate to hydrogen sulfide. Other bacteria liberate hydrogen sulfide from sulfur-containing amino acids. Several groups of bacteria can use hydrogen sulfide as fuel, oxidizing it to elemental sulfur or to sulfate by using oxygen or nitrate as oxidant. The purple sulfur bacteria and the green sulfur bacteria use hydrogen sulfide as electron donor in photosynthesis, thereby producing elemental sulfur. (In fact, this mode of photosynthesis is older than the mode of cyanobacteria, algae and plants which uses water as electron donor and liberates oxygen).7783-06-4C002831877992616136HS391SH2SInChI=1S/H2S/h1H2RWSOTUBLDIXVET-UHFFFAOYSA-N34.08133.987720754FDB009599Acide sulfhydrique;Dihydrogen disulfide;Dihydrogen monosulfide;Dihydrogen sulfide;Hepatate;Hepatic acid;Hepatic gas;Hydrogen monosulfide;Hydrogen sulfide;Hydrogen-sulfide;Hydrogene sulfure;Hydrosulfurate;Hydrosulfuric acid;Idrogeno solforato;Schwefelwasserstoff;Sewer gas;Siarkowodor;Sour gas;Stink damp;Sulfur hydride;Sulfur hydroxide;Sulfureted hydrogen;Sulfuretted hydrogen;Zwavelwaterstof;[sh2];H2s;Hydrogen sulphide;Sulfide;Sulfure d'hydrogene;Acide sulphhydrique;Dihydrogen monosulphide;Dihydrogen sulphide;Hydrogen monosulphide;Hydrogen-sulphide;Hydrogene sulphure;Hydrosulfate;Hydrosulphate;Hydrosulphuric acid;Sulphide;Sulphure d'hydrogenePW_C001827H2SO71487778511112057212212320613535AmmoniaHMDB0000051Ammonia 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-N17.030517.026549101FDB003908Ammonia 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_C000035NH3979112513381424438247913550141468542533222572353381116016147702216071772051178619811848277118852151270829112718292769662257704629477329133773431327746933377499113775393347759711577985347779931127807232979244293806501358065711911620310911992112212004940812005312612013640712034340612036341212046240512104612412116142512211938212280037412280544312299312012301044612309637612361011812373346012467139912531129712542748212543130112550248112566347912570847812610229912627448412696650212697020712703920612715850112720020912760038812783738910563-Mercaptopyruvic acidHMDB00013683-Mercaptopyruvic acid is an intermediate in the metabolism of Cysteine. It is a substrate for L-lactate dehydrogenase A chain, 3-mercaptopyruvate sulfurtransferase, Aspartate aminotransferase (mitochondrial), L-lactate dehydrogenase C chain, L-lactate dehydrogenase A-like 6A, Aspartate aminotransferase (cytoplasmic), L-lactate dehydrogenase B chain and L-lactate dehydrogenase A-like 6B.2464-23-5C0095798162083-MERCAPTO-PYRUVATE96OC(=O)C(=O)CSC3H4O3SInChI=1S/C3H4O3S/c4-2(1-7)3(5)6/h7H,1H2,(H,5,6)OJOLFAIGOXZBCI-UHFFFAOYSA-N120.127119.988114684FDB0218623-mercapto-pyruvate;3-mercapto-pyruvic acid;3-mercaptopyruvate;3-mercaptopyruvic acid;Mercaptopyruvate;Mercaptopyruvic acid;Thiopyruvate;Beta-3-mercapto-2-oxo-propanoate;Beta-3-mercapto-2-oxo-propanoic acid;Beta-mercaptopyruvate;Beta-mercaptopyruvic acid;Beta-thiopyruvate;Beta-thiopyruvic acid;3-mercapto-2-oxopropanoic acid;3-mercapto-2-oxopropanoatePW_C0010563McPyra7158777861111205641221231981351399CyanideHMDB0002084The cyanide ion consists of a carbon triple bonded to a nitrogen. It readily reacts with hydrogen to form hydrogen cyanide gas, which has a faint almond-like smell. Most people can smell hydrogen cyanide; however, due to an apparent genetic trait, some individuals cannot. Cyanide gas (HCN) can be generated via combustion, including the exhaust of internal combustion engines, tobacco smoke, and especially some plastics derived from acrylonitrile (because of the latter effect, house fires can result in poisonings of the inhabitants). Cyanides are also produced by certain bacteria, fungi, and algae and are found in a number of foods and plants. Small amounts of cyanide can be found in apple seeds, mangoes and bitter