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Record Information
StatusDetected and Quantified
Creation Date2005-11-16 15:48:42 UTC
Update Date2021-09-14 14:57:20 UTC
Secondary Accession Numbers
  • HMDB01487
Metabolite Identification
Common NameNADH
DescriptionNicotinamide adenine dinucleotide (NAD) is a coenzyme central to metabolism. Found in all living cells, NAD is called a dinucleotide because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine nucleobase and the other nicotinamide. NAD exists in two forms: an oxidized and reduced form, abbreviated as NAD+ and NADH (H for hydrogen) respectively. NADH is the reduced form of NAD+, and NAD+ is the oxidized form of NADH. NAD (or nicotinamide adenine dinucleotide) is used extensively in glycolysis and the citric acid cycle of cellular respiration. The reducing potential stored in NADH can be either converted into 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 via cellular respiration. NAD is a coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by a 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). NADP is formed through the addition of a phosphate group to the 2' position of the adenosyl nucleotide through an ester linkage.
1,4-DIHYDRONICOTINAMIDE adenine dinucleotideChEBI
Nicotinamide adenine dinucleotide (reduced)ChEBI
Reduced nicotinamide adenine dinucleotideChEBI
Dihydrocodehydrogenase IHMDB
Dihydronicotinamide adenine dinucleotideHMDB
Dihydronicotinamide mononucleotideHMDB
Reduced codehydrogenase IHMDB
Reduced diphosphopyridine nucleotideHMDB
Reduced nicotinamide adenine diphosphateHMDB
Reduced nicotinamide-adenine dinucleotideHMDB
Coenzyme IHMDB
Diphosphopyridine nucleotideHMDB
Nicotinamide adenine dinucleotideHMDB
Nicotinamide-adenine dinucleotideHMDB
Nucleotide, diphosphopyridineHMDB
Adenine dinucleotide, dihydronicotinamideHMDB
Dinucleotide, dihydronicotinamide adenineHMDB
Dinucleotide, nicotinamide-adenineHMDB
Chemical FormulaC21H29N7O14P2
Average Molecular Weight665.441
Monoisotopic Molecular Weight665.124771695
IUPAC Name[({[(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 acid
Traditional NameNADH
CAS Registry Number58-68-4
InChI Identifier
Chemical Taxonomy
Description Belongs to the class of organic compounds known as (5'->5')-dinucleotides. These are dinucleotides where the two bases are connected via a (5'->5')-phosphodiester linkage.
KingdomOrganic compounds
Super ClassNucleosides, nucleotides, and analogues
Sub ClassNot Available
Direct Parent(5'->5')-dinucleotides
Alternative Parents
  • (5'->5')-dinucleotide
  • Purine nucleotide sugar
  • Purine ribonucleoside diphosphate
  • Purine ribonucleoside monophosphate
  • Nicotinamide-nucleotide
  • Pentose phosphate
  • Pentose-5-phosphate
  • Glycosyl compound
  • N-glycosyl compound
  • 6-aminopurine
  • Monosaccharide phosphate
  • N-substituted nicotinamide
  • Organic pyrophosphate
  • Imidazopyrimidine
  • Purine
  • Monoalkyl phosphate
  • Dihydropyridine
  • Aminopyrimidine
  • Pyrimidine
  • Imidolactam
  • Monosaccharide
  • N-substituted imidazole
  • Alkyl phosphate
  • Phosphoric acid ester
  • Hydropyridine
  • Organic phosphoric acid derivative
  • Heteroaromatic compound
  • Tetrahydrofuran
  • Imidazole
  • Vinylogous amide
  • Azole
  • Amino acid or derivatives
  • Primary carboxylic acid amide
  • Secondary alcohol
  • Carboxamide group
  • Organoheterocyclic compound
  • Enamine
  • Azacycle
  • Oxacycle
  • Carboxylic acid derivative
  • Hydrocarbon derivative
  • Alcohol
  • Organic nitrogen compound
  • Organonitrogen compound
  • Organooxygen compound
  • Carbonyl group
  • Organic oxygen compound
  • Organopnictogen compound
  • Primary amine
  • Amine
  • Organic oxide
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors

Route of exposure:


Biological location:


Naturally occurring process:


Industrial application:

Physical Properties
Experimental Molecular Properties
Melting Point140.0 - 142.0 °CNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Molecular Properties
Water Solubility2.95 g/LALOGPS
pKa (Strongest Acidic)1.85ChemAxon
pKa (Strongest Basic)4.01ChemAxon
Physiological Charge-2ChemAxon
Hydrogen Acceptor Count16ChemAxon
Hydrogen Donor Count8ChemAxon
Polar Surface Area317.62 ŲChemAxon
Rotatable Bond Count11ChemAxon
Refractivity143 m³·mol⁻¹ChemAxon
Polarizability57.65 ųChemAxon
Number of Rings5ChemAxon
Rule of FiveNoChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleYesChemAxon
Predicted Spectral Properties

