| Record Information |
| Version |
3.5 |
| Creation Date |
2005-11-16 08:48:42 -0700 |
| Update Date |
2013-05-15 14:41:54 -0600 |
| HMDB ID |
HMDB01487 |
| Secondary Accession Numbers |
None |
| Metabolite Identification |
| Common Name |
NADH |
| Description |
NADH 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). |
| Structure |
Download:
MOL |
SDF |
SMILES |
InChI
Display:
2D Structure |
3D Structure
|
| Synonyms |
- 1,4-Dihydronicotinamide adenine dinucleotide
- b-DPNH
- b-NADH
- beta-DPNH
- beta-NADH
- Dihydrocodehydrogenase I
- Dihydrocozymase
- Dihydronicotinamide adenine dinucleotide
- Dihydronicotinamide mononucleotide
- DPNH
- ENADA
- NADH
- NADH2
- Reduced codehydrogenase I
- Reduced diphosphopyridine nucleotide
- Reduced nicotinamide adenine diphosphate
- Reduced nicotinamide-adenine dinucleotide
|
| Chemical Formula |
C21H29N7O14P2 |
| Average Molecular Weight |
665.441 |
| Monoisotopic Molecular Weight |
665.124771695 |
| IUPAC Name |
{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}[({[(2R,3S,4R,5R)-5-(3-carbamoyl-1,4-dihydropyridin-1-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy]phosphinic acid |
| Traditional IUPAC Name |
[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy({[(2R,3S,4R,5R)-5-(3-carbamoyl-4H-pyridin-1-yl)-3,4-dihydroxyoxolan-2-yl]methoxy(hydroxy)phosphoryl}oxy)phosphinic acid |
| CAS Registry Number |
58-68-4 |
| SMILES |
NC(=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]1O |
| InChI Identifier |
InChI=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/s1 |
| InChI Key |
BOPGDPNILDQYTO-NNYOXOHSSA-N |
| Chemical Taxonomy |
| Kingdom |
Organic Compounds |
| Super Class |
Nucleosides, Nucleotides, and Analogues |
| Class |
Purine Nucleotides |
| Sub Class |
Purine Ribonucleotides |
| Other Descriptors |
- Aromatic Heteropolycyclic Compounds
|
| Substituents |
- 1,2 Diol
- 1 Phosphoribosyl Imidazole
- Aminopyrimidine
- Carboxamide Group
- Dihydropyridine
- Disaccharide Phosphate
- Enamine
- Glycosyl Compound
- Hemiaminal
- Hydropyridine
- Imidazole
- Imidazopyrimidine
- N Glycosyl Compound
- Nicotinamide Nucleotide
- Organic Hypophosphite
- Organic Phosphite
- Organic Pyrophosphate
- Oxolane
- Pentose Disaccharide
- Phosphoric Acid Ester
- Primary Carboxylic Acid Amide
- Purine
- Pyrimidine
- Saccharide
- Secondary Alcohol
|
| Direct Parent |
Purine Ribonucleoside Diphosphates |
| Ontology |
| Status |
Detected and Quantified |
| Origin |
|
| Biofunction |
- Component of Aminosugars metabolism
- Component of Arginine and proline metabolism
- Component of Ascorbate and aldarate metabolism
- Component of Bile acid biosynthesis
- Component of Butanoate metabolism
- Component of Cysteine metabolism
- Component of Fatty acid metabolism
- Component of Fructose and mannose metabolism
- Component of Glutamate metabolism
- Component of Glycerolipid metabolism
- Component of Glycerophospholipid metabolism
- Component of Glycine, serine and threonine metabolism
- Component of Glyoxylate and dicarboxylate metabolism
- Component of Histidine metabolism
- Component of Inositol metabolism
- Component of Methane metabolism
- Component of Nicotinate and nicotinamide metabolism
- Component of Nucleotide sugars metabolism
- Component of Propanoate metabolism
- Component of Purine metabolism
- Component of Pyruvate metabolism
- Component of Retinol metabolism
- Component of Starch and sucrose metabolism
- Component of Tryptophan metabolism
- Component of Tyrosine metabolism
- Component of Ubiquinone biosynthesis
- Component of beta-Alanine metabolism
|
| Application |
Not Available |
| Cellular locations |
- Mitochondria
- Endoplasmic reticulum
- Peroxisome
|
| Physical Properties |
| State |
Solid |
| Experimental Properties |
| Property |
Value |
Reference |
| Melting Point |
140.0 - 142.0 °C |
Not Available |
| Boiling Point |
Not Available |
Not Available |
| Water Solubility |
Not Available |
Not Available |
| LogP |
Not Available |
Not Available |
|
| Predicted Properties |
|
| Spectra |
|
Not Available
|
| Biological Properties |
| Cellular Locations |
- Mitochondria
- Endoplasmic reticulum
- Peroxisome
|
| Biofluid Locations |
|
| Tissue Location |
- Muscle
- Bladder
- Fibroblasts
- Brain
- Platelet
|
| Pathways |
|
| Normal Concentrations |
|
| Blood |
Detected and Quantified |
|
22.0 (14.0-40.0) uM |
Adult (>18 years old) |
Both |
Normal |
Not Available |
|
| Abnormal Concentrations |
|
Not Available |
| Associated Disorders and Diseases |
| Disease References |
None |
| Associated OMIM IDs |
None |
| External Links |
| DrugBank ID |
Not Available |
| Phenol Explorer Compound ID |
Not Available |
| Phenol Explorer Metabolite ID |
Not Available |
| FoodDB ID |
FDB022649 |
| KNApSAcK ID |
Not Available |
| Chemspider ID |
903  |
| KEGG Compound ID |
C00004  |
| BioCyc ID |
NADH  |
| BiGG ID |
33484  |
| Wikipedia Link |
NADH  |
| NuGOwiki Link |
HMDB01487  |
| Metagene Link |
HMDB01487  |
| METLIN ID |
3687  |
| PubChem Compound |
928  |
| PDB ID |
Not Available |
| ChEBI ID |
16908  |
| References |
| Synthesis Reference |
Marek, 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 |
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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. 2000 Dec;89(6):2352-8.