almonds. Hydrocyanic acid (a solution of hydrogen cyanide in water) is present in freshly distilled bitter almond oil (2-4%) prior to its removal by precipitation as calcium ferrocyanide to give food quality oil. Hydrogen cyanide and most cyanide salts readily dissolve in water (or other biofluids) and exists in solution as the cyanide ion. Cyanide ions bind to the iron atom of the enzyme cytochrome c oxidase (also known as aa3) in the fourth complex in the mitochondrial membrane in the mitochondria of cells. The binding of cyanide to this cytochrome prevents transport of electrons from cytochrome c oxidase to oxygen. As a result, the electron transport chain is disrupted, meaning that the cell can no longer aerobically produce ATP for energy. Tissues that mainly depend on aerobic respiration, such as the central nervous system and the heart, are particularly affected. Because of its respiratory chain toxicity cyanide has been used as a poison many times throughout history. Its most infamous application was the use of hydrogen cyanide by the Nazi regime in Germany for mass murder in some gas chambers during the Holocaust. Hydrogen cyanide (with the historical common name of Prussic acid) is a colorless and highly volatile liquid that boils slightly above room temperature at 26 °C (78.8 °F). Hydrogen cyanide is weakly acidic and partly ionizes in solution to give the cyanide anion, CN-. The salts of hydrogen cyanide are known as cyanides. HCN is a highly valuable precursor to many chemical compounds ranging from polymers to pharmaceuticals. Hydrogen cyanide is a linear molecule, with a triple bond between carbon and nitrogen. It is a weak acid with a pKa of 9.2. A minor tautomer of HCN is HNC, hydrogen isocyanide.57-12-5C001775975175145755C#[N-]CHNInChI=1S/CHN/c1-2/h1H/q-1ATBDVLSINHAXGY-UHFFFAOYSA-N27.025327.010899037FDB006696Carbon nitride ion;Chuck norrisium;Cyanide;Cyanide ion;Cyanide(1-) ion;Cyano;Cyanure;Isocyanide;PrussiatePW_C001399Cyanide7168777871111205651221231991351122ThiocyanateHMDB0001453Thiocyanate is analogous to the cyanate ion, [OCN]-, wherein oxygen is replaced by sulfur. [SCN]- is one of the pseudohalogens, due to the similarity of its reactions to that of halide ions. Thiocyanate was formerly known as rhodanide (from a Greek word for rose) because of the red color of its complexes with iron. Thiocyanates are typically colorless. Cyanide ions can react with cystine to yield thicocyanate. This reaction occurs to a slight extent even in neutral solution, but is more pronounced in alkaline solutions of cystine. In addition to this non-enzymatic route, cyanide produced in vivo can be converted in part to thiocyanate by sulfur transferase systems. The thiocyanate ion can be oxidized at acid pH by hydrogen peroxide to generate sulfate and cyanide. The reaction is catalyzed by hemoglobin acting as a peroxidase.302-04-5C01755932218022HSCN8961[S-]C#NCNSInChI=1S/CHNS/c2-1-3/h3H/p-1ZMZDMBWJUHKJPS-UHFFFAOYSA-M58.08257.975144695FDB013883Rhodanide;Scn;Ammonium rhodanate;Ammonium rhodanide;Ammonium sulfocyanate;Hscn;Hydrogen thiocyanate;Nitridosulfanidocarbon;Rhodanid;Silver thiocyanate agscn;Thallium thiocyanate;Thiocyanate ion;Thiocyanic acid;Thiocyanid;Weedazol tl;[s-c#n](-);N#c-s(-);Scn(-);Thiocyanate ion (1-);ThiozyanatPW_C001122SCN71787778811112056612212320013514313-Mercaptolactic acidHMDB00021273-Mercaptolactic acid, also known as 3-mercaptolactate, belongs to the class of organic compounds known as monosaccharides. Monosaccharides are compounds containing one carbohydrate unit not glycosidically linked to another such unit, and no set of two or more glycosidically linked carbohydrate units. Monosaccharides have the general formula CnH2nOn. 3-Mercaptolactic acid is soluble (in water) and a weakly acidic compound (based on its pKa). Within the cell, 3-mercaptolactic acid is primarily located in the cytoplasm. In humans, 3-mercaptolactic acid is involved in the cysteine metabolism pathway and the cystinosis, ocular nonnephropathic pathway. 