| Identification | |||||||||||||||||||||||||||||||||||||||||||
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| Name | Nicotinamide-Adenine-Dinucleotide | ||||||||||||||||||||||||||||||||||||||||||
| Accession Number | DB01907 (DB03527, EXPT02287) | ||||||||||||||||||||||||||||||||||||||||||
| Type | small molecule | ||||||||||||||||||||||||||||||||||||||||||
| Groups | experimental | ||||||||||||||||||||||||||||||||||||||||||
| Description | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Structure |
Download: MOL | SDF | SMILES | InChI Display: 2D Structure | 3D Structure |
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| Synonyms | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Salts | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Brand names | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Brand mixtures | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Categories | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| CAS number | 53-84-9 | ||||||||||||||||||||||||||||||||||||||||||
| Weight |
Average: 663.4251 Monoisotopic: 663.109121631 |
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| Chemical Formula | C21H27N7O14P2 | ||||||||||||||||||||||||||||||||||||||||||
| InChI Key | InChIKey=BAWFJGJZGIEFAR-DQQFMEOOSA-N | ||||||||||||||||||||||||||||||||||||||||||
| InChI |
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+/m0/s1
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| IUPAC Name |
1-[(2S,3S,4R,5S)-5-({[(S)-({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl phosphonato)]oxy}methyl)-3,4-dihydroxyoxolan-2-yl]-3-carbamoyl-1$l^{5}-pyridin-1-ylium
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| SMILES |
NC(=O)C1=CC=C[N+](=C1)[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=C2N=CN=C3N)[C@H](O)[C@@H]1O
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| Mass Spec | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Taxonomy | |||||||||||||||||||||||||||||||||||||||||||
| Kingdom | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Classes | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Substructures | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pharmacology | |||||||||||||||||||||||||||||||||||||||||||
| Indication | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pharmacodynamics | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Mechanism of action | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Absorption | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Volume of distribution | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Protein binding | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Metabolism | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Route of elimination | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Half life | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Clearance | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Toxicity | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Affected organisms | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pathways | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pharmacoeconomics | |||||||||||||||||||||||||||||||||||||||||||
| Manufacturers | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Packagers | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Dosage forms | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Prices | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Patents | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Properties | |||||||||||||||||||||||||||||||||||||||||||
| State | solid | ||||||||||||||||||||||||||||||||||||||||||
| Experimental Properties | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Predicted Properties |
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| References | |||||||||||||||||||||||||||||||||||||||||||
| Synthesis Reference | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| General Reference | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| External Links |
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| ATC Codes | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| AHFS Codes | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| PDB Entries | |||||||||||||||||||||||||||||||||||||||||||
| FDA label | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| MSDS | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Interactions | |||||||||||||||||||||||||||||||||||||||||||
| Drug Interactions | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Food Interactions | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Targets |
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1. dTDP-4-dehydrorhamnose reductase Pharmacological action: unknowndTDP-6-deoxy-L-mannose + NADP(+) = dTDP-4- dehydro-6-deoxy-L-mannose + NADPH Organism class: bacterialUniProt ID: P26392 ![]() Gene: rfbD Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
