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Cover Feature: A Defined and Flexible Pocket Explains Aryl Substrate Promiscuity of the Cahuitamycin Starter Unit–Activating Enzyme CahJ (ChemBioChem 15/2018)
ChemBioChem ( IF 3.2 ) Pub Date : 2018-07-09 , DOI: 10.1002/cbic.201800363
Ashootosh Tripathi 1, 2 , Sung Ryeol Park 1, 3 , Andrew P. Sikkema 1, 4, 5 , Hyo Je Cho 6 , Jianfeng Wu 7 , Brian Lee 1 , Chuanwu Xi 7 , Janet L. Smith 1, 4 , David H. Sherman 1, 2, 8, 9
Affiliation  

The cover feature picture shows the substrate binding pocket of the promiscuous aryl transferase CahJ in complex with salicyl adenylate. This enzyme activates aryl substrates with ATP to form adenylate intermediates that are subsequently transferred to an aryl carrier protein (ArCP) as the first step in cahuitamycin biosynthesis. CahJ acts as a gatekeeper for cahuitamycin structural diversification, and structural and function studies of CahJ substrate flexibility guided the creation of a new cahuitamycin congener. More information can be found in the communication by D. H. Sherman et al. on page 1595 in Issue 15, 2018 (DOI: 10.1002/cbic.201800233).
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中文翻译:

封面功能:明确而灵活的口袋说明了Cahuitamycin起始剂单元-活化酶CahJ的芳基底物混杂性(ChemBioChem 15/2018)

封面特征图片显示了混杂的芳基转移酶CahJ与水杨基腺苷酸复合的底物结合口袋。该酶用ATP激活芳基底物以形成腺苷酸中间体,随后将其转移至芳基载体蛋白(ArCP),作为卡他霉素生物合成的第一步。CahJ充当cahuitamycin结构多样化的守门人,CahJ底物柔性的结构和功能研究指导了新cahuitamycin同源物的产生。在D. H. Sherman等人的来文中可以找到更多信息。就在第15期,2018页1595(:10.1002 / cbic.201800233 DOI)。
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更新日期:2018-07-09
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