3-Mercaptolactic acid is also involved in the metabolic disorder called the Beta-mercaptolactate-cysteine disulfiduria pathway. 3-Mercaptolactic acid is a thiol that has been confirmed to be found in urine (PMID 8852041).2614-83-7C05823160645141158OC(CS)C(O)=OC3H6O3SInChI=1S/C3H6O3S/c4-2(1-7)3(5)6/h2,4,7H,1H2,(H,5,6)OLQOVQTWRIJPRE-UHFFFAOYSA-N122.143122.003764748FDB0228563-mercaptolactate;B-mercaptolactate;B-mercaptolactic acid;Beta-mercaptolactate;Beta-mercaptolactic acidPW_C0014313-Mcla719877790111120568122123202135721NADHMDB0000902NAD (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-N663.4251663.109121631FDB0223093-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_C000721NAD140415033538651101114211344312735146654222949277917283529310794807184813184819284902649603151679552381035334111536011254691235482125559013556101185696100573810858271415912147594215160241556072157607616163851646917867721176890160701218870971637174205719720674051987459222824122683592259085224118192161232224913006298130183001325622342404322426193157710413277120133772091347737033177650336776673347770233277709130779151137798334778406356800063688069011993825124110552388112750166112853941199291221199524061201714071208344191209844081211594251212421261212594291218173831226143841227421201231304471231411361234194551235493741237314601238124431238294641243703981251871211253192971253424791255304811258062991258254901259244821265154951267654801268855011272785071273835021280893901283603911284283951407571851144NADHHMDB0001487NADH 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-N665.441665.124771695FDB0226491,4-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_C001144NADH14341533490864810111521275514695422304927811728362931099480618481218482128490464959315169955240103533211153581125466123547912555931355698100573710858291415915147594515160271556079161638716472178677111768931607011188709916371722057195206746222282442268360225908622411809198118212161232024913003298130153001325522342403322426183157710713277123133772081347737133177651336776683347770033277707130779171137798634780009368806911199382212411054938811285494115838118119955406120172407120378122120986408121162425121244126121693429121818383122616384122745120123127447123138136123551374123734460123814443124242464124371398125189121125345479125531481125762297125808299125926482126516495126767480126888501127385502128090390128362391128429395140759185448L-CysteineHMDB0000574Cysteine is a naturally occurring, sulfur-containing amino acid that is found in most proteins, although only in small quantities. Cysteine is unique amongst the twenty natural amino acids as it contains a thiol group. Thiol groups can undergo oxidation/reduction (redox) reactions; when cysteine is oxidized it can form cystine, which is two cysteine residues joined by a disulfide bond. This reaction is reversible since the reduction of this disulphide bond regenerates two cysteine molecules. The disulphide bonds of cystine are crucial to defining the structures of many proteins. Cysteine is often involved in electron-transfer reactions, and help the enzyme catalyze its reaction. Cysteine is also part of the antioxidant glutathione. N-Acetyl-L-cysteine (NAC) is a form of cysteine where an acetyl group is attached to cysteine's nitrogen atom and is sold as a dietary supplement. Cysteine is named after cystine, which comes from the Greek word kustis meaning bladder (cystine was first isolated from kidney stones). Oxidation of cysteine can produce a disulfide bond with another thiol and further oxidation can produce sulphfinic or sulfonic acids. The cysteine