UDP-glucose = UDP-galactose Organism class: bacterialUniProt ID: P09147 ![]() Gene: galE Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 3. GDP-mannose 6-dehydrogenase Pharmacological action: unknownCatalyzes the oxidation of guanosine diphospho-D-mannose (GDP-D-mannose) to GDP-D-mannuronic acid, a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics Organism class: bacterialUniProt ID: P11759 ![]() Gene: algD Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 4. Dihydrodipicolinate reductase Pharmacological action: unknown2,3,4,5-tetrahydrodipicolinate + NAD(P)(+) = 2,3-dihydrodipicolinate + NAD(P)H Organism class: bacterialUniProt ID: P72024 ![]() Gene: dapB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 5. NH(3)-dependent NAD(+) synthetase Pharmacological action: unknownCatalyzes a key step in NAD biosynthesis, transforming deamido-NAD into NAD by a two-step reaction Organism class: bacterialUniProt ID: P08164 ![]() Gene: nadE Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Catalyzes the reversible oxidation of malate to oxaloacetate Organism class: bacterialUniProt ID: Q9ZF99 ![]() Gene: mdh Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 7. D-2-hydroxyisocaproate dehydrogenase Pharmacological action: unknownCatalyzes the NAD dependent reversible, stereospecific interconversion between 2-ketocarboxylic acids and D-2-hydroxy- carboxylic acids Organism class: bacterialUniProt ID: P17584 ![]() Protein Sequence: FASTA Gene Sequence: FASTA References:
Pharmacological action: unknown
Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine Organism class: bacterialUniProt ID: P06988 ![]() Gene: hisD Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Catalyzes the isomeration of CDP-paratose to CDP- tyvelose Organism class: bacterialUniProt ID: P14169 ![]() Gene: rfbE Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 10. NADP-dependent malic enzyme, mitochondrial Pharmacological action: unknownOrganism class: human UniProt ID: Q16798 ![]() Gene: ME3 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Adenosylhomocysteine is a competitive inhibitor of S- adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine Organism class: humanUniProt ID: P23526 ![]() Gene: AHCY ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
12. dTDP-glucose 4,6-dehydratase Pharmacological action: unknowndTDP-glucose = dTDP-4-dehydro-6-deoxy-D- glucose + H(2)O Organism class: bacterialUniProt ID: P26391 ![]() Gene: rfbB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 13. 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase Pharmacological action: unknownAndrostan-3-alpha,17-beta-diol + NAD(+) = 17- beta-hydroxyandrostan-3-one + NADH Organism class: bacterialUniProt ID: P69167 ![]() Gene: fabG3 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 14. Gamma-aminobutyraldehyde dehydrogenase Pharmacological action: unknownCatalyzes the oxidation of 1-pyrroline, which is spontaneously formed from 4-aminobutanal, leading to 4- aminobutanoate (GABA). Can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency Organism class: bacterialUniProt ID: P77674 ![]() Gene: prr Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
(R)-lactate + NAD(+) = pyruvate + NADH Organism class: bacterialUniProt ID: P30901 ![]() Protein Sequence: FASTA Gene Sequence: FASTA References:
Pharmacological action: unknown
3-deoxy-arabino-heptulonate 7-phosphate = 3- dehydroquinate + phosphate Organism class: bacterialUniProt ID: Q6GGU4 ![]() Gene: aroB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 17. AGR_L_3209p Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q7CRW4 ![]() Gene: AGR_L_3209 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 18. Dihydrodipicolinate reductase Pharmacological action: unknown2,3,4,5-tetrahydrodipicolinate + NAD(P)(+) = 2,3-dihydrodipicolinate + NAD(P)H Organism class: bacterialUniProt ID: P04036 ![]() Gene: dapB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 19. Glutamate dehydrogenase 1, mitochondrial Pharmacological action: unknownMay be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate Organism class: humanUniProt ID: P00367 ![]() Gene: GLUD1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Catalyzes the reversible oxidation of malate to oxaloacetate Organism class: bacterialUniProt ID: P80039 ![]() Gene: mdh Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Binds free retinal and cellular retinol-binding protein- bound retinal. Can convert/oxidize retinaldehyde to retinoic acid Organism class: humanUniProt ID: P00352 ![]() Gene: ALDH1A1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: human UniProt ID: P08319 ![]() Gene: ADH4 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor Organism class: humanUniProt ID: P53004 ![]() Gene: BLVRA ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
