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3 Alpha-hydroxysteroid dehydrogenase (3 alpha-HSD) from Pseudomonas testosteroni was shown to reduce the xenobiotic carbonyl compound metyrapone (MPON). Reversely, MPON reductase purified from mouse liver microsomes and previously characterized as aldehyde reductase, was competitively inhibited by 3 alpha-HSD steroid substrates. For MPON reduction both enzymes can use either NADH or NADPH as co-substrate. Immunoblot analysis after native and SDS gel electrophoresis of 3 alpha-HSD gave a specific crossreaction with the antibodies against the microsomal mouse liver MPON reductase pointing to structural homologies between these enzymes. In conclusion, there seem to exist structural as well as functional relationships between a mammalian liver aldehyde reductase and prokaryotic 3 alpha-HSD. Moreover, based on the molecular weights and the co-substrate specificities microsomal mouse liver MPON reductase and Pseudomonas 3 alpha-HSD seem to be members of the short-chain alcohol dehydrogenase family.

Original publication

DOI

10.1016/0014-5793(92)80359-o

Type

Journal article

Journal

FEBS letters

Publication Date

02/1992

Volume

297

Pages

196 - 200

Addresses

Department of Pharmacology and Toxicology, School of Medicine, University of Marburg, Marburg/Lahn, Germany.

Keywords

Microsomes, Liver, Animals, Mice, Pseudomonas, NAD, NADP, Alcohol Oxidoreductases, Hydroxysteroid Dehydrogenases, Blotting, Western, Electrophoresis, Polyacrylamide Gel, Cross Reactions, Substrate Specificity, Oxidation-Reduction, Female