title: Hydroxylation of steroids with nonpolar side chains with 11 alpha-hydroxylase of Rhizopus nigricans.
abstract: 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.
authors: Institute of Biochemistry, Medical Faculty, University E. Kardelj, Ljubljana, Yugoslavia.
authors: M
authors: M
authors: Zakelj-Mavric
authors: T
authors: T
authors: Kastelic-Suhadolc
authors: H E
authors: HE
authors: Gottlieb
authors: I
authors: I
authors: Belic
mesh_terms: D006900:Hydroxylation; D012233:Rhizopus / Q000201:enzymology*; D013252:Steroid 11-beta-Hydroxylase / Q000378:metabolism*; D013250:Steroid Hydroxylases / Q000378:metabolism*; D013256:Steroids / Q000378:metabolism*
chemical_list: D013256:Steroids; D013250:Steroid Hydroxylases; D013252:Steroid 11-beta-Hydroxylase