24. Nicotinamide mononucleotide adenylyltransferase 3 Pharmacological action: unknownATP + nicotinamide ribonucleotide = diphosphate + NAD(+) Organism class: humanUniProt ID: Q96T66 ![]() Gene: NMNAT3 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Catalyzes the regio- and stereoselective reversible NAD- dependent reduction of (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) to (4R,6R)-4-hydroxy-2,2,6-trimethylcyclohexanone (actinol) Organism class: bacterialUniProt ID: Q9LBG2 ![]() Gene: lvr Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 26. Enoyl-[acyl-carrier-protein] reductase [NADH] Pharmacological action: unknownAcyl-[acyl-carrier-protein] + NAD(+) = trans- 2,3-dehydroacyl-[acyl-carrier-protein] + NADH Organism class: bacterialUniProt ID: O24990 ![]() Gene: fabI Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Adenosylhomocysteine is a competitive inhibitor of S- adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine (By similarity) Organism class: parasiticUniProt ID: P50250 ![]() Gene: PFE1050w Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 28. L-lactate dehydrogenase A chain Pharmacological action: unknownOrganism class: human UniProt ID: P00338 ![]() Gene: LDHA ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
29. Nicotinamide mononucleotide adenylyltransferase 1 Pharmacological action: unknownATP + nicotinamide ribonucleotide = diphosphate + NAD(+) Organism class: humanUniProt ID: Q9HAN9 ![]() Gene: NMNAT1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 30. 3-hydroxy-3-methylglutaryl-coenzyme A reductase Pharmacological action: unknownP.mevalonii can use mevalonate as sole carbon source. With this enzyme mevalonate is deacetylated to HMG-CoA Organism class: bacterialUniProt ID: P13702 ![]() Gene: mvaA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 31. Dehydrogenase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q746L8 ![]() Gene: TT_P0035 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 32. Glyceraldehyde-3-phosphate dehydrogenase Pharmacological action: unknownD-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH Organism class: bacterialUniProt ID: P17721 ![]() Gene: gap Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 33. TDP-glucose-4,6-dehydratase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9ZGH3 ![]() Gene: desIV Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 34. Redox-sensing transcriptional repressor rex Pharmacological action: unknownModulates transcription in response to changes in cellular NADH/NAD(+) redox state (By similarity) Organism class: bacterialUniProt ID: Q9X2V5 ![]() Gene: rex Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 35. Glutamate dehydrogenase 2, mitochondrial Pharmacological action: unknownImportant for recycling the chief excitatory neurotransmitter, glutamate, during neurotransmission Organism class: humanUniProt ID: P49448 ![]() Gene: GLUD2 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
36. 2,4-dienoyl-CoA reductase, mitochondrial Pharmacological action: unknownAuxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3- enoyl-CoA Organism class: humanUniProt ID: Q16698 ![]() Gene: DECR1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
37. Dihydrolipoyl dehydrogenase, mitochondrial Pharmacological action: unknownLipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes Organism class: humanUniProt ID: P09622 ![]() Gene: DLD ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. Does not show aspartate oxidase activity. Is also able to catalyze the reverse reaction, i.e. the reductive amination of oxaloacetate Organism class: bacterialUniProt ID: Q9X1X6 ![]() Gene: nadX Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 39. Glyceraldehyde 3-phosphate dehydrogenase Pharmacological action: unknownOrganism class: bacterial UniProt ID: P84125 ![]() Gene: tthHB8IM Protein Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
(S)-lactate + NAD(+) = pyruvate + NADH Organism class: bacterialUniProt ID: P56511 ![]() Gene: ldh Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Catalyzes the reversible oxidation of malate to oxaloacetate Organism class: bacterialUniProt ID: P10584 ![]() Gene: mdh Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Organism class: bacterial UniProt ID: Q52437 ![]() Gene: bphA4 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 43. NADH peroxidase Pharmacological action: unknownPeroxidase whose active site is a redox-active cysteine- sulfenic acid Organism class: bacterialUniProt ID: P37062 ![]() Gene: npr Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
