IDENTIFICATION OF AN ESSENTIAL GLUTAMATE RESIDUE IN THE ACTIVE-SITE OF ENDOGLUCANASE-III FROM TRICHODERMA-REESEI

被引：45

作者：

MACARRON, R

VANBEEUMEN, J

HENRISSAT, B

DELAMATA, I

CLAEYSSENS, M

机构：

[1] STATE UNIV GHENT,FAC WETENSCHAPPEN,VAKGRP BIOCHEM FYSIOL MICROBIOL,B-9000 GHENT,BELGIUM

[2] UNIV COMPLUTENSE,FAC CIENCIAS BIOL,DEPT BIOQUIM,E-28040 MADRID,SPAIN

[3] CTR RECH MACROMOLEC VEGETALES,CNRS,F-38041 GRENOBLE,FRANCE

来源：

FEBS LETTERS | 1993年 / 316卷 / 02期

关键词：

AFFINITY LABELING; CELLULASE; ENDOGLUCANASE-III; TRICHODERMA-REESEI; EPOXY-ALKYL CELLOBIOSIDE;

D O I：

10.1016/0014-5793(93)81202-B

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

n-Propyl, n-butyl and n-pentyl beta-cellobiosides with a reactive omega-epoxide in their aglycon completely and irreversibly inactivate endoglucanase III from Trichoderma reesei. The pentyl derivative was found to be most effective. From these affinity labeling experiments evidence was found for the implication of Glu329 in the reaction mechanism. This is discussed in relation to other structural/functional data known for endoglucanase III and several other family A glycanases.

引用

页码：137 / 140

页数：4

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