Hydroxylation of steroids with nonpolar side chains with 11 alpha-hydroxylase of Rhizopus nigricans.
Steroids with nonpolar side chains with 2, 4 and 8 C atoms were used as substrates for the 11 alpha-hydroxylase of Rhizopus nigricans. Their bioconversion was compared to that of progesterone, which was found to be far the best substrate giving the highest total bioconversion. 3-keto-4-ene steroids with nonpolar side chains were converted to their hydroxylated products in a small yield or not at all. The absence of an oxygen function in the side chain did not affect the regio-specificity of the hydroxylation, but resulted in a much lower total bioconversion. The strong effect of the oxygen function and of the length of the side chain on hydroxylation with the 11 alpha-hydroxylase of Rhizopus nigricans was demonstrated.
Zakelj-Mavric
M
M
Institute of Biochemistry, Medical Faculty, University E. Kardelj, Ljubljana, Yugoslavia.
Kastelic-Suhadolc
T
T
Gottlieb
H E
HE
Belic
I
I
D006900:Hydroxylation; D012233:Rhizopus / Q000201:enzymology*; D013252:Steroid 11-beta-Hydroxylase / Q000378:metabolism*; D013250:Steroid Hydroxylases / Q000378:metabolism*; D013256:Steroids / Q000378:metabolism*
D013256:Steroids; D013250:Steroid Hydroxylases; D013252:Steroid 11-beta-Hydroxylase