Collision Cross Sections

NameAdductTypeData SourceValueReference
DarkChem[M+H]+PredictedNot Available31661259
DarkChem[M-H]-PredictedNot Available31661259
AllCCS[M+H]+PredictedNot Available231.93732859911
AllCCS[M-H]-PredictedNot Available223.94532859911

Retention Indices


Not Available


Not Available


Spectrum TypeDescriptionSplash KeyDeposition DateView
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-002b-1301902000-1a1639ad87019605438c2017-09-01View Spectrum
MSMass Spectrum (Electron Ionization)splash10-002b-1301902000-1a1639ad87019605438c2021-09-05View Spectrum


Spectrum TypeDescriptionSplash KeyDeposition DateView
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-00n0-0210192000-bf07b6b154c5778067ce2018-05-25View Spectrum
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-0udi-0150291000-84ef746651797f0679a52018-05-25View Spectrum
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-004i-0970000000-0688003193d7fc4612352018-05-25View Spectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT 35V, negativesplash10-00di-0190000000-775fe0fdd09a45ed6a962020-07-21View Spectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT 35V, negativesplash10-052b-0019600000-3247f3ea96ec22c0e1902020-07-21View Spectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT 35V, negativesplash10-052b-0019600000-c62f2c56a1ce8a2874fb2020-07-21View Spectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF 32V, negativesplash10-03di-3212549000-5bb7a136d3e7ca7d8edd2020-07-21View Spectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF 30V, negativesplash10-00ea-1219600000-1e722b38e19c9839c3362020-07-21View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-000i-0931104000-bf6579d19ee9bc297e132015-09-15View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-000i-0901000000-92672b1d4b96838f86522015-09-15View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-000i-1900000000-ef56d203da65089e145f2015-09-15View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-03e9-1900207000-f248eb28a7283de7118b2015-09-15View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-001i-1900100000-efadf1d6c54e9e86671d2015-09-15View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0a7i-3900000000-f258fc2bf1d8e54ac6da2015-09-15View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-03di-0000009000-7483a50cefc91ed6c5232021-09-06View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-01t9-8300019000-ff2563ac55ede9fc0f692021-09-06View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0a6s-4539513000-6750c13a8d6fe643a5eb2021-09-06View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-014j-0200019000-83faade2f285d81f15202021-09-07View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-000j-0833149000-ab3d358d7d6c8e3a9c4e2021-09-07View Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-000j-1923200000-b013fe21d9ec536d8c042021-09-07View Spectrum


