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Record Information
Version4.0
StatusDetected and Quantified
Creation Date2005-11-16 15:48:42 UTC
Update Date2020-09-15 17:33:08 UTC
HMDB IDHMDB0000902
Secondary Accession Numbers
  • HMDB00902
Metabolite Identification
Common NameNAD
DescriptionNAD (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 (Wikipedia ). 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) (Dorland, 27th ed).
Structure
Data?1600191188
Synonyms
ValueSource
Codehydrogenase IChEBI
Coenzyme IChEBI
Cozymase IChEBI
Diphosphopyridine nucleotideChEBI
DPNChEBI
NadideChEBI
NICOTINAMIDE-adenine-dinucleotideChEBI
Adenine dinucleotide, dihydronicotinamideMeSH
NADMeSH
Nicotinamide-adenine dinucleotideMeSH
Nucleotide, diphosphopyridineMeSH
Dihydronicotinamide adenine dinucleotideMeSH
NADHMeSH
Nicotinamide adenine dinucleotideMeSH
Dinucleotide, nicotinamide-adenineMeSH
Dinucleotide, dihydronicotinamide adenineMeSH
Adenine-nicotinamide dinucleotideHMDB
NAD+HMDB
Oxidized diphosphopyridine nucleotideHMDB
beta-Diphosphopyridine nucleotideHMDB
beta-NADHMDB
beta-NAD+HMDB
beta-Nicotinamide adenine dinucleotideHMDB
beta-Nicotinamide adenine dinucleotide hydrateHMDB
β-Diphosphopyridine nucleotideHMDB
β-NADHMDB
β-NAD+HMDB
β-Nicotinamide adenine dinucleotideHMDB
β-Nicotinamide adenine dinucleotide hydrateHMDB
Chemical FormulaC21H27N7O14P2
Average Molecular Weight663.4251
Monoisotopic Molecular Weight663.109121631
IUPAC Name1-[(2R,3R,4S,5R)-5-({[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphono}oxy)(hydroxy)phosphoryl]oxy}methyl)-3,4-dihydroxyoxolan-2-yl]-3-(C-hydroxycarbonimidoyl)-1lambda5-pyridin-1-ylium
Traditional Name1-[(2R,3R,4S,5R)-5-{[({[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphono}oxy(hydroxy)phosphoryl)oxy]methyl}-3,4-dihydroxyoxolan-2-yl]-3-(C-hydroxycarbonimidoyl)-1lambda5-pyridin-1-ylium
CAS Registry Number53-84-9
SMILES
NC(=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]1O
InChI Identifier
InChI=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/s1
InChI KeyBAWFJGJZGIEFAR-NNYOXOHSSA-N
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
Class(5'->5')-dinucleotides
Sub ClassNot Available
Direct Parent(5'->5')-dinucleotides
Alternative Parents
Substituents
  • (5'->5')-dinucleotide
  • Purine nucleotide sugar
  • Purine ribonucleoside diphosphate
  • Purine ribonucleoside monophosphate
  • Nicotinamide-nucleotide
  • Pyridine nucleotide
  • Pentose-5-phosphate
  • Pentose phosphate
  • Glycosyl compound
  • N-glycosyl compound
  • 6-aminopurine
  • Monosaccharide phosphate
  • Organic pyrophosphate
  • Purine
  • Imidazopyrimidine
  • Nicotinamide
  • Monoalkyl phosphate
  • Aminopyrimidine
  • Monosaccharide
  • N-substituted imidazole
  • Organic phosphoric acid derivative
  • Imidolactam
  • Phosphoric acid ester
  • Alkyl phosphate
  • Pyrimidine
  • Pyridinium
  • Pyridine
  • Tetrahydrofuran
  • Azole
  • Imidazole
  • Heteroaromatic compound
  • Secondary alcohol
  • Carboximidic acid derivative
  • Carboximidic acid
  • Organoheterocyclic compound
  • Oxacycle
  • Azacycle
  • Hydrocarbon derivative
  • Organopnictogen compound
  • Organic oxide
  • Organic zwitterion
  • Primary amine
  • Organonitrogen compound
  • Amine
  • Organic nitrogen compound
  • Alcohol
  • Organic oxygen compound
  • Organooxygen compound
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors
Ontology
Physiological effect

Health effect:

Disposition

Source:

Biological location:

Process

Naturally occurring process:

Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting Point140.0 - 142.0 °CNot Available
Boiling PointNot AvailableNot Available
Water Solubility752.5 mg/mLNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
Water Solubility1.81 g/LALOGPS
logP-1.2ALOGPS
logP-10ChemAxon
logS-2.5ALOGPS
pKa (Strongest Acidic)1.85ChemAxon
pKa (Strongest Basic)6.38ChemAxon
Physiological Charge-1ChemAxon
Hydrogen Acceptor Count16ChemAxon
Hydrogen Donor Count8ChemAxon
Polar Surface Area322.08 ŲChemAxon
Rotatable Bond Count11ChemAxon
Refractivity151.81 m³·mol⁻¹ChemAxon
Polarizability58.5 ųChemAxon
Number of Rings5ChemAxon
BioavailabilityNoChemAxon
Rule of FiveNoChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleYesChemAxon
Spectra
Spectrum TypeDescriptionSplash KeyView
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-03di-0000029000-870aa620464a4fedbe8dSpectrum
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-002r-0930610000-ccd233f26036136ba3e8Spectrum
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-000i-0900000000-ec77ba41ae7dbcfd08a2Spectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-00dl-0219003700-2f52e3c5db41066a112cSpectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0uk9-0301009000-a3d0c464e56f6e320c80Spectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-00dl-0000090000-c18a7719161c63a71938Spectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0udi-0000009000-1dde5b221786fe375304Spectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0002-0911001000-bd16ca8021ab63e9e290Spectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-001i-0900000000-662adda5a00fce5c5017Spectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-03di-0900000000-a2724dbab2ca6eb7e8daSpectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-00dl-0400090000-19bb49ef6fe960f224d2Spectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-006x-0011297400-efee4fe3a4cf024c960aSpectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-004i-0028900000-8ec9bcaf25513495b979Spectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0a4i-0011953000-577487fb6aff29c77330Spectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-00di-0000009000-e1d0afb4e7926a0f845eSpectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0006-0001092010-1dcbca7a5ffe61f23e50Spectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-004i-0028900000-764e3ecea72fe178a87eSpectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-004i-0018900000-3b774fba9b96129baa6cSpectrum
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0006-0000090000-d4236efb9eec36017416Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-03di-0000009000-3cb1cc8e613a3e179149Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-014j-0000009000-4bd400c0be81ab938465Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0006-6920102000-5fc300f474c5dc2b8600Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-03di-0000009000-96d7faa48cdd181798a0Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-03di-1100109000-f496601a0ac75ae3d4a5Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-003s-9201000000-c06274c9b4d1b70a9ce2Spectrum
1D NMR1H NMR SpectrumNot AvailableSpectrum
1D NMR1H NMR SpectrumNot AvailableSpectrum
1D NMR1H NMR SpectrumNot AvailableSpectrum
1D NMR1H NMR SpectrumNot AvailableSpectrum
1D NMR13C NMR SpectrumNot AvailableSpectrum
2D NMR[1H,1H] 2D NMR SpectrumNot AvailableSpectrum
2D NMR[1H,13C] 2D NMR SpectrumNot AvailableSpectrum
Biological Properties
Cellular Locations
  • Extracellular
  • Mitochondria
  • Nucleus
  • Endoplasmic reticulum
  • Peroxisome
Biospecimen Locations
  • Blood
  • Cellular Cytoplasm
Tissue Locations
  • Adrenal Gland
  • Brain
  • Epidermis
  • Fibroblasts
  • Liver
  • Placenta
  • Platelet
  • Prostate
  • Skeletal Muscle
Pathways
Normal Concentrations
BiospecimenStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified24.3 (23.0-25.6) uMAdult (>18 years old)BothNormal details
Cellular CytoplasmDetected and Quantified88.7 uMAdult (>18 years old)BothNormal details
Abnormal Concentrations
BiospecimenStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified0.0036 uMInfant (0-1 year old)FemaleNicotinamide Adenine Dinucleotide Deficiency details
BloodDetected and Quantified29.1 (25.0-33.2) uMAdult (>18 years old)BothPellagra details
Associated Disorders and Diseases
Disease References
Pellagra
  1. Creeke PI, Dibari F, Cheung E, van den Briel T, Kyroussis E, Seal AJ: Whole blood NAD and NADP concentrations are not depressed in subjects with clinical pellagra. J Nutr. 2007 Sep;137(9):2013-7. [PubMed:17709435 ]
