CATH Classification

Domain Context

CATH Clusters

Superfamily NADP-dependent oxidoreductase domain
Functional Family Aldo-keto reductase family 1 member B1

Enzyme Information
Aldehyde reductase.
based on mapping to UniProt P15121
Alditol + NAD(P)(+) = aldose + NAD(P)H.
-!- Wide specificity. -!- Formerly EC
Allyl-alcohol dehydrogenase.
based on mapping to UniProt P15121
Allyl alcohol + NADP(+) = acrolein + NADPH.
-!- Also acts on saturated primary alcohols.
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 -!- Km-values for NADP(+) and NADPH are at least 800-fold lower than those for NAD(+) and NADH. -!- This enzyme differs from EC which prefers NAD(+) and NADH. -!- Formerly EC 1.1.1.n2.
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.

UniProtKB Entries (1)

Homo sapiens
Aldo-keto reductase family 1 member B1

PDB Structure

PDB 1T41
External Links
Organism Escherichia
Primary Citation
The crystallographic structure of the aldose reductase-IDD552 complex shows direct proton donation from tyrosine 48.
Ruiz, F., Hazemann, I., Mitschler, A., Joachimiak, A., Schneider, T., Karplus, M., Podjarny, A.
Acta Crystallogr.,Sect.D