Spectrum TypeDescriptionDeposition DateView
1D NMR1H NMR Spectrum (1D, 500 MHz, H2O, experimental)2018-05-25View Spectrum
2D NMR[1H, 1H] 2D NMR Spectrum (predicted)2018-05-25View Spectrum
2D NMR[1H, 13C] NMR Spectrum (2D, 600 MHz, H2O, predicted)2018-05-25View Spectrum
Biological Properties
Cellular Locations
  • Mitochondria
  • Endoplasmic reticulum
  • Peroxisome
Biospecimen Locations
  • Blood
Tissue Locations
  • Bladder
  • Brain
  • Fibroblasts
  • Platelet
  • Skeletal Muscle
Normal Concentrations
BloodDetected and Quantified22.0 (14.0-40.0) uMAdult (>18 years old)BothNormal
    • Geigy Scientific ...
Abnormal Concentrations
BloodDetected and Quantified0.0081 uMInfant (0-1 year old)FemaleNicotinamide Adenine Dinucleotide Deficiency details
Associated Disorders and Diseases
Disease References
Nicotinamide Adenine Dinucleotide Deficiency
  1. Shi H, Enriquez A, Rapadas M, Martin EMMA, Wang R, Moreau J, Lim CK, Szot JO, Ip E, Hughes JN, Sugimoto K, Humphreys DT, McInerney-Leo AM, Leo PJ, Maghzal GJ, Halliday J, Smith J, Colley A, Mark PR, Collins F, Sillence DO, Winlaw DS, Ho JWK, Guillemin GJ, Brown MA, Kikuchi K, Thomas PQ, Stocker R, Giannoulatou E, Chapman G, Duncan EL, Sparrow DB, Dunwoodie SL: NAD Deficiency, Congenital Malformations, and Niacin Supplementation. N Engl J Med. 2017 Aug 10;377(6):544-552. doi: 10.1056/NEJMoa1616361. [PubMed:28792876 ]
Associated OMIM IDsNone
DrugBank IDDB00157
Phenol Explorer Compound IDNot Available
FooDB IDFDB022649
KNApSAcK IDC00019343
Chemspider ID903
KEGG Compound IDC00004
BiGG ID33484
Wikipedia LinkNicotinamide_adenine_dinucleotide
PubChem Compound439153
PDB IDNot Available
ChEBI ID16908
Food Biomarker OntologyNot Available
MarkerDB IDNot Available
Synthesis ReferenceMarek, Miroslav; Vrbova, Eva; Horakova, Irena; Musil, Petr; Kefurt, Karel. NADH manufacture with immobilized Candida formate dehydrogenase. Czech. (1992), 4 pp.
Material Safety Data Sheet (MSDS)Download (PDF)
General References
  1. Yamamoto T, Moriwaki Y, Takahashi S, Suda M, Higashino K: Ethanol as a xanthine dehydrogenase inhibitor. Metabolism. 1995 Jun;44(6):779-85. [PubMed:7783663 ]
  2. Nadlinger K, Westerthaler W, Storga-Tomic D, Birkmayer JG: Extracellular metabolisation of NADH by blood cells correlates with intracellular ATP levels. Biochim Biophys Acta. 2002 Nov 14;1573(2):177-82. [PubMed:12399028 ]
  3. Saada A, Bar-Meir M, Belaiche C, Miller C, Elpeleg O: Evaluation of enzymatic assays and compounds affecting ATP production in mitochondrial respiratory chain complex I deficiency. Anal Biochem. 2004 Dec 1;335(1):66-72. [PubMed:15519572 ]
  4. Heiman-Patterson TD, Argov Z, Chavin JM, Kalman B, Alder H, DiMauro S, Bank W, Tahmoush AJ: Biochemical and genetic studies in a family with mitochondrial myopathy. Muscle Nerve. 1997 Oct;20(10):1219-24. [PubMed:9324076 ]
  5. Mintun MA, Vlassenko AG, Rundle MM, Raichle ME: Increased lactate/pyruvate ratio augments blood flow in physiologically activated human brain. Proc Natl Acad Sci U S A. 2004 Jan 13;101(2):659-64. Epub 2004 Jan 2. [PubMed:14704276 ]
  6. Yeo SF, Zhang Y, Schafer D, Campbell S, Wong B: A rapid, automated enzymatic fluorometric assay for determination of D-arabinitol in serum. J Clin Microbiol. 2000 Apr;38(4):1439-43. [PubMed:10747122 ]
  7. Uppal A, Ghosh N, Datta A, Gupta PK: Fluorimetric estimation of the concentration of NADH from human blood samples. Biotechnol Appl Biochem. 2005 Feb;41(Pt 1):43-7. [PubMed:15035655 ]
  8. Yamamoto T, Moriwaki Y, Takahashi S, Suda M, Higashino K: Xylitol-induced increase in the concentration of oxypurines and its mechanism. Int J Clin Pharmacol Ther. 1995 Jun;33(6):360-5. [PubMed:7582389 ]
