title: Characterization of progesterone 11 alpha-hydroxylase of Aspergillus ochraceus TS: a cytochrome P-450 linked monooxygenase.
abstract: The monooxygenase of Aspergillus ochraceus TS capable of 11 alpha-hydroxylation of progesterone has been resolved into three components and characterized as (i) cytochrome P450, (ii) NADPH-cytochrome P450-reductase and (iii) phosphatidyl choline. The 11 alpha-hydroxylase was observed to be NADPH dependent, and hydroxylation was enhanced by a NADPH regenerating system. This fungal monooxygenase has many features in common with that of mammalian liver microsomes. The role of mammalian cytochrome P450 inducers were tested for induction of 11 alpha-hydroxylase in Aspergillus ochraceus TS. The reductase has been partially purified.
authors: Department of Microbiology, Bose Institute, Calcutta, India.
authors: T B
authors: TB
authors: Samanta
authors: D K
authors: DK
authors: Ghosh
mesh_terms: D001230:Aspergillus / Q000201:enzymology*; D002413:Cations, Divalent; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D004790:Enzyme Induction; D007700:Kinetics; D013250:Steroid Hydroxylases / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D002413:Cations, Divalent; D003577:Cytochrome P-450 Enzyme System; D013250:Steroid Hydroxylases; C074514:steroid 11-alpha-hydroxylase