CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.180 | Quinone Oxidoreductase; Chain A, domain 1 |
|
3.90.180.10 | Medium-chain alcohol dehydrogenases, catalytic domain |
Domain Context
CATH Clusters
| Superfamily | Medium-chain alcohol dehydrogenases, catalytic domain |
| Functional Family | S-(hydroxymethyl)glutathione dehydrogenase |
Enzyme Information
| 1.1.1.1 |
Alcohol dehydrogenase.
based on mapping to UniProt P00327
(1) A primary alcohol + NAD(+) = an aldehyde + NADH. (2) A secondary alcohol + NAD(+) = a ketone + NADH.
-!- Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. -!- The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
|
UniProtKB Entries (1)
| P00327 |
ADH1E_HORSE
Equus caballus
Alcohol dehydrogenase E chain
|
PDB Structure
| PDB | 6OA7 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Substitutions of amino acid residues in the substrate binding site of horse liver alcohol dehydrogenase have small effects on structure but significantly affect catalysis of hydrogen transfer.
To Be Published
|