(S)-lactate + NAD(+) = pyruvate + NADH Organism class: bacterialUniProt ID: P00344 ![]() Gene: ldh Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 45. Quinate/shikimate dehydrogenase Pharmacological action: unknownThe physiological substrate is not known Organism class: bacterialUniProt ID: P0A6D5 ![]() Gene: ydiB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 46. Glyceraldehyde-3-phosphate dehydrogenase, testis-specific Pharmacological action: unknownMay play an important role in regulating the switch between different pathways for energy production during spermiogenesis and in the spermatozoon. Required for sperm motility and male fertility Organism class: humanUniProt ID: O14556 ![]() Gene: GAPDHS ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
47. Aldehyde dehydrogenase, dimeric NADP-preferring Pharmacological action: unknownALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. This protein preferentially oxidizes aromatic aldehyde substrates. It may play a role in the oxidation of toxic aldehydes Organism class: humanUniProt ID: P30838 ![]() Gene: ALDH3A1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
48. 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9ZFY9 ![]() Protein Sequence: FASTA Gene Sequence: FASTA
Pharmacological action: unknown
Organism class: bacterial UniProt ID: O07615 ![]() Gene: yhfP Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 50. L-2-hydroxyisocaproate dehydrogenase Pharmacological action: unknownCatalyzes the NADP dependent reversible and stereospecific interconversion between 2-ketocarboxylic acids and L-2-hydroxy-carboxylic acids. 2-ketoacids with medium chain length (five to six C-atoms) are the best substrates Organism class: bacterialUniProt ID: P14295 ![]() Protein Sequence: FASTA Gene Sequence: FASTA
Pharmacological action: unknown
Organism class: bacterial UniProt ID: Q9ADS9 ![]() Protein Sequence: FASTA Gene Sequence: FASTA
Pharmacological action: unknown
Organism class: bacterial UniProt ID: Q46220 ![]() Protein Sequence: FASTA Gene Sequence: FASTA 53. Vip2Ac Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q844J9 ![]() Gene: vip2Ac Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 54. Glyceraldehyde-3-phosphate dehydrogenase Pharmacological action: unknownD-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH Organism class: bacterialUniProt ID: P00362 ![]() Gene: gap Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Glycerol + NAD(+) = glycerone + NADH Organism class: bacterialUniProt ID: P32816 ![]() Gene: gldA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 56. Inorganic polyphosphate/ATP-NAD kinase Pharmacological action: unknownCatalyzes the phosphorylation of NAD to NADP. Utilizes ATP and other nucleoside triphosphates as well as inorganic polyphosphate as a source of phosphorus Organism class: bacterialUniProt ID: P0A5S6 ![]() Gene: ppnK Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 57. Alcohol dehydrogenase [NADP+] Pharmacological action: unknownCatalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. In vitro substrates include succinic semialdehyde, 4- nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D- glucuronic acid. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs, including the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN) Organism class: humanUniProt ID: P14550 ![]() Gene: AKR1A1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
58. D-3-phosphoglycerate dehydrogenase Pharmacological action: unknown3-phospho-D-glycerate + NAD(+) = 3- phosphonooxypyruvate + NADH Organism class: bacterialUniProt ID: P0A9T0 ![]() Gene: serA Protein Sequence: FASTA SNPs: SNPJam Report ![]() References: 59. Citrate synthase Pharmacological action: unknownAcetyl-CoA + H(2)O + oxaloacetate = citrate + CoA Organism class: bacterialUniProt ID: P0ABH7 ![]() Gene: gltA Protein Sequence: FASTA SNPs: SNPJam Report ![]() References: 60. Glyceraldehyde-3-phosphate dehydrogenase A Pharmacological action: unknownD-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH Organism class: bacterialUniProt ID: P0A9B2 ![]() Gene: gapA Protein Sequence: FASTA SNPs: SNPJam Report ![]() References: 61. NAD(P) transhydrogenase subunit alpha part 1 Pharmacological action: unknownThe transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane Organism class: bacterialUniProt ID: P0C186 ![]() Gene: pntAA Protein Sequence: FASTA SNPs: SNPJam Report ![]() References: 62. Dihydrodipicolinate reductase Pharmacological action: unknown2,3,4,5-tetrahydrodipicolinate + NAD(P)(+) = 2,3-dihydrodipicolinate + NAD(P)H Organism class: bacterialUniProt ID: Q9X1K8 ![]() Gene: dapB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 63. Glutathione-independent formaldehyde dehydrogenase Pharmacological action: unknownCatalyzes the oxidation of long-chain alcohols but is inactive against ethanol Organism class: bacterialUniProt ID: P46154 ![]() Gene: fdhA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 64. Alpha-glucosidase, putative Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9WZL1 ![]() Gene: TM_0752 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Alpha-glycosidase