CATH Classification

Domain Context

CATH Clusters

Superfamily NADP-dependent oxidoreductase domain
Functional Family Aldo-keto reductase family 1 member A1

Enzyme Information

1.1.1.54
Allyl-alcohol dehydrogenase.
based on mapping to UniProt P50578
Allyl alcohol + NADP(+) = acrolein + NADPH.
-!- Also acts on saturated primary alcohols.
1.1.1.33
Mevaldate reductase (NADPH).
based on mapping to UniProt P50578
(R)-mevalonate + NADP(+) = mevaldate + NADPH.
-!- May be identical with EC 1.1.1.2.
1.1.1.19
Glucuronate reductase.
based on mapping to UniProt P50578
L-gulonate + NADP(+) = D-glucuronate + NADPH.
-!- Also reduces D-galacturonate. -!- May be identical with EC 1.1.1.2.
1.1.1.2
Alcohol dehydrogenase (NADP(+)).
based on mapping to UniProt P50578
An alcohol + NADP(+) = an aldehyde + NADPH.
-!- Some members of this group oxidize only primary alcohols; others act also on secondary alcohols. -!- May be identical with EC 1.1.1.19, EC 1.1.1.33 and EC 1.1.1.55. -!- Re-specific with respect to NADPH.
1.1.1.20
Glucuronolactone reductase.
based on mapping to UniProt P50578
L-gulono-1,4-lactone + NADP(+) = D-glucurono-3,6-lactone + NADPH.
1.1.1.372
D/L-glyceraldehyde reductase.
based on mapping to UniProt P50578
(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)

P50578
AK1A1_PIG
Sus scrofa
Aldo-keto reductase family 1 member A1

PDB Structure

PDB 3H4G
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure of aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity
El-Kabbani, O., Carbone, V., Darmanin, C., Oka, M., Mitschler, A., Podjarny, A., Schulze-Briese, C., Chung, R.P.
J.Med.Chem.