thiol group is also a nucleophile and can undergo addition and substitution reactions. Thiol groups become much more reactive when they are ionized, and cysteine residues in proteins have pKa values close to neutrality, so they are often in their reactive thiolate form in the cell. The thiol group also has a high affinity for heavy metals and proteins containing cysteine will bind metals such as mercury, lead, and cadmium tightly. Due to this ability to undergo redox reactions, cysteine has antioxidant properties. Cysteine is an important source of sulfur in human metabolism, and although it is classified as a non-essential amino acid, cysteine may be essential for infants, the elderly, and individuals with certain metabolic disease or who suffer from malabsorption syndromes. Cysteine may at some point be recognized as an essential or conditionally essential amino acid (Wikipedia). Cysteine is important in energy metabolism. As cystine, it is a structural component of many tissues and hormones. Cysteine has clinical uses ranging from baldness to psoriasis to preventing smoker's hack. In some cases, oral cysteine therapy has proved excellent for treatment of asthmatics, enabling them to stop theophylline and other medications. Cysteine also enhances the effect of topically applied silver, tin, and zinc salts in preventing dental cavities. In the future, cysteine may play a role in the treatment of cobalt toxicity, diabetes, psychosis, cancer, and seizures (http://www.dcnutrition.com/AminoAcids/).52-90-4C00097586217561CYS5653DB00151N[C@@H](CS)C(O)=OC3H7NO2SInChI=1S/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1XUJNEKJLAYXESH-REOHCLBHSA-N121.158121.019749163DBMET00503FDB012678(+)-2-amino-3-mercaptopropionic acid;(2r)-2-amino-3-mercaptopropanoate;(2r)-2-amino-3-mercaptopropanoic acid;(2r)-2-amino-3-sulfanylpropanoate;(2r)-2-amino-3-sulfanylpropanoic acid;(r)-(+)-cysteine;(r)-2-amino-3-mercaptopropanoate;(r)-2-amino-3-mercaptopropanoic acid;(r)-2-amino-3-mercapto-propanoate;(r)-2-amino-3-mercapto-propanoic acid;(r)-cysteine;2-amino-3-mercaptopropanoate;2-amino-3-mercaptopropanoic acid;2-amino-3-mercaptopropionate;2-amino-3-mercaptopropionic acid;3-mercapto-l-alanine;Acetylcysteine;B-mercaptoalanine;Carbocysteine;Cisteina;Cisteinum;Cystein;Cysteine;Cysteinum;Free cysteine;Half-cystine;L cysteine;L-(+)-cysteine;L-2-amino-3-mercaptopropanoate;L-2-amino-3-mercaptopropanoic acid;L-2-amino-3-mercaptopropionic acid;L-cystein;L-cysteine;Polycysteine;Thioserine;Alpha-amino-beta-thiolpropionic acid;Beta-mercaptoalanine;C;Cys;E920;L-zystein;(2r)-2-amino-3-sulphanylpropanoate;(2r)-2-amino-3-sulphanylpropanoic acid;L-2-amino-3-mercaptopropionatePW_C000448Cys17481867228649287015576710158011086756117675910770781887496224759416082562278260225120122811226915142651315437303227777811177795113777961328070413512012512212013112412058012612286311812321044312549129712549829912702920512703538832Adenosine monophosphateHMDB0000045Adenosine 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.61-19-8C00020608316027AMP5858DB00131NC1=C2N=CN([C@@H]3O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]3O)C2=NC=N1C10H14N5O7PInChI=1S/C10H14N5O7P/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(22-10)1-21-23(18,19)20/h2-4,6-7,10,16-17H,1H2,(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1UDMBCSSLTHHNCD-KQYNXXCUSA-N347.2212347.063084339DBMET00485FDB0218065'-amp;5'-adenosine monophosphate;5'-adenylate;5'-adenylic acid;Amp;Adenosine 5'-monophosphate;Adenosine 5'-phosphate;Adenosine 5'-phosphorate;Adenosine 5'-phosphoric acid;Adenosine phosphate;Adenosine-5'-monophosphorate;Adenosine-5'-monophosphoric acid;Adenosine-5-monophosphorate;Adenosine-5-monophosphoric acid;Adenosine-monophosphate;Adenosine-phosphate;Adenovite;Adenylate;Adenylic acid;Cardiomone;Lycedan;Muscle adenylate;Muscle adenylic acid;My-b-den;My-beta-den;Phosaden;Phosphaden;Phosphentaside;5'-o-phosphonoadenosine;Adenosine 5'-(dihydrogen phosphate);Adenosine monophosphate;Adenosine-5'p;Adenosini phosphas;Ado5'p;Fosfato de adenosina;Pa;Pado;Phosphate d'adenosine;5'-adenosine monophosphoric acid;Adenosine phosphoric acid;Adenosine 5'-(dihydrogen phosphoric acid);Adenosine 5'-monophosphoric acid;Adenosine monophosphoric acid;Adenosine-5'-monophosphate;Phosphoric acid d'adenosinePW_C000032AMP112344628270167343288122118914457254867545033895251104540811754231035432118545712055581325583133577910157951086977199707218811789198118681611198815112003222125802261263631126942901333122542266342646315772343297732511178392334788091157932011280399180684135809007119916122120016124120031406120246382120888405121954408122920399123464376124507374125306297125394299125409479125596484126853205126934388126949501127124389127311209127711502140771891170PyrophosphateHMDB0000250The 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.14000-31-8C0001364410218361PPI559142DB04160OP(O)(=O)OP(O)(O)=OH4O7P2InChI=1S/H4O7P2/c1-8(2,3)7-9(4,5)6/h(H2,1,2,3)(H2,4,5,6)XPPKVPWEQAFLFU-UHFFFAOYSA-N177.9751177.943225506FDB021918(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 ionPW_C000170Ppi1223546384292373532882221217316204924105928152941751448685450348952521045294101540911754241035433118545812055481115559132558413356061355655108587910762391666978199707318871341637272160731219873182138275151828321011869161120022221204116412315225123232491251228812579226126952901521930615375183476017425613154269731877235329773171287763533678416335789283317915311279950134799581308004737280417170856301947863849481412594819382986782231106343911132703951132753891155271361155323991199341221200171241200324061203304101209364071212614291213411211214863831224074221229854441235021191238314641240443981249773751253242971253952991254104791255974841256564851258764811265524911268692051269353881269505011273372061281245081407728911005Zinc (II) ionHMDB0001303Zinc 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.23713-49-7C000383205129105ZN%2b229723DB01593[Zn++]ZnInChI=1S/Zn/q+2PTFCDOFLOPIGGS-UHFFFAOYSA-N65.40963.929146578FDB003729Zinc;Zinc ion;Dietary zinc;Zinc cation;Zinc, ion (zn2+);Zn(ii);Zn(2+);Zn2+PW_C001005Zinc1323841188271165291529575130446831202931477054101175425103543411854591205560132558513355981357449166117871981246622612724290133211517696722577401111775801147792933680400112002012412003540612006012212044140912125742912307513712382746412539829912541347912543829712568548312693838812695350112697620512718020815tRNA(Cys)RNAPW_NA00001529167TRNACYS730473787779211112057712212320713516L-Cysteinyl-tRNA(Cys)RNAPW_NA00001629152LCTC7314738877793111120578122123208135491Glutamate--cysteine ligase catalytic subunitP48506HMDBP00512GCLC6p12L3977316.3.2.2176846592492Glutamate--cysteine ligase regulatory subunitP48507HMDBP00513GCLM1p22.1CR5418331177846602891Cysteine dioxygenase type 1Q16878Initiates several important metabolic pathways related to pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. Critical regulator of cellular cysteine concentrations. Has an important role in maintaining the hepatic concentation of intracellular free cysteine within a proper narrow range.
HMDBP00948CDO15q23.2CH47108611.13.11.207108277Aspartate aminotransferase, cytoplasmicP17174Plays a key role in amino acid metabolism (By similarity).
HMDBP00283GOT110q24.1-q25.1BC00049812.6.1.1; 2.6.1.3712819952141826261431431511Cystathionine gamma-lyaseP32929Catalyzes the last step in the trans-sulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two cysteine molecules to lanthionine and hydrogen sulfide. Can also accept homocysteine as substrate. Specificity depends on the levels of the endogenous substrates. Generates the endogenous signaling molecule hydrogen sulfide (H2S), and so contributes to the regulation of blood pressure. Acts as a cysteine-protein sulfhydrase by mediating sulfhydration of target proteins: sulfhydration consists of converting -SH groups into -SSH on specific cysteine residues of target proteins such as GAPDH, PTPN1 and NF-kappa-B subunit RELA, thereby regulating their function.
HMDBP00538CTH1p31.1BC01580714.4.1.13388186929863171458601187263-mercaptopyruvate sulfurtransferaseP25325Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. May have a role in cyanide degradation or in thiosulfate biosynthesis.
HMDBP00781MPST22q13.1Z7342012.8.1.27188836L-lactate dehydrogenase A-like 6AQ6ZMR3Displays an lactate dehydrogenase activity. Significantly increases the transcriptional activity of JUN, when overexpressed.
HMDBP00893LDHAL6A11p15.1AY58131311.1.1.277208240021423349994895CystinosinO60931Thought to transport cystine out of lysosomesHMDBP10818CTNS17p13CH4711081144087904437Cysteine--tRNA ligase, cytoplasmicP49589HMDBP09253CARS11p15.5BC00288016.1.1.1673982356L-lactate dehydrogenase A chainP00338HMDBP03579LDHA11p15.4CR54171411.1.1.278964814050211421172614378811692607Probable cysteine--tRNA ligase, mitochondrialQ9HA77HMDBP07369CARS213q34AK02218016.1.1.16732450Glutamate--cysteine ligase1PW_P0000505149115249211731202Cysteine dioxygenase type 11PW_P0002022208911915441203Aspartate aminotransferase, cytoplasmic1PW_P0002032212772921148182Cystathionine gamma-lyase1PW_P000082965114451148133582083-mercaptopyruvate sulfurtransferase1PW_P0002082267261210L-lactate dehydrogenase1PW_P00021022823561719Cystinosin1PW_P0007198124895212Cysteine--tRNA ligase, cytoplasmic1PW_P000212230443719610051211Probable cysteine--tRNA ligase, mitochondrial1PW_P0002112292607195100511337383711falsePW_R000711Right29107891Compoundfalse29111341Compoundtrue291210851Compoundfalse2913951Compoundtrue220203713truePW_R000713Right291610851Compoundfalse291714201Compoundtrue29181641Compoundfalse29191621Compoundtrue717falsePW_R000717Right292610561Compoundfalse292713991Compoundtrue29281641Compoundfalse292911221Compoundtrue2262082.8.1.2721falsePW_R000721Right293914311Compoundfalse29407211Compoundtrue294110561Compoundfalse294211441Compoundtrue2292101.1.1.27710falsePW_R000710Right29074481Compoundfalse290810651Compoundtrue29097891Compoundfalse2192021.13.11.20192falsePW_R000192Right8484481Compoundfalse84914201Compoundtrue85018271Compoundtrue8511641Compoundfalse852351Compoundtrue221824.4.1.1720falsePW_R000720Both29354481Compoundfalse29361341Compoundtrue293710561Compoundfalse2938951Compoundtrue228203300falsePW_R000300Right12634141Compoundtrue1264951Compoundfalse12654481Compoundfalse126610341Compoundtrue126714411Compoundtrue12688261Compoundfalse55506.3.2.2722falsePW_R000722Right29434141Compoundtrue29444481Compoundfalse2945151NucleicAcidtrue2946321Compoundtrue29471701Compoundtrue2948161NucleicAcidfalse2302116.1.1.162312126.1.1.16126PW_T0001261484481Compound92Right977192013-08-30T09:33:21-06:002013-08-30T09:33:21-06:0091024414842false130590510regular5030102595881false124056510regular20019010271034843false98090510regular503010281441846false97070510regular44431029826881false65074010regular20019010301065865false182688810regular78781031789881false218073410regular200190103254489false197078210regular100251033134881false238089410regular20019010341085881false2180131410regular200190103595881false2380112910regular2001901036114889false2235106419regular1003510371420849false2070150410regular78781038164881false1535132010regular2001901039162881false1745150910regular20019010401420849false170497010regular787810411827881false1357112010regular200190104235863false1708117610regular78781043114889false1584105219regular1003510441056881false750132010regular20019010451399881false985151010regular20019010461122881false1290151010regular2001