  9. Helge JW, Fraser AM, Kriketos AD, Jenkins AB, Calvert GD, Ayre KJ, Storlien LH: Interrelationships between muscle fibre type, substrate oxidation and body fat. Int J Obes Relat Metab Disord. 1999 Sep;23(9):986-91. [PubMed:10490806 ]
  10. Fulco M, Schiltz RL, Iezzi S, King MT, Zhao P, Kashiwaya Y, Hoffman E, Veech RL, Sartorelli V: Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state. Mol Cell. 2003 Jul;12(1):51-62. [PubMed:12887892 ]
  11. Krotz F, Sohn HY, Gloe T, Zahler S, Riexinger T, Schiele TM, Becker BF, Theisen K, Klauss V, Pohl U: NAD(P)H oxidase-dependent platelet superoxide anion release increases platelet recruitment. Blood. 2002 Aug 1;100(3):917-24. [PubMed:12130503 ]
  12. Li D, Gan Y, Wientjes MG, Badalament RA, Au JL: Distribution of DT-diaphorase and reduced nicotinamide adenine dinucleotide phosphate: cytochrome p450 oxidoreductase in bladder tissues and tumors. J Urol. 2001 Dec;166(6):2500-5. [PubMed:11696818 ]
  13. Desir G, Bratusch-Marrain P, DeFronzo RA: Effect of hyperketonemia on renal ammonia excretion in man. Metabolism. 1986 Aug;35(8):736-43. [PubMed:3736414 ]
  14. Odland LM, Heigenhauser GJ, Spriet LL: Effects of high fat provision on muscle PDH activation and malonyl-CoA content in moderate exercise. J Appl Physiol (1985). 2000 Dec;89(6):2352-8. [PubMed:11090589 ]
  15. Rani K, Garg P, Pundir CS: Measurement of bile acid in serum and bile with arylamine-glass-bound 3alpha-hydroxysteroid dehydrogenase and diaphorase. Anal Biochem. 2004 Sep 1;332(1):32-7. [PubMed:15301946 ]
  16. Nomura H, Koike F, Tsuruta Y, Iwaki A, Iwaki T: Autopsy case of autosomal recessive hereditary spastic paraplegia with reference to the muscular pathology. Neuropathology. 2001 Sep;21(3):212-7. [PubMed:11666018 ]
  17. Orallo F, Alvarez E, Camina M, Leiro JM, Gomez E, Fernandez P: The possible implication of trans-Resveratrol in the cardioprotective effects of long-term moderate wine consumption. Mol Pharmacol. 2002 Feb;61(2):294-302. [PubMed:11809853 ]
  18. Jawed S, Stevens CR, Harrison R, Blake DR: Elevated circulating plasma NADH oxidising activity of xanthine oxidoreductase in plasma. Biochem Soc Trans. 1997 Aug;25(3):531S. [PubMed:9388747 ]
  19. Harbord MG, Hwang PA, Robinson BH, Becker LE, Hunjan A, Murphy EG: Infant-onset progressive myoclonus epilepsy. J Child Neurol. 1991 Apr;6(2):134-42. [PubMed:1904460 ]
  20. Mayevsky A, Meilin S, Manor T, Ornstein E, Zarchin N, Sonn J: Multiparametric monitoring of brain oxygen balance under experimental and clinical conditions. Neurol Res. 1998;20 Suppl 1:S76-80. [PubMed:9584930 ]
  21. Biellmann JF, Lapinte C, Haid E, Weimann G: Structure of lactate dehydrogenase inhibitor generated from coenzyme. Biochemistry. 1979 Apr 3;18(7):1212-7. [PubMed:218616 ]
  22. Lin SJ, Guarente L: Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease. Curr Opin Cell Biol. 2003 Apr;15(2):241-6. [PubMed:12648681 ]
  23. Belenky P, Bogan KL, Brenner C: NAD+ metabolism in health and disease. Trends Biochem Sci. 2007 Jan;32(1):12-9. Epub 2006 Dec 11. [PubMed:17161604 ]
  24. Pollak N, Dolle C, Ziegler M: The power to reduce: pyridine nucleotides--small molecules with a multitude of functions. Biochem J. 2007 Mar 1;402(2):205-18. [PubMed:17295611 ]
  25. Khan JA, Forouhar F, Tao X, Tong L: Nicotinamide adenine dinucleotide metabolism as an attractive target for drug discovery. Expert Opin Ther Targets. 2007 May;11(5):695-705. [PubMed:17465726 ]
  26. Brunk E, Sahoo S, Zielinski DC, Altunkaya A, Drager A, Mih N, Gatto F, Nilsson A, Preciat Gonzalez GA, Aurich MK, Prlic A, Sastry A, Danielsdottir AD, Heinken A, Noronha A, Rose PW, Burley SK, Fleming RMT, Nielsen J, Thiele I, Palsson BO: Recon3D enables a three-dimensional view of gene variation in human metabolism. Nat Biotechnol. 2018 Mar;36(3):272-281. doi: 10.1038/nbt.4072. Epub 2018 Feb 19. [PubMed:29457794 ]
  27. WholeHealthMD [Link]