with a very broad specificity. Hydrolyzes maltose and other small maltooligosaccharides but is inactive against the polymeric substrate starch. AglA is not specific with respect to the configuration at the C-4 position of its substrates because glycosidic derivatives of D-galactose are also hydrolyzed. Does not cleave beta-glycosidic bonds Organism class: bacterialUniProt ID: O33830 ![]() Gene: aglA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 66. Nicotinate-nucleotide adenylyltransferase Pharmacological action: unknownCatalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD) (By similarity) Organism class: bacterialUniProt ID: P0A753 ![]() Gene: nadD Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 67. CDP-D-glucose-4,6-dehydratase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q57329 ![]() Gene: ascB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Beta-D-glucose + NAD(P)(+) = D-glucono-1,5- lactone + NAD(P)H Organism class: bacterialUniProt ID: P40288 ![]() Protein Sequence: FASTA Gene Sequence: FASTA 69. 4-trimethylaminobutyraldehyde dehydrogenase Pharmacological action: unknownConverts gamma-trimethylaminobutyraldehyde into gamma- butyrobetaine. Catalyzes the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction Organism class: humanUniProt ID: P49189 ![]() Gene: ALDH9A1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
70. Hypothetical protein Rv0046c/MT0052 Pharmacological action: unknownOrganism class: bacterial UniProt ID: P71703 ![]() Gene: ino1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Organism class: bacterial UniProt ID: O08355 ![]() Gene: mtlD Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 72. Dihydrolipoyl dehydrogenase Pharmacological action: unknownThe branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components:branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) Organism class: bacterialUniProt ID: P09063 ![]() Gene: lpdV Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 73. Malate dehydrogenase, cytoplasmic Pharmacological action: unknownOrganism class: human UniProt ID: P40925 ![]() Gene: MDH1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Does metabolize octanal and decanal but does not metabolize citral, benzaldehyde, acetaldehyde and propanal efficiently Organism class: humanUniProt ID: O94788 ![]() Gene: ALDH1A2 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: parasitic UniProt ID: Q8T8E9 ![]() Gene: galE Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 76. 2,5-diketo-D-gluconic acid reductase A Pharmacological action: unknownCatalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates. 25DKGR-A exhibits a greater selectivity for the substrate and higher thermal stability than 25DKGR-B Organism class: bacterialUniProt ID: P06632 ![]() Gene: dkgA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 77. Phenol 2-hydroxylase component B Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9LAG2 ![]() Gene: pheA2 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 78. Transcriptional regulator nadR Pharmacological action: unknownNadR is bifunctional; it interacts with pnuC at low internal NAD levels, permitting transport of NMN intact into the cell. As NAD levels increase within the cell, the affinity of nadR for the operator regions of some genes increases, repressing the transcription of these genes (By similarity) Organism class: bacterialUniProt ID: P44308 ![]() Gene: nadR Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 79. NADH-cytochrome b5 reductase 3 Pharmacological action: unknownDesaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction Organism class: humanUniProt ID: P00387 ![]() Gene: CYB5R3 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
80. Glyceraldehyde-3-phosphate dehydrogenase Pharmacological action: unknownD-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH Organism class: bacterialUniProt ID: P00361 ![]() Gene: gap Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
NAD(+) + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + nicotinamide nucleotide + (deoxyribonucleotide)(n+m) Organism class: bacterialUniProt ID: Q837V6 ![]() Gene: ligA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 82. 3-oxoacyl-(Acyl carrier protein) reductase Pharmacological action: unknownAcyl-[acyl-carrier-protein] + NAD(+) = trans- 2,3-dehydroacyl-[acyl-carrier-protein] + NADH Organism class: bacterialUniProt ID: Q9X0Q1 ![]() Gene: TM_1169 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 83. C-terminal-binding protein 1 Pharmacological action: unknownInvolved in controlling the equilibrium between tubular and stacked structures in the Golgi complex (By similarity). Co- repressor targeting diverse transcription regulators such as GLIS2. Has dehydrogenase activity Organism class: humanUniProt ID: Q13363 ![]() Gene: CTBP1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
