Hydroxysteroid dehydrogenase of Cochliobolus lunatus.
Cochliobolus lunatus is known to be able to hydroxylate steroids at position 11 beta. Besides this inducible enzyme, we found a constitutive hydroxysteroid dehydrogenase activity which is strongly regioselective with the highest activity at position 17, and the best substrate was found to be androstenedione. Using different substrates, no such activities were observed at positions 3 or 11. The enzyme is membrane bound and NADH or NADPH dependent. The protoplasts of Cochliobolus lunatus show the same activity as intact cells, which means that the cell wall does not influence the reaction.
Plemenitas
A
A
Institute of Biochemistry, Medical Faculty, University E. Kardelj, Ljubljana, Yugoslavia.
Zakelj-Mavric
M
M
Komel
R
R
D015067:17-Hydroxysteroid Dehydrogenases / Q000378:metabolism; D001203:Ascomycota / Q000201:enzymology*; D002462:Cell Membrane / Q000201:enzymology; D006913:Hydroxysteroid Dehydrogenases / Q000378:metabolism*; D009243:NAD / Q000494:pharmacology; D009249:NADP / Q000494:pharmacology
D009243:NAD; D009249:NADP; D015067:17-Hydroxysteroid Dehydrogenases; D006913:Hydroxysteroid Dehydrogenases; C032690:3-alpha-(17-beta)-hydroxysteroid dehydrogenase (NAD(+))