Dihydrodiol Dehydrogenase 2 (DDH2)

Dihydrodiol dehydrogenase (DD; EC 1.3.1.20), a member of the aldo-oxo reductase (AKR) superfamily, catalyzes the NADP-linked oxidation of trans-dihydrodiols of aromatic hydrocarbons to corresponding catechols. DDH2 encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols using NADH and/or NADPH as cofactors. The enzymes display overlapping but distinct substrate specificity. This enzyme binds bile acid with high affinity, and shows minimal 3-alpha-hydroxysteroid dehydrogenase activity. This gene shares high sequence identity with three other gene members and is clustered with those three genes at chromosome 10p15-p14.