CATH Classification

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.
1.1.1.300
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.
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.

UniProtKB Entries (1)

P15121
ALDR_HUMAN
Homo sapiens
Aldo-keto reductase family 1 member B1

PDB Structure

PDB 4YS1
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Price for Opening the Transient Specificity Pocket in Human Aldose Reductase upon Ligand Binding: Structural, Thermodynamic, Kinetic, and Computational Analysis.
Rechlin, C., Scheer, F., Terwesten, F., Wulsdorf, T., Pol, E., Fridh, V., Toth, P., Diederich, W.E., Heine, A., Klebe, G.
ACS Chem. Biol.