1. The 16α‐Hydroxylation of Progesterone by Cytochrome P450 107X1 from Streptomyces avermitilis
- Author
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Susu Lin, Bingbing Ma, Qilin Gao, Jian Yang, Gang Lai, Runhao Lin, Bingxian Yang, Bing‐Nan Han, and Lian‐Hua Xu
- Subjects
Cytochrome P-450 Enzyme System ,Molecular Medicine ,Bioengineering ,General Chemistry ,General Medicine ,Hydroxylation ,Molecular Biology ,Biochemistry ,Progesterone ,Streptomyces - Abstract
Cytochrome P450 enzymes (CYPs or P450s) are ubiquitous heme-dependent enzymes that catalyze the monooxygenation of non-activated C-H bonds to modify the structure of the substrate. In this study, we heterologously expressed CYP107X1 from Streptomyces avermitilis and conducted in vitro substrate screening using the alternative redox partners putidaredoxin and putidaredoxin reductase. CYP107X1 catalyzed the 16α-hydroxylation of progesterone with regio- and stereoselectivity. The spectroscopic analyses showed that CYP107X1 bound progesterone with a relatively high K
- Published
- 2022
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