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Publication Abstract from PubMed

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 16alpha-hydroxylation of progesterone with regio- and stereoselectivity. The spectroscopic analyses showed that CYP107X1 bound progesterone with a relatively high K(d) value of 65.3+/-38.9 muM. The K(m) and k(cat) values for progesterone were estimated to be 47.7+/-12.0 muM and 0.30 min(-1) , respectively. Furthermore, a crystal structure was obtained of CYP107X1 bound with glycerol from the buffer solution. Interestingly, a conserved threonine was replaced with asparagine in CYP107X1, indicating that it may adopt an unnatural proton transfer process and play a crucial role in its catalytic activity.

The 16alpha-Hydroxylation of Progesterone by Cytochrome P450 107X1 from Streptomyces avermitilis.,Lin S, Ma B, Gao Q, Yang J, Lai G, Lin R, Yang B, Han BN, Xu LH Chem Biodivers. 2022 May;19(5):e202200177. doi: 10.1002/cbdv.202200177. Epub 2022 , Apr 26. PMID:35426465^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.