CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.100 | NADP-dependent oxidoreductase domain |
Domain Context
CATH Clusters
| Superfamily | NADP-dependent oxidoreductase domain |
| Functional Family | Aldo-keto reductase family 1 member B10 |
Enzyme Information
| 1.1.1.54 |
Allyl-alcohol dehydrogenase.
based on mapping to UniProt O60218
Allyl alcohol + NADP(+) = acrolein + NADPH.
-!- Also acts on saturated primary alcohols.
|
| 1.1.1.300 |
NADP-retinol dehydrogenase.
based on mapping to UniProt O60218
All-trans-retinol + NADP(+) = all-trans-retinal + NADPH.
-!- Greater catalytic efficiency in the reductive direction. -!- This observation, and the enzyme's localization at the entrance to the mitochondrial matrix, suggest that it may function to protect mitochondria against oxidative stress associated with the highly reactive retinal produced from dietary beta-carotene by EC 1.13.11.63. -!- Km-values for NADP(+) and NADPH are at least 800-fold lower than those for NAD(+) and NADH. -!- This enzyme differs from EC 1.1.1.105 which prefers NAD(+) and NADH. -!- Formerly EC 1.1.1.n2.
|
UniProtKB Entries (1)
| O60218 |
AK1BA_HUMAN
Homo sapiens
Aldo-keto reductase family 1 member B10
|
PDB Structure
| PDB | 4ICC |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Identification of a novel polyfluorinated compound as a lead to inhibit the human enzymes aldose reductase and AKR1B10: structure determination of both ternary complexes and implications for drug design.
Acta Crystallogr.,Sect.D
|