84. Benzyl alcohol dehydrogenase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q59096 ![]() Gene: xylB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Organism class: bacterial UniProt ID: Q88H32 ![]() Gene: PP3533 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 86. dTDP-glucose 4,6-dehydratase Pharmacological action: unknowndTDP-glucose = dTDP-4-dehydro-6-deoxy-D- glucose + H(2)O Organism class: bacterialUniProt ID: P95780 ![]() Gene: rmlB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
(S)-lactate + NAD(+) = pyruvate + NADH Organism class: bacterialUniProt ID: P19869 ![]() Gene: ldh2 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Multifunctional enzyme that catalyze the SAM-dependent methylation of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 and then position C-12 or C-18 to form trimethylpyrrocorphin 2. It also catalyzes the conversion of precorrin-2 into siroheme. This reaction consist of the NAD- dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme Organism class: bacterialUniProt ID: P25924 ![]() Gene: cysG Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Formate + NAD(+) = CO(2) + NADH Organism class: bacterialUniProt ID: P33160 ![]() Protein Sequence: FASTA 90. NADPH-flavin oxidoreductase Pharmacological action: unknownInvolved in bioluminescence. It is a good supplier of reduced flavin mononucleotide (FMNH2) to the bioluminescence reaction Organism class: bacterialUniProt ID: Q56691 ![]() Gene: frp Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 91. WbpP Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q8KN66 ![]() Protein Sequence: FASTA Gene Sequence: FASTA 92. Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase Pharmacological action: unknownCis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD(+) = biphenyl-2,3-diol + NADH Organism class: bacterialUniProt ID: P47227 ![]() Gene: bphB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 93. Myo-inositol-1-phosphate synthase-related protein Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9X1D6 ![]() Gene: TM_1419 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Organism class: bacterial UniProt ID: O52942 ![]() Gene: ald Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Organism class: bacterial UniProt ID: Q9HTD9 ![]() Gene: adhA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 96. Acetoin(diacetyl) reductase Pharmacological action: unknownCatalyzes the reversible reduction of acetoin to 2,3- butanediol in the presence of NADH Organism class: bacterialUniProt ID: Q48436 ![]() Gene: budC Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
(R)-lactate + NAD(+) = pyruvate + NADH Organism class: bacterialUniProt ID: P26297 ![]() Gene: ldhA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 98. UDP-glucose 6-dehydrogenase Pharmacological action: unknownCatalyzes the formation of UDP-glucuronic acid which is required for capsular hyaluronic acid synthesis Organism class: bacterialUniProt ID: P0C0F4 ![]() Gene: hasB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 99. Enoyl-[acyl-carrier-protein] reductase [NADH] Pharmacological action: unknownAcyl-[acyl-carrier-protein] + NAD(+) = trans- 2,3-dehydroacyl-[acyl-carrier-protein] + NADH Organism class: bacterialUniProt ID: P0AEK4 ![]() Gene: fabI Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 100. 7-alpha-hydroxysteroid dehydrogenase Pharmacological action: unknown7-alpha-dehydroxylation of cholic acid, yielding deoxycholic acid and lithocholic acid, respectively. Highest affinity with taurochenodeoxycholic acid Organism class: bacterialUniProt ID: P0AET8 ![]() Gene: hdhA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 101. 3-isopropylmalate dehydrogenase Pharmacological action: unknownCatalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate Organism class: bacterialUniProt ID: Q5SIY4 ![]() Gene: leuB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: human UniProt ID: P00326 ![]() Gene: ADH1C ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
103. NH(3)-dependent NAD(+) synthetase Pharmacological action: unknownCatalyzes a key step in NAD biosynthesis, transforming deamido-NAD into NAD by a two-step reaction Organism class: bacterialUniProt ID: P18843 ![]() Gene: nadE Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
(S)-lactate + NAD(+) = pyruvate + NADH Organism class: bacterialUniProt ID: P16115 ![]() Gene: ldh Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 105. Inositol-3-phosphate synthase 1 Pharmacological action: unknownOrganism class: human UniProt ID: Q9NPH2 ![]() Gene: ISYNA1 SNPs: SNPJam Report ![]() References:
