Interaction between cellohexaose and cellulose binding domains from Trichoderma reesei cellulases

被引：52

作者：

Mattinen, ML ^{[1
]}

Linder, M ^{[1
]}

Teleman, A ^{[1
]}

Annila, A ^{[1
]}

机构：

[1] VTT, BIOTECHNOL & FOOD RES, FIN-02044 ESPOO, FINLAND

来源：

FEBS LETTERS | 1997年 / 407卷 / 03期

基金：

芬兰科学院;

关键词：

NMR spectroscopy; Trichoderma reesei cellulase; cellulose binding domain; protein-ligand interaction;

D O I：

10.1016/S0014-5793(97)00356-6

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：

Most Trichoderma reesei cellulases consist of a catalytic and a cellulose binding domain (CBD) joined by a linker. We have used cellohexaose as a model compound for the glucose chain to investigate the interaction between the soluble enzyme and cellulose, The binding of cellohexaose to family I CBDs was studied by NMR spectroscopy. CBDs cause line broadening effects and decreasing T-2 relaxation times for certain cellohexaose resonances, whereas there are no effects in the presence of a mutant which binds weakly to cellulose. Yet it remains uncertain how well the soluble cellooligosaccharide mimics the binding of CBD to the cellulose. (C) 1997 Federation of European Biochemical Societies.

引用

页码：291 / 296

页数：6

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