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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)
Author(s) -
Tripathi Ashootosh,
Park Sung Ryeol,
Sikkema Andrew P.,
Cho Hyo Je,
Wu Jianfeng,
Lee Brian,
Xi Chuanwu,
Smith Janet L.,
Sherman David H.
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800363
Subject(s) - aryl , adenylate kinase , enzyme , stereochemistry , substrate (aquarium) , chemistry , flexibility (engineering) , combinatorial chemistry , function (biology) , biochemistry , biology , microbiology and biotechnology , mathematics , organic chemistry , statistics , alkyl , ecology
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).