Carbonyl reductase activity exhibited by pig testicular 20β- hydroxysteroid dehydrogenase

Article abstract of DOI:10.1248/bpb.20.1215

The carbonyl reductase activity exhibited by pig testicular 20β- hydroxysteroid dehydrogenase (20β-HSD) was examined using a recombinant enzyme. Kinetic parameters were obtained for 48 carbonyl group-containing substrates, including aromatic aldehydes, aromatic ketones, cycloketones, quinones, aliphatic aldehydes and aliphatic ketones. 20β-HSD showed a high affinity towards quinones, such as 9,10-phenanthrenequinone, α- naphthoquinone and menadione (K(m) values of 4, 2 and 5 μM, respectively), and the substrate utilization efficiency (V(max)/K(m)) of the enzyme against these quinones was very high. Cyclohexanone and 2-methylcyclohexanone were also reduced with a high V(max)/K(m) value, but not cyclopentanone or 2- methylcyclopentanone. Various aromatic aldehydes and ketones including benzaldehyde- and acetophenone-derivatives were reduced by 20β-HSD. Especially, 4-nitrobenzaldehyde and 4-nitroacetophenone were reduced with high V(max)/K(m) values in the related compounds. The enzyme also reduced the pyridine-derivatives, 2-, 3-, and 4-benzoylpyridine, with the V(max)/K(m) value for 2-benzoylpyridine being the highest. 20β-HSD reduced aliphatic aldehydes and aliphatic ketones, but was more effective on the former. The correlation between the structure of carbonyl compounds and their substrate V(max)/K(m) is discussed.

Full text of DOI:10.1248/bpb.20.1215

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