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Hydroxylation, Epoxidation, and Dehydrogenation of Capsaicin by a Microbial Promiscuous Cytochrome P450 105D7
Author(s) -
Ma Bingbing,
Wang Qianwen,
Han BingNan,
Ikeda Haruo,
Zhang Chunfang,
Xu LianHua
Publication year - 2021
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.202000910
Subject(s) - chemistry , hydroxylation , capsaicin , cytochrome p450 , dehydrogenation , monooxygenase , stereochemistry , docking (animal) , streptomyces avermitilis , cytochrome , naringenin , enzyme , catalysis , biochemistry , streptomyces , bacteria , antioxidant , medicine , receptor , nursing , flavonoid , biology , genetics
Cytochrome P450 enzymes (P450s) are versatile biocatalysts, which insert a molecular oxygen into inactivated C−H bonds under mild conditions. CYP105D7 from Streptomyces avermitilis has been reported as a bacterial substrate‐promiscuous P450 which catalyzes the hydroxylation of 1‐deoxypentalenic acid, diclofenac, naringenin, compactin and steroids. In this study, CYP105D7 catalyzes hydroxylation, epoxidation and dehydrogenation of capsaicin, a pharmaceutical agent, revealing its functional diversity. The kinetic parameters of the CYP105D7 oxidation of capsaicin were determined as K m =311.60±87.30 μM and k cat =2.01±0.33 min −1 . In addition, we conducted molecular docking, mutagenesis and substrate binding analysis, indicating that Arg81 plays crucial role in the capsaicin binding and catalysis. To our best knowledge, this study presents the first report to illustrate that capsaicin can be catalyzed by prokaryotic P450s.