A Defined and Flexible Pocket Explains Aryl Substrate Promiscuity of the Cahuitamycin Starter Unit-Activating Enzyme CahJ.
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ABSTRACT:
SUBMITTER: Tripathi A
PROVIDER: S-EPMC6105470 | biostudies-literature | 2018 Aug
REPOSITORIES: biostudies-literature
Publications
A Defined and Flexible Pocket Explains Aryl Substrate Promiscuity of the Cahuitamycin Starter Unit-Activating Enzyme CahJ.
Tripathi Ashootosh A Park Sung Ryeol SR Sikkema Andrew P AP Cho Hyo Je HJ Wu Jianfeng J Lee Brian B Xi Chuanwu C Smith Janet L JL Sherman David H DH
Chembiochem : a European journal of chemical biology 20180621 15
Cahuitamycins are biofilm inhibitors assembled by a convergent nonribosomal peptide synthetase pathway. Previous genetic analysis indicated that a discrete enzyme, CahJ, serves as a gatekeeper for cahuitamycin structural diversification. Here, the CahJ protein was probed structurally and functionally to guide the formation of new analogues by mutasynthetic studies. This analysis enabled the in vivo production of a new cahuitamycin congener through targeted precursor incorporation. ...[more]
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