Substrate distortion by a lichenase highlights the different conformational itineraries harnessed by related glycoside hydrolases

被引：41

作者：

Money, Victoria A.

Smith, Nicola L.

Scaffidi, Adrian

Stick, Robert V.

Gilbert, Harry J.

Davies, Gideon J. ^{[1
]}

机构：

[1] Univ York, Dept Chem, York Struct Biol Lab, York YO10 5DD, N Yorkshire, England

[2] Univ Newcastle Upon Tyne, Inst Cell & Mol Biosci, Newcastle Upon Tyne NE2 4HH, Tyne & Wear, England

[3] Univ Western Australia, Sch Biomed Biomol & Chem Sci, Crawley, WA 6009, Australia

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2006年 / 45卷 / 31期

基金：

英国生物技术与生命科学研究理事会;

关键词：

drug design; enzyme models; glycosides; reaction pathways; transition states;

D O I：

10.1002/anie.200600802

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Chemical Equation Presented) Pick-a-path: A series of enzymatic snap-shots along the reaction coordinate of a lichenase (specific for gluco-configured substrates) demonstrates that this enzyme uses a different reaction pathway, featuring a 1S3→4H3→ 4C1 migration, to that previously observed for the closely related mannanases. © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：5136 / 5140

页数：5

共 32 条

[1] Structural insights into the catalytic mechanism of Trypanosoma cruzi trans-sialidase [J].