化学
单加氧酶
生物合成
黄素组
立体化学
含黄素单加氧酶
生物化学
酶
细胞色素P450
作者
Jiang Chen,Hongjie Zhu,Ming Peng,Shanwen Zhang,Qinglian Li,Yu‐Cheng Gu,Jianhua Ju
摘要
Kendomycin B is distinguished from other ansamycins by its unique, fully carbogenic ansa scaffold. We show here that FAD-dependent monooxygenase Kmy13 is solely responsible for installing the rare ansa structural framework; in vivo gene disruption/complementation experiments and in vitro enzymatic assays are described in detail. Moreover, the compound with a β-keto ester, kendolactone A (2), was confirmed as the natural substrate of Kmy13 and a bona fide biosynthetic intermediate en route to kendomycin B. Further structural prediction and biochemical assays have provided significant insights into the catalytic mechanism of Kmy13.
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