Interaction between cellohexaose and cellulose binding domains from Trichoderma reesei cellulases

FEBS Letters

Mattinen, Maija-Liisa²  Teleman, Anita²  Annila, Arto²  Linder, Markus¹ 

[1] VTT, Biotechnology and Food Research, Box 1500, FIN-02044 VTT, Finland;VTT, Chemical Technology, Box 1400, FIN-02044 VTT, Finland

关键词: NMR spectroscopy;    Trichoderma reesei cellulase;    Cellulose binding domain;    Protein-ligand interaction;    CBD;    cellulose binding domain;    CBