在替考拉宁生物合成中鉴定两种细胞色素 P450 揭示了修饰的反应时间。
Characterizing Two Cytochrome P450s in Tiacumicin Biosynthesis Reveals Reaction Timing for Tailoring Modifications.
机构信息
Key Laboratory of Tropical Marine Bio-resources and Ecology, Guangdong Key Laboratory of Marine Materia Medica , South China Sea Institute of Oceanology, Innovation Academy for South China Sea Ecology and Environmental Engineering, Chinese Academy of Sciences , 164 West Xingang Road , Guangzhou 510301 , P. R. China.
Key Laboratory of Microbial Molecular Biology of Hunan Province, College of Life Science , Hunan Normal University , No. 36, Lushan Road , Changsha 410081 , P. R. China.
出版信息
Org Lett. 2019 Sep 20;21(18):7679-7683. doi: 10.1021/acs.orglett.9b03100. Epub 2019 Sep 11.
Functions of the tailoring enzymes for the biosynthesis of tiacumicin B () have been previously determined. However, the reaction timing remains elusive. Herein, we report the biochemical characterization of two P450 enzymes TiaP1 and TiaP2. The investigation of their substrate scope and kinetic parameters clearly demonstrates that the TiaP2-catalyzed C-20 hydroxylation is the first tailoring step and the TiaP1-catalyzed C-18 hydroxylation is the last step in the biosynthesis of .
此前已经确定了 tiacumicin B()生物合成中修饰酶的功能。然而，反应时间仍然难以捉摸。在此，我们报告了两种 P450 酶 TiaP1 和 TiaP2 的生化特征。对它们的底物范围和动力学参数的研究清楚地表明，TiaP2 催化的 C-20 羟化是第一个修饰步骤，而 TiaP1 催化的 C-18 羟化是 tiacumicin B()生物合成中的最后一步。
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