赭曲霉TS孕酮11α-羟化酶的特性：一种细胞色素P-450连接的单加氧酶。
Characterization of progesterone 11 alpha-hydroxylase of Aspergillus ochraceus TS: a cytochrome P-450 linked monooxygenase.
作者信息
Samanta T B, Ghosh D K
机构信息
Department of Microbiology, Bose Institute, Calcutta, India.
出版信息
J Steroid Biochem. 1987 Sep;28(3):327-32. doi: 10.1016/0022-4731(87)91026-0.
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.
能够对孕酮进行11α-羟基化的赭曲霉TS单加氧酶已被分离为三个组分，并被鉴定为：（i）细胞色素P450，（ii）NADPH-细胞色素P450还原酶和（iii）磷脂酰胆碱。观察到11α-羟化酶依赖于NADPH，并且NADPH再生系统可增强羟基化作用。这种真菌单加氧酶与哺乳动物肝脏微粒体的单加氧酶有许多共同特征。测试了哺乳动物细胞色素P450诱导剂对赭曲霉TS中11α-羟化酶的诱导作用。还原酶已被部分纯化。
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