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.- |
With NAD(+) or NADP(+) as acceptor.
based on mapping to UniProt P11766
|
| 1.1.1.1 |
Alcohol dehydrogenase.
based on mapping to UniProt P11766
(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.
|
| 1.1.1.284 |
S-(hydroxymethyl)glutathione dehydrogenase.
based on mapping to UniProt P11766
S-(hydroxymethyl)glutathione + NAD(P)(+) = S-formylglutathione + NAD(P)H.
-!- The substrate, S-(hydroxymethyl)glutathione, forms spontaneously from glutathione and formaldehyde; its rate of formation is increased in some bacteria by the presence of EC 4.4.1.22. -!- Forms part of the pathway that detoxifies formaldehyde, since the product is hydrolyzed by EC 3.1.2.12. -!- Also specifically reduces S-nitrosylglutathione. -!- Formerly EC 1.2.1.1.
|
UniProtKB Entries (1)
| P11766 |
ADHX_HUMAN
Homo sapiens
Alcohol dehydrogenase class-3
|
PDB Structure
| PDB | 2FZE |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure-function relationships in human glutathione-dependent formaldehyde dehydrogenase. Role of Glu-67 and Arg-368 in the catalytic mechanism.
Biochemistry
|