106. Glyceraldehyde-3-phosphate dehydrogenase Pharmacological action: unknownOrganism class: human UniProt ID: P04406 ![]() Gene: GAPDH ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: human UniProt ID: P00325 ![]() Gene: ADH1B ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: human UniProt ID: Q00796 ![]() Gene: SORD ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 109. Enoyl-[acyl-carrier-protein] reductase [NADH] Pharmacological action: unknownInvolved in the resistance against the antituberculosis drugs isoniazid and ethionamide Organism class: bacterialUniProt ID: P0A5Y6 ![]() Gene: inhA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 110. Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial Pharmacological action: unknownPlays an essential role in the mitochondrial beta- oxidation of short chain fatty acids. Exerts it highest activity toward 3-hydroxybutyryl-CoA Organism class: humanUniProt ID: Q16836 ![]() Gene: HADH ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
(S)-lactate + NAD(+) = pyruvate + NADH Organism class: parasiticUniProt ID: Q27743 ![]() Protein Sequence: FASTA Gene Sequence: FASTA References:
Pharmacological action: unknown
Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue Organism class: humanUniProt ID: P49366 ![]() Gene: DHPS ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 113. Inosine-5'-monophosphate dehydrogenase 2 Pharmacological action: unknownRate limiting enzyme in the de novo synthesis of guanine nucleotides and therefore is involved in the regulation of cell growth. It may also have a role in the development of malignancy and the growth progression of some tumors Organism class: humanUniProt ID: P12268 ![]() Gene: IMPDH2 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 114. Nitric oxide synthase oxygenase Pharmacological action: unknownCatalyzes the production of nitric oxide Organism class: bacterialUniProt ID: P0A094 ![]() Gene: nos Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Catalyzes two distinct but analogous reactions:the epimerization of UDP-glucose to UDP-galactose and the epimerization of UDP-N-acetylglucosamine to UDP-N- acetylgalactosamine Organism class: humanUniProt ID: Q14376 ![]() Gene: GALE ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Maintains high levels of reduced glutathione in the cytosol Organism class: bacterialUniProt ID: P06715 ![]() Gene: gor Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 117. Alcohol dehydrogenase class 3 Pharmacological action: unknownClass-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione Organism class: humanUniProt ID: P11766 ![]() Gene: ADH5 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
118. Glutathione reductase, mitochondrial Pharmacological action: unknownMaintains high levels of reduced glutathione in the cytosol Organism class: humanUniProt ID: P00390 ![]() Gene: GSR ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 119. Isocitrate dehydrogenase [NADP] Pharmacological action: unknownIsocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH Organism class: bacterialUniProt ID: P08200 ![]() Gene: icd Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 120. Malate dehydrogenase Pharmacological action: unknownCatalyzes the reversible oxidation of malate to oxaloacetate Organism class: bacterialUniProt ID: P80040 ![]() Gene: mdh Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 121. Peroxisomal multifunctional enzyme type 2 Pharmacological action: unknownBifunctional enzyme acting on the peroxisomal beta- oxidation pathway for fatty acids. Catalyzes the formation of 3- ketoacyl-CoA intermediates from both straight-chain and 2-methyl- branched-chain fatty acids Organism class: humanUniProt ID: P51659 ![]() Gene: HSD17B4 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 122. Urocanate hydratase Pharmacological action: unknown3-(5-oxo-4,5-dihydro-3H-imidazol-4- yl)propanoate = urocanate + H(2)O Organism class: bacterialUniProt ID: Q88CZ6 ![]() Gene: hutU Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 123. Estradiol 17-beta-dehydrogenase 1 Pharmacological action: unknownFavors the reduction of estrogens and androgens. Also has 20-alpha-HSD activity. Uses preferentially NADH Organism class: humanUniProt ID: P14061 ![]() Gene: HSD17B1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 124. NAD-dependent malic enzyme, mitochondrial Pharmacological action: unknownOrganism class: human UniProt ID: P23368 ![]() Gene: ME2 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 125. Glucose-6-phosphate 1-dehydrogenase Pharmacological action: unknownD-glucose 6-phosphate + NADP(+) = D-glucono- 1,5-lactone 6-phosphate + NADPH Organism class: bacterialUniProt ID: P11411 ![]() Gene: zwf Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 126. Aldehyde dehydrogenase, mitochondrial Pharmacological action: unknownOrganism class: human UniProt ID: P05091 ![]() Gene: ALDH2 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
