18.104.22.168 - Alcohol dehydrogenase
- Aldehyde reductase.
primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Zn(2+) or Fe cation.
An NAD+-dependent enzyme that catalyzes the oxidation of alcohols to aldehydes/ketones and that is also able to further oxidize aldehydes to their corresponding carboxylic acids. It is a zinc-independent protein which is a member of the short-chain dehydrogenases/reductases (SDR) family. It is known to be inhibited by 2,2,2-trifluoroethanol and pyrazole.
The NAD cofactor binds first, causing one of the active site waters to deprotonate Tyr152. Once the alcohol substrate has been bound, Tyr152 abstracts its hydroxyl proton, initiating the hydride transfer to NAD. The ketone product is released first, followed by the NADH.
|AA||Uniprot||Uniprot Resid||PDB||PDB Resid|
hydride transfer, proton transfer, aromatic bimolecular nucleophilic addition, overall product formed, cofactor used
Organism KM Value [mM] Substrate Comment Aeropyrum pernix 1.1 1-Pentanol pH 8.0, 60°C Yokenella sp. 11 (2E)-but-2-en-1-ol pH 8.0, 55°C Sulfolobus acidocaldarius 8.4 NAD+ 65°C, pH 8.0 Oenococcus oeni 4.9 NAD+ pH 9.0, 60°C, recombinant enzyme Thermus thermophilus 0.7 4-methoxybenzaldehyde pH 6.0, 65°C
Organism Temperature Range Comment Natronomonas pharaonis 50 - 80 50°C: 45% of maximal activity, 80°C: about 60% of maximal activity Candida parapsilosis 20 - 50 20°C: about 80% of maximal activity, 50°C: about 55% of maximal activity Magnusiomyces capitatus 20 - 50 20°C: about 80% of maximal activity, 50°C: about 60% of maximal activity, reduction of N-benzyl-3-pyrrolidinone Saccharomyces cerevisiae 15 - 50 Sporotrichum pulverulentum 10 - 60 10°C: about 65% of maximal activity, 50°C: about 40% of maximal activity
Organism pH Range Comment Saccharomyces cerevisiae 5 - 9 [Candida] maris 5.5 - 9 reduction reaction activity range, profile overview Geobacillus thermodenitrificans 6 - 9 Equus caballus 7 - 11 under the analyzed conditions, the activity of HLADH steadily increases with increasing pH up to pH 9.0 and then decreases at more alkaline conditions, but highest oxidative lactimization activity at pH 11.00 in the coupled assay with NADH oxidase Homo sapiens 8 - 12 about 30% of maximal activity at pH 8.0 and at pH 12.0
- Utilizing Alcohol for Alkane Biosynthesis by Introducing a Fatty Alcohol Dehydrogenase.
- Enhancement of solubility of recombinant alcohol dehydrogenase from Rhodococcus ruber using predictive tool
- Alcohol dehydrogenase 4 is a TP53-associated gene signature for the prediction of prognosis in hepatocellular carcinoma.
- Investigating the Effect of Alcohol Dehydrogenase Gene Knockout on Lipid Accumulation in Mucor circinelloides WJ11.
- Enhancement of solubility of recombinant alcohol dehydrogenase from Rhodococcus ruber using predictive tool.
- Electrospun aluminum silicate nanofibers as novel support material for immobilization of alcohol dehydrogenase.
- [Substitutability of metal-binding sites in an alcohol dehydrogenase].
- Transcriptional and metabolic changes associated with internode development and reduced cinnamyl alcohol dehydrogenase activity in sorghum.
- The alcohol dehydrogenase isoenzyme (ADH I) as a marker of intrahepatic cholestasis of pregnancy.
- Maternal Alcohol Dehydrogenase 1 Heterozygosity Drives Resistance of Offspring to Weight Gain
- Dependence of crystallographic atomic displacement parameters on temperature (25-150 K) for complexes of horse liver alcohol dehydrogenase.