Pubmed: 11090589
- 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
- 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
- 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
- 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
- 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
- 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
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| Enzymes |
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| Name: |
Tyrosinase
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| Reactions: |
- L-tyrosine + L-dopa + O2 = L-dopa + dopaquinone + H2O [RN:R02078]
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| Gene Name: |
TYR |
| Uniprot ID: |
P14679  |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
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| Name: |
Aldose reductase
|
| Reactions: |
- alditol + NAD(P)+ = aldose + NAD(P)H + H+ [RN:R02819 R02820]
|
| Gene Name: |
AKR1B1 |
| Uniprot ID: |
P15121  |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
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| Name: |
Lathosterol oxidase
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| Reactions: |
- 5alpha-cholest-7-en-3beta-ol + NAD(P)H + H+ + O2 = cholesta-5,7-dien-3beta-ol + NAD(P)+ + 2 H2O [RN:R03310 R07215]
|
| Gene Name: |
SC5DL |
| Uniprot ID: |
O75845  |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
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| Name: |
C-4 methylsterol oxidase
|
| Reactions: |
- (1) (1a) 4,4-dimethyl-5alpha-cholest-7-en-3beta-ol + NAD(P)H + H+ + O2 = 4beta-hydroxymethyl-4alpha-methyl-5alpha-cholest-7-en-3beta-ol + NAD(P)+ + H2O [RN:R04501 R05736]
- (2) (1b) 4beta-hydroxymethyl-4alpha-methyl-5alpha-cholest-7-en-3beta-ol + NAD(P)H + H+ + O2 = 3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde + NAD(P)+ + 2 H2O [RN:R05733 R05737]
- (3) (1c) 3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde + NAD(P)H + H+ + O2 = 3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate + NAD(P)+ + H2O [RN:R05734 R05738]
|
| Gene Name: |
SC4MOL |
| Uniprot ID: |
Q15800  |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
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| Name: |
Cytochrome P450 4A11
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| Reactions: |
- octane + reduced rubredoxin + O2 = 1-octanol + oxidized rubredoxin + H2O [RN:R02879]
|
| Gene Name: |
CYP4A11 |
| Uniprot ID: |
Q02928  |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
|
| Name: |
2-oxoglutarate dehydrogenase, mitochondrial
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| Reactions: |
- 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2 [RN:R01700]
|
| Gene Name: |
OGDH |
| Uniprot ID: |
Q02218  |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
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| Name: |
Peroxisomal multifunctional enzyme type 2
|
| Reactions: |
- (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl- CoA = (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA + H2O [RN:R04813]
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| Gene Name: |
HSD17B4 |
| Uniprot ID: |
P51659  |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
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| Name: |
Aminomethyltransferase, mitochondrial
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| Reactions: |
- [protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3 [RN:R04125]
|
| Gene Name: |
AMT |
| Uniprot ID: |
P48728  |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
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| Name: |
Flavin reductase
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| Reactions: |
- reduced riboflavin + NADP+ = riboflavin + NADPH + H+ [RN:R05707]
|
| Gene Name: |
BLVRB |
| Uniprot ID: |
P30043  |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
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| Name: |
3-keto-steroid reductase
|
| Reactions: |
- 4alpha-methyl-5alpha-cholest-7-en-3beta-ol + NADP+ = 4alpha-methyl-5alpha-cholest-7-en-3-one + NADPH + H+ [RN:R05691]
|
| Gene Name: |
HSD17B7 |
| Uniprot ID: |
P56937  |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
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| Name: |
Tankyrase-2
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| Reactions: |
- NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ [RN:R04176]
|
| Gene Name: |
TNKS2 |
| Uniprot ID: |
Q9H2K2  |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
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| Name: |
Tankyrase-1
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| Reactions: |
- NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+ [RN:R04176]
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| Gene Name: |
TNKS |
| Uniprot ID: |
O95271  |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
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| Name: |
Urocanate hydratase
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| Reactions: |
- 3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate = urocanate + H2O [RN:R02914]
|
| Gene Name: |
UROC1 |
| Uniprot ID: |
Q96N76  |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
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| Name: |
NAD kinase
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| Reactions: |
- ATP + NAD+ = ADP + NADP+ [RN:R00104]
|
| Gene Name: |
NADK |
| Uniprot ID: |
O95544  |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
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| Name: |
D-3-phosphoglycerate dehydrogenase
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| Reactions: |
- (1) 3-phospho-D-glycerate + NAD+ = 3-phosphonooxypyruvate + NADH + H+ [RN:R01513]
- (2) 2-hydroxyglutarate + NAD+ = 2-oxoglutarate + NADH + H+ [RN:R08198]
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| Gene Name: |
PHGDH |
| Uniprot ID: |
O43175  |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
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| Name: |
Cytochrome P450 4A22
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| Reactions: |
- octane + reduced rubredoxin + O2 = 1-octanol + oxidized rubredoxin + H2O [RN:R02879]
|
| Gene Name: |
CYP4A22 |
| Uniprot ID: |
Q5TCH4  |
| Protein Sequence: |
FASTA |
| Gene Sequence: |
FASTA |
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