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 | Sorbitol dehydrogenase |
Enzyme Information
| 1.1.1.9 |
D-xylulose reductase.
based on mapping to UniProt Q00796
Xylitol + NAD(+) = D-xylulose + NADH.
-!- Also acts as an L-erythrulose reductase.
|
| 1.1.1.56 |
Ribitol 2-dehydrogenase.
based on mapping to UniProt Q00796
Ribitol + NAD(+) = D-ribulose + NADH.
|
| 1.1.1.4 |
(R,R)-butanediol dehydrogenase.
based on mapping to UniProt Q00796
(R,R)-butane-2,3-diol + NAD(+) = (R)-acetoin + NADH.
-!- Also converts diacetyl into acetoin with NADH as reductant.
|
| 1.1.1.- |
With NAD(+) or NADP(+) as acceptor.
based on mapping to UniProt Q00796
|
| 1.1.1.14 |
L-iditol 2-dehydrogenase.
based on mapping to UniProt Q00796
L-iditol + NAD(+) = L-sorbose + NADH.
-!- This enzyme is widely distributed and has been described in archaea, bacteria, yeast, plants and animals. -!- It acts on a number of sugar alcohols, including (but not limited to) L-iditol, D-glucitol, D-xylitol, and D-galactitol. -!- Enzymes from different organisms or tissues display different substrate specificity. -!- The enzyme is specific to NAD(+) and can not use NADP(+).
|
UniProtKB Entries (1)
| Q00796 |
DHSO_HUMAN
Homo sapiens
Sorbitol dehydrogenase
|
PDB Structure
| PDB | 1PL7 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
X-ray crystallographic and kinetic studies of human sorbitol dehydrogenase.
Structure
|