901047134881false1150112010regular200190104895881false65096510regular2001901049114889false103599510regular1003510561431881false245132010regular2001901057721859false460133010regular503010581144860false685133010regular50305710448981false208528010regular2001901588147448281false153574010regular2001901588161414842false151561010regular5030158816232844false151141010regular50301588163170845false174140310regular63431588164100589false158750219regular10025244615968false171059014120nucleic_acidregular120115244716968false157930514120nucleic_acidregular120115313491897false10908008noneregular1507031449282false10857908proteinregular1507031589182false19457978subunitregular1507031627786false220010748subunitregular1608031751188false156410778subunitregular1408531872682false116513808subunitregular1507031927786false100510208subunitregular1608032383682false52013808subunitregular15070235048959076false18954708subunitregular15070594590443782false15625178subunitregular150702885025831331331431428920225831531515410321390Cofactor29020325831631615510361395Cofactor2918225831731715610431405Cofactor29220825831831829320325831931915710491414Cofactor2972102583233232100719259023432350482747212258593254594590812315881642165080Cofactor1390M1895 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1465 1109 1414 1165 1415 5false181408M1535 1415 C1505 1415 1345 1415 1315 1415 5false18trueM 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345false1409M1390 1510 C1389 1479 1378 1413 1315 1415 5false18trueM 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345false1414M1125 1040 L1125 1090 L1175 1040 z10true181423M445 1415 C475 1415 490 1415 520 1415 5false181424M485 1360 C484 1385 490 1415 520 1415 5false181425M750 1415 C720 1415 700 1415 670 1415 5false18trueM 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345false1426M710 1360 C710 1388 700 1415 670 1415 5false18trueM 25.946855044164835 13.26155629629604 L 11 12 L 17.380887721185843 25.575134323078345false16395M1340 565 C1340 535 1340 477 1340 447 5false18trueM 1102.5 527.0096189432334 L 1110 540 L 1117.5 527.0096189432334false16396M650 835 C620 835 560 835 530 835 5false18trueM 472.9903810567666 727.5 L 460 735 L 472.9903810567666 742.5false16400M2280 924 C2278 974 2162 983 2105 984 5false18trueM 1827.0096189432334 781.5 L 1840 774 L 1827.0096189432334 766.5false16401M2280 924 C2282 976 2271 1052 2190 1054 5false18trueM 1931.2893234255962 924.0555145587341 L 1930 939 L 1943.586965751421 932.6443441196277false16402M1635 1510 C1635 1540 1635 1600 1635 1630 5false18trueM 1357.5 1442.0096189432334 L 1365 1455 L 1372.5 1442.0096189432334false2165011M1740 781 C1775 762 2099 612 2145 585 5false18trueM 1435.9903810567666 688.5 L 1423 696 L 1435.9903810567666 703.5falsetrueM 2047.3358625362048 541.244701793366 L 2056 529 L 2041.0637084532825 527.6189877511558false2165012M1738 809 C1765 793 1967 697 2055 657 5false18trueM 1491.173764898285 728.8270007385537 L 1478 736 L 1490.7988820308822 743.8223154346755falsefalsefalse2165013M1735 835 C1788 810 1886 768 1975 730 5false18trueM 2052.0096189432334 662.5 L 2065 655 L 2052.0096189432334 647.5false2165014M1735 835 C1765 835 1915 832 1945 832 5false182165015M1865 888 C1870 853 1915 832 1945 832 5false182165016M2180 829 C2150 829 2125 832 2095 832 5false18trueM 861.9468550441649 251.26155629629605 L 847 250 L 853.3808877211858 263.5751343230783false2165022M1635 930 C1635 960 1634 1047 1634 1077 5false182165023M1704 1009 C1669 1014 1634 1047 1634 1077 5false182165024M1557 1215 C1586 1217 1634 1192 1634 1162 5false18trueM 721.9468550441649 626.261556296296 L 707 625 L 713.3808877211858 638.5751343230784false2165025M1635 1320 C1635 1290 1634 1192 1634 1162 5false18trueM 721.9468550441649 626.261556296296 L 707 625 L 713.3808877211858 638.5751343230784false2165026M1708 1215 C1687 1216 