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 B1 |
Enzyme Information
| 1.1.1.21 |
Aldehyde reductase.
based on mapping to UniProt P15121
Alditol + NAD(P)(+) = aldose + NAD(P)H.
-!- Wide specificity. -!- Formerly EC 1.1.1.139.
|
| 1.1.1.54 |
Allyl-alcohol dehydrogenase.
based on mapping to UniProt P15121
Allyl alcohol + NADP(+) = acrolein + NADPH.
-!- Also acts on saturated primary alcohols.
|
| 1.1.1.372 |
D/L-glyceraldehyde reductase.
based on mapping to UniProt P15121
(1) Glycerol + NADP(+) = L-glyceraldehyde + NADPH. (2) Glycerol + NADP(+) = D-glyceraldehyde + NADPH.
-!- The enzyme takes part in a D-galacturonate degradation pathway in the fungi Aspergillus niger and Trichoderma reesei (Hypocrea jecorina). -!- It has equal activity with D- and L-glyceraldehyde, and can also reduce glyoxal and methylglyoxal. -!- The reaction is only observed in the direction of glyceraldehyde reduction.
|
| 1.1.1.300 |
NADP-retinol dehydrogenase.
based on mapping to UniProt P15121
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)
| P15121 |
ALDR_HUMAN
Homo sapiens
Aldo-keto reductase family 1 member B1
|
PDB Structure
| PDB | 2ACR |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
An anion binding site in human aldose reductase: mechanistic implications for the binding of citrate, cacodylate, and glucose 6-phosphate.
Biochemistry
|