LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Conserved_site |
| Description | Alcohol dehydrogenase ( ) (ADH) catalyzes the reversible oxidation of ethanol to acetaldehyde with the concomitant reduction of NAD: Ethanol + NAD = Acetaldehyde + NADH Currently three structurally and catalytically different types of alcohol dehydrogenases are known:Zinc-containing 'long-chain' alcohol dehydrogenases.Insect-type, or 'short-chain' alcohol dehydrogenases.Iron-containing alcohol dehydrogenases.Zinc-containing ADH's [, ] are dimeric or tetrameric enzymes that bind twoatoms of zinc per subunit. One of the zinc atom is essential for catalytic activity while the other is not. Both zinc atoms are coordinated by eithercysteine or histidine residues; the catalytic zinc is coordinated by two cysteines and one histidine. Zinc-containing ADH's are found in bacteria,mammals, plants, and in fungi. In most species there are more than one isozyme (for example, human have at least six isozymes, yeast have three, etc.). A number of other zinc-dependent dehydrogenases are closely related to zincADH [ ] and are included in this family, includingxylitol dehydrogenase ( ); sorbitol dehydrogenase ( ); aryl-alcohol dehydrogenase (); threonine 3-dehydrogenase ( ); cinnamyl-alcohol dehydrogenase ( ) (CAD); galactitol-1-phosphate dehydrogenase (); and Pseudomonas putida 5-exo-alcohol dehydrogenase ( ). |
| Short Name | ADH_Zn_CS |