Only showing the first 10 proteins. There are 219 proteins in total.


General function:
Involved in catalytic activity
Specific function:
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
Specific function:
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Gene Name:
Uniprot ID:
Molecular weight:
Coenzyme A + NAD + Pyruvic acid → Carbon dioxide + Hydrogen Ion + NADH + Acetyl-CoAdetails
General function:
Involved in oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
Specific function:
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in oxidoreductase activity
Specific function:
Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA.
Gene Name:
Uniprot ID:
Molecular weight:
2-Methyl-3-oxopropanoic acid + Coenzyme A + Water + NAD → Propionyl-CoA + Hydrogen carbonate + NADHdetails
Malonic semialdehyde + Coenzyme A + NAD → Acetyl-CoA + Carbon dioxide + NADH + Hydrogen Iondetails
(S)-Methylmalonic acid semialdehyde + Coenzyme A + NAD → Propionyl-CoA + Carbon dioxide + NADH + Hydrogen Iondetails
(S)-Methylmalonic acid semialdehyde + Coenzyme A + NAD → Methylmalonyl-CoA + NADH + Hydrogen Iondetails
General function:
Involved in oxidoreductase activity
Specific function:
Lipoamide 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.
Gene Name:
Uniprot ID:
Molecular weight:
Protein N(6)-(dihydrolipoyl)lysine + NAD → protein N(6)-(lipoyl)lysine + NADHdetails
Dihydrolipoamide + NAD → Lipoamide + NADH + Hydrogen Iondetails
Dihydrolipoylprotein + NAD → Lipoylprotein + NADH + Hydrogen Iondetails
Enzyme N6-(dihydrolipoyl)lysine + NAD → Enzyme N6-(lipoyl)lysine + NADH + Hydrogen Iondetails
Coenzyme A + NAD + Pyruvic acid → Carbon dioxide + Hydrogen Ion + NADH + Acetyl-CoAdetails
General function:
Involved in acyltransferase activity
Specific function:
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Gene Name:
Uniprot ID:
Molecular weight:
Coenzyme A + NAD + Pyruvic acid → Carbon dioxide + Hydrogen Ion + NADH + Acetyl-CoAdetails
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the transformation of the potent androgen dihydrotestosterone (DHT) into the less active form, 5-alpha-androstan-3-alpha,17-beta-diol (3-alpha-diol). Also has some 20-alpha-hydroxysteroid dehydrogenase activity. The biotransformation of the pesticide chlordecone (kepone) to its corresponding alcohol leads to increased biliary excretion of the pesticide and concomitant reduction of its neurotoxicity since bile is the major excretory route.
Gene Name:
Uniprot ID:
Molecular weight:
Androsterone + NAD → Androstanedione + NADH + Hydrogen Iondetails
Etiocholanolone + NAD → Etiocholanedione + NADH + Hydrogen Iondetails
3a,7a-Dihydroxy-5b-cholestane + NAD → 7a-Hydroxy-5b-cholestan-3-one + NADH + Hydrogen Iondetails
5beta-Cholestane-3alpha,7alpha,12alpha-triol + NAD → 7a,12a-Dihydroxy-5b-cholestan-3-one + NADH + Hydrogen Iondetails
Tetrahydrocortisone + NAD → 17a,21-Dihydroxy-5b-pregnane-3,11,20-trione + NADH + Hydrogen Iondetails
Tetrahydrocortisol + NAD → Dihydrocortisol + NADH + Hydrogen Iondetails
3a,11b,21-Trihydroxy-20-oxo-5b-pregnan-18-al + NAD → 11b,21-Dihydroxy-3,20-oxo-5b-pregnan-18-al + NADH + Hydrogen Iondetails
Tetrahydrocorticosterone + NAD → 11b,21-Dihydroxy-5b-pregnane-3,20-dione + NADH + Hydrogen Iondetails
3a,21-Dihydroxy-5b-pregnane-11,20-dione + NAD → 21-Hydroxy-5b-pregnane-3,11,20-trione + NADH + Hydrogen Iondetails
3a-Hydroxy-5b-pregnane-20-one + NAD → 5a-Pregnane-3,20-dione + NADH + Hydrogen Iondetails
General function:
Involved in oxidoreductase activity
Specific function:
Prostaglandin inactivation. Contributes to the regulation of events that are under the control of prostaglandin levels. Catalyzes the NAD-dependent dehydrogenation of lipoxin A4 to form 15-oxo-lipoxin A4. Inhibits in vivo proliferation of colon cancer cells.
Gene Name:
Uniprot ID:
Molecular weight:
(5Z,13E,15S)-11-alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD → (5Z,13E)-11-alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADHdetails
General function:
Involved in oxidoreductase activity
Specific function:
This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6-dihydroxyindole to indole-5,6 quinone.
Gene Name:
Uniprot ID:
Molecular weight:
Tyramine + Oxygen + NADH + Hydrogen Ion → Dopamine + NAD + Waterdetails
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Gene Name:
Uniprot ID:
Molecular weight:
Glycerol + NAD → Glyceraldehyde + NADH + Hydrogen Iondetails
beta-D-Galactose + NADH + Hydrogen Ion → Galactitol + NADdetails
L-Arabitol + NAD → L-Arabinose + NADH + Hydrogen Iondetails
Lactaldehyde + NAD → Pyruvaldehyde + NADH + Hydrogen Iondetails

Only showing the first 10 proteins. There are 219 proteins in total.