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 IDDB14128
Phenol Explorer Compound IDNot Available
FooDB IDFDB022309
KNApSAcK IDC00007256
Chemspider ID5682
KEGG Compound IDC00003
BioCyc IDNAD
BiGG IDNot Available
Wikipedia LinkNicotinamide_adenine_dinucleotide
METLIN IDNot Available
PubChem Compound5892
PDB IDNot Available
ChEBI ID44215
Food Biomarker OntologyNot Available
VMH IDNot Available
MarkerDB ID
References
Synthesis ReferenceHughes, N. A.; Kenner, G. W.; Todd, Alexander. Codehydrogenases. III. Synthesis of diphosphopyridine nucleotide (cozymase) and triphosphopyridine nucleotide. Journal of the Chemical Society (1957), 3733-8.
Material Safety Data Sheet (MSDS)Download (PDF)
General References
  1. Brautigam CA, Chuang JL, Tomchick DR, Machius M, Chuang DT: Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations. J Mol Biol. 2005 Jul 15;350(3):543-52. [PubMed:15946682 ]
  2. Ying W: NAD+ and NADH in cellular functions and cell death. Front Biosci. 2006 Sep 1;11:3129-48. [PubMed:16720381 ]
  3. Hamza A, Cho H, Tai HH, Zhan CG: Understanding human 15-hydroxyprostaglandin dehydrogenase binding with NAD+ and PGE2 by homology modeling, docking and molecular dynamics simulation. Bioorg Med Chem. 2005 Jul 15;13(14):4544-51. [PubMed:15908215 ]
  4. Begonja AJ, Gambaryan S, Geiger J, Aktas B, Pozgajova M, Nieswandt B, Walter U: Platelet NAD(P)H-oxidase-generated ROS production regulates alphaIIbbeta3-integrin activation independent of the NO/cGMP pathway. Blood. 2005 Oct 15;106(8):2757-60. Epub 2005 Jun 23. [PubMed:15976180 ]
  5. Bruzzone S, Moreschi I, Guida L, Usai C, Zocchi E, De Flora A: Extracellular NAD+ regulates intracellular calcium levels and induces activation of human granulocytes. Biochem J. 2006 Feb 1;393(Pt 3):697-704. [PubMed:16225456 ]
  6. Kim MY, Zhang T, Kraus WL: Poly(ADP-ribosyl)ation by PARP-1: 'PAR-laying' NAD+ into a nuclear signal. Genes Dev. 2005 Sep 1;19(17):1951-67. [PubMed:16140981 ]
  7. Kunsman GW, Manno JE, Cockerham KR, Manno BR: A modification and validation of two urine ethanol procedures for use with the Monarch 2000 Chemistry System. J Anal Toxicol. 1991 May-Jun;15(3):130-5. [PubMed:1943056 ]
  8. Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2:18. [PubMed:15882454 ]
  9. Orczyk J, Morre DM, Morre DJ: Periodic fluctuations in oxygen consumption comparing HeLa (cancer) and CHO (non-cancer) cells and response to external NAD(P)+/NAD(P)H. Mol Cell Biochem. 2005 May;273(1-2):161-7. [PubMed:16013451 ]
  10. 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 ]
  11. Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4. doi: 10.1038/nature07762. [PubMed:19212411 ]
  12. Elshenawy S, Pinney SE, Stuart T, Doulias PT, Zura G, Parry S, Elovitz MA, Bennett MJ, Bansal A, Strauss JF 3rd, Ischiropoulos H, Simmons RA: The Metabolomic Signature of the Placenta in Spontaneous Preterm Birth. Int J Mol Sci. 2020 Feb 4;21(3). pii: ijms21031043. doi: 10.3390/ijms21031043. [PubMed:32033212 ]

Only showing the first 10 proteins. There are 261 proteins in total.

Enzymes

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:
PDHB
Uniprot ID:
P11177
Molecular weight:
39233.1
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:
PDHA1
Uniprot ID:
P08559
Molecular weight:
43295.255
Reactions
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:
PDHA2
Uniprot ID:
P29803
Molecular weight:
42932.855
General function:
Involved in oxidoreductase activity
Specific function:
Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA.
Gene Name:
ALDH6A1
Uniprot ID:
Q02252
Molecular weight:
57839.31
Reactions
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:
DLD
Uniprot ID:
P09622
Molecular weight:
54176.91
Reactions
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:
DLAT
Uniprot ID:
P10515
Molecular weight:
68996.03
Reactions
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:
AKR1C4
Uniprot ID:
P17516
Molecular weight:
37094.57
Reactions
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:
HPGD
Uniprot ID:
P15428
Molecular weight:
28977.105
Reactions
(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:
TYR
Uniprot ID:
P14679
Molecular weight:
60392.69
Reactions
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:
AKR1B1
Uniprot ID:
P15121
Molecular weight:
35853.125
Reactions
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 261 proteins in total.