Ocean College, Zhejiang University, Dinghai, Zhoushan, 316021, P. R. China.
College of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou, 310018, P. R. China.
Chem Biodivers. 2021 Apr;18(4):e2000910. doi: 10.1002/cbdv.202000910. Epub 2021 Mar 3.
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 =311.60±87.30 μM and k =2.01±0.33 min . 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.
细胞色素 P450 酶（P450s）是多功能的生物催化剂，可在温和条件下将分子氧插入失活的 C-H 键中。链霉菌属avermitilis 的 CYP105D7 已被报道为一种细菌底物混杂的 P450，可催化 1-去氧戊烯酸、双氯芬酸、柚皮素、康帕丁和类固醇的羟化。在这项研究中，CYP105D7 催化辣椒素的羟化、环氧化和脱氢作用，揭示了其功能多样性。CYP105D7 氧化辣椒素的动力学参数确定为 K =311.60±87.30 μM 和 k =2.01±0.33 min 。此外，我们进行了分子对接、突变和底物结合分析，表明 Arg81 在辣椒素结合和催化中起关键作用。据我们所知，这项研究首次报道了原核 P450s 可以催化辣椒素。
