Biochemical Characterization of an Arginine 2,3-Aminomutase with Dual Substrate Specificity

作     者：Junfeng Zhao Wenjuan Ji Xinjian Ji Qi Zhang Junfeng Zhao;Wenjuan Ji;Xinjian Ji;Qi Zhang

作者机构：Department of ChemistryFudan University2005 Songhu RoadShanghai 200438China 

出 版 物：《Chinese Journal of Chemistry》 (中国化学（英文版）)

年 卷 期：2020年第38卷第9期

页      面：959-962页

核心收录：

学科分类：081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 070303[理学-有机化学] 0703[理学-化学] 

基　　金：This work is supported in part by grants from the National Natural Science Foundation of China(Nos.21822703,31670060,and 21921003) from the National Key Research and Devel­opment Program(2018Y F A0900402 and 2016 Y F A0501302) 

主　　题：radical catalytic conclusion 

摘      要：Summary of main observation and conclusion The radical S-adenosylmethionine(SAM)aminomutases represent an important pathway for the bio­synthesis of p-amino *** this study,we report biochemical characterization of BlsG involved in blasticidin S biosynthesis as a radical SAM arginine 2,*** showed that BlsG acts on both£-arginine and L-lysine with comparable catalytic *** dual substrate specificity was also observed for the lysine 2,3-aminomutase from Escherichia coli(LAMec).The catalytic efficiency of LAMEc is similar to that of BlsG,but is significantly lower than that of the enzyme from Clostridium subterminale(LAMcs),which acts only on L-lysine rather than on ***,we showed that enzymes can be grouped into two major phylogenetic clades,each corresponding to a certain C3 stereochemistry of the P-amino acid *** study expands the radical SAM aminomutase members and provides insights into enzyme evolution,supporting a trade-off between substrate promiscuity and catalytic efficiency.