Abstract
Growing cultures of Aspergillus niger hydroxylate progesterone at the 6α and 11αpositions. The properties of the 6β-hydroxylase activity were studied in extracts of this organism using 11α hydroxyprogesterone as substrate. Maximum 6β-hydroxylase activity was obtained at pH 6·5. EDTA and thiophenol inhibited hydroxylation, while NADPH, 2-oxoglutarate and pyruvate stimulated it. Cobalt and cadmium ions inhibited the 6β-hydroxylase activity. The feasibility of introducing a hydroxyl group into the 6β-position of various steroid compounds was tested: the 3-Δ4 configuration appeared to exert a directional effect for 6β-hydroxylation, while an 11β-hydroxyl group exerted some kind of steric hindrance against 6β-hydroxylation.
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