CATH Domain 4lb4A00

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.
1.1.1.300	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)

ALDR_HUMAN

Homo sapiens

Aldo-keto reductase family 1 member B1

PDB Structure

PDB	4LB4
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Modulation of aldose reductase inhibition by halogen bond tuning. Fanfrlik, J., Kolar, M., Kamlar, M., Hurny, D., Ruiz, F.X., Cousido-Siah, A., Mitschler, A., Rezac, J., Munusamy, E., Lepsik, M., Matejicek, P., Vesely, J., Podjarny, A., Hobza, P. Acs Chem.Biol.