1634 1192 1634 1162 5false18trueM 721.9468550441649 626.261556296296 L 707 625 L 713.3808877211858 638.5751343230784false2165031M1635 930 C1638 1088 1298 1061 1165 1060 5false18trueM 419.94685504416486 653.261556296296 L 405 652 L 411.38088772118584 665.5751343230784false2165032M1250 1120 C1249 1073 1195 1060 1165 1060 5false18trueM 419.94685504416486 653.261556296296 L 405 652 L 411.38088772118584 665.5751343230784false2165033M850 1320 C852 1218 906 1060 1005 1060 5false18trueM 419.94685504416486 653.261556296296 L 405 652 L 411.38088772118584 665.5751343230784false2165034M850 1060 C880 1060 975 1060 1005 1060 5false18trueM 419.94685504416486 653.261556296296 L 405 652 L 411.38088772118584 665.5751343230784false2165047M1330 905 C1331 869 1336 835 1240 835 5false182165048M1340 755 C1340 821 1279 837 1240 835 5false182165049M1535 835 C1505 835 1270 835 1240 835 5false182165050M1005 905 C1009 872 1022 835 1090 835 5false18trueM 392.94685504416486 364.261556296296 L 378 363 L 384.38088772118584 376.5751343230783false2165051M992 748 C994 789 1008 833 1090 835 5false18trueM 392.94685504416486 364.261556296296 L 378 363 L 384.38088772118584 376.5751343230783false2165052M850 835 C880 835 1060 835 1090 835 5false18trueM 392.94685504416486 364.261556296296 L 378 363 L 384.38088772118584 376.5751343230783false2165074M1565 625 C1600 624 1637 617 1637 587 5false182165075M1635 740 C1635 710 1637 617 1637 587 5false182165076M1561 425 C1594 424 1637 487 1637 517 5false18trueM 633.9468550441649 542.261556296296 L 619 541 L 625.3808877211858 554.5751343230784false2165077M1741 424.5 C1692 425.5 1637 487 1637 517 5false18trueM 633.9468550441649 542.261556296296 L 619 541 L 625.3808877211858 554.5751343230784false2165078M1715 620 C1675 625 1638 607 1637 587 5false182165079M1639 412 C1639 442 1637 487 1637 517 5false18trueM 1676.5 759.9903810567666 L 1669 747 L 1661.5 759.9903810567666false2165080M1427.5 627.5 L1427.5 677.5 L1477.5 627.5 z10true182168865M2085 375 C2025 374 1969 421 1970 470 83false182168866M1740 757 C1843 731 1969 618 1970 540 83false18trueM 750.9468550441649 62.26155629629604 L 736 61 L 742.3808877211858 74.57513432307834false306257118111410311391Left111510331392Left111610341393Right111710351394Right288220290307257138111810341396Left111910371397Left112010381398Right112110391399Right309257178112710441406Left112810451407Left112910381408Right113010461409Right290226292314257218114310561423Left114410571424Left114510441425Right114610581426Right295229297488718257108195846915881472165014Left195847010302165015Left195847110312165016Right447092219289488720251928195847715881472165022Left195847810402165023Left195847910412165024Right195848010382165025Right195848110422165026Right447094221291488722257208195848615881472165031Left195848710472165032Left195848810442165033Right195848910482165034Right447096228293488725253008195850210242165047Left195850310252165048Left195850415881472165049Left195850510272165050Right195850610282165051Right195850710292165052Right44709955288488729257228195852015881612165074Left195852115881472165075Left195852215881622165076Right195852315881632165077Right68124462165078Left68224472165079Right44710323148274723064126254683757102168865Left4683815881472168866Right224702100979258282514false126537716regular857102516395Right9268292514false38080016regular858102916396Left9308372514false195594916regular862103116400Left9318382514false2040101916regular863103116401Left9328392514false1560163016regular864103816402Left572058342514false214555016regular5421015881472165011Left572068362514false205562216regular5421115881472165012Right572078352514false197569516regular5421215881472165013Left3196823502600.70.70252853201871982152551.71.7031432726747967320511300.80.8-40214902404796745803451.31.3-2523280360171M125 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