Molecular basis of perhydrolase activity in serine hydrolases

被引：57

作者：

Bernhardt, P

Halt, K

Kazlauskas, RJ

机构：

[1] Univ Minnesota, Dept Biochem Mol Biol & Biophys, St Paul, MN 55108 USA

[2] Univ Minnesota, Ctr Microbial & Plant Genom, St Paul, MN 55108 USA

[3] AlbaNova Univ Ctr, Royal Inst Technol, Sch Biotechnol, Dept Biochem, S-10691 Stockholm, Sweden

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2005年 / 44卷 / 18期

关键词：

enzyme catalysis; hydrolases; molecular modeling; mutagenesis; peroxides;

D O I：

10.1002/anie.200463006

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Chemical Equation Presented) Changing substrates: A mutation that forms a cis-proline-peptide bond in a loop structure close to the active site of an aryl esterase from Pseudomonas fluorescens converts the enzyme into a perhydrolase (see picture). The switch in activity is explained by a new hydrogen bond formed between a backbone carbonyl oxygen atom and the peroxy deacylation intermediate. © 2005 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：2742 / 2746

页数：5