An Acyl Transfer Reaction Catalyzed by an Epimerase MarH

详细信息    查看全文

• 作者：Mo Han ; Haixing Yin ; Yi Zou ; Nelson L. Brock ; Tingting Huang ; Zixin Deng ; Yiwen Chu ; Shuangjun Lin
• 刊名：ACS Catalysis
• 出版年：2016
• 出版时间：February 5, 2016
• 年：2016
• 卷：6
• 期：2
• 页码：788-792
• 全文大小：308K
• ISSN：2155-5435

文摘

MarH, a small protein (129 amino acids) belonging to the cupin superfamily, was previously characterized as an epimerase involved in the (2S,3S)-β-methyltryptophan formation in the maremycin biosynthesis. Here, MarH was discovered to act as an acyltransferase that can catalyze the 3-O-acylation of chloramphenicol. Furthermore, MarH can catalyze N-acylation of deacylated chloramphenicol analogue thereby activating them for 3-O-acylation. By systematic site-directed mutagenesis, H64 was revealed as a potential catalytic base that deprotonates the acyl acceptor substrate. Nucleophilic attack at the carbonyl carbon of the acyl donor then gives the acylation product.