127. Glyceraldehyde-3-phosphate dehydrogenase, glycosomal Pharmacological action: unknownD-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH Organism class: parasiticUniProt ID: P22513 ![]() Protein Sequence: FASTA Gene Sequence: FASTA References: 128. Alcohol dehydrogenase class 4 mu/sigma chain Pharmacological action: unknownCould function in retinol oxidation for the synthesis of retinoic acid, a hormone important for cellular differentiation. Medium-chain (octanol) and aromatic (m-nitrobenzaldehyde) compounds are the best substrates. Ethanol is not a good substrate but at the high ethanol concentrations reached in the digestive tract, it plays a role in the ethanol oxidation and contributes to the first pass ethanol metabolism Organism class: humanUniProt ID: P40394 ![]() Gene: ADH7 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 129. Maltose-6'-phosphate glucosidase Pharmacological action: unknownHydrolyzes maltose-6'P and trehalose-6'P. Is involved in the catabolism of alpha-glycosides accumulated via a phosphoenolpyruvate-dependent maltose phosphotransferase system (PEP-PTS) Organism class: bacterialUniProt ID: P54716 ![]() Gene: glvA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 130. Diphtheria toxin Pharmacological action: unknownDiphtheria toxin, produced by a phage infecting corynebacterium diphtheriae, is a proenzyme that, after activation, catalyzes the covalent attachment of the ADP ribose moiety of NAD to elongation factor 2. Fragment A is responsible for enzymatic ADP-ribosylation of elongation factor 2, while fragment B is responsible for binding of toxin to cell receptors and entry of fragment A Organism class: viralUniProt ID: P00587 ![]() Protein Sequence: FASTA Gene Sequence: FASTA References: 131. GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1 Pharmacological action: unknownNAD(P)(+) + protein-L-arginine = nicotinamide + omega-N-(ADP-D-ribosyl)-protein-L-arginine Organism class: humanUniProt ID: P52961 ![]() Gene: ART1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
132. 6-phospho-beta-glucosidase bglT Pharmacological action: unknownHydrolyzes cellobiose 6'-phosphate into glucose 6- phosphate (Glc6P) and glucose Organism class: bacterialUniProt ID: Q9X108 ![]() Gene: bglT Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 133. Glucose--fructose oxidoreductase Pharmacological action: unknownD-glucose + D-fructose = D-gluconolactone + D- glucitol Organism class: bacterialUniProt ID: Q07982 ![]() Gene: gfo Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: human UniProt ID: P07327 ![]() Gene: ADH1A ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 135. Dihydropteridine reductase Pharmacological action: unknownThe product of this enzyme, tetrahydrobiopterin (BH-4), is an essential cofactor for phenylalanine, tyrosine, and tryptophan hydroxylases Organism class: humanUniProt ID: P09417 ![]() Gene: QDPR ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
136. Malate dehydrogenase Pharmacological action: unknownCatalyzes the reversible oxidation of malate to oxaloacetate Organism class: bacterialUniProt ID: P61889 ![]() Gene: mdh Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 137. 3-hydroxyacyl-CoA dehydrogenase type-2 Pharmacological action: unknownBinds intracellular amyloid-beta. By interacting with amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD) Organism class: humanUniProt ID: Q99714 ![]() Gene: HSD17B10 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
138. L-lactate dehydrogenase B chain Pharmacological action: unknownOrganism class: human UniProt ID: P07195 ![]() Gene: LDHB ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 139. 2,3-diketo-L-gulonate reductase Pharmacological action: unknownCatalyzes the reduction of 2,3-diketo-L-gulonate in the presence of NADH, to form 3-keto-L-gulonate Organism class: bacterialUniProt ID: P37672 ![]() Gene: dlgD Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 140. 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase Pharmacological action: unknownAndrostan-3-alpha,17-beta-diol + NAD(+) = 17- beta-hydroxyandrostan-3-one + NADH Organism class: bacterialUniProt ID: P19992 ![]() Protein Sequence: FASTA References: 141. NAD-dependent deacetylase sirtuin-5 Pharmacological action: unknownProbable NAD-dependent deacetylase (By similarity) Organism class: humanUniProt ID: Q9NXA8 ![]() Gene: SIRT5 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
142. Mono-ADP-ribosyltransferase C3 Pharmacological action: unknownADP-ribosylates eukaryotic Rho and Rac proteins on an asparagine residue Organism class: viralUniProt ID: P15879 ![]() Gene: C3 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 143. Dehydrogenase/reductase SDR family member 4-like 2 Pharmacological action: unknownProbable oxidoreductase (By similarity) Organism class: humanUniProt ID: Q6PKH6 ![]() Gene: DHRS4L2 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
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