Hydroxylation of steroids with 11 alpha-hydroxylase of Rhizopus nigricans.
Three groups of 3-keto-4-ene steroids with different side chains were used as substrates for the induced 11 alpha-hydroxylase of Rhizopus nigricans. The highest total bioconversion as well as the highest yield of 11 alpha-hydroxylated product is found using progesterone as substrate. By changing the polarity of the side chain, much higher yields of 6 beta- and 7 beta-hydroxylated products relative to 11 alpha-hydroxylated product are obtained. Our results thus provide evidence for the importance of the side chain in steroid-enzyme interactions.
D001426:Bacterial Proteins / Q000378:metabolism*; D001711:Biotransformation; D008968:Molecular Conformation; D011374:Progesterone / Q000378:metabolism; D012233:Rhizopus / Q000201:enzymology*; D013252:Steroid 11-beta-Hydroxylase / Q000378:metabolism*; D013250:Steroid Hydroxylases / Q000378:metabolism*; D013256:Steroids / Q000378:metabolism; D013379:Substrate Specificity
D001426:Bacterial Proteins; D013256:Steroids; D011374:Progesterone; D013250:Steroid Hydroxylases; D013252:Steroid 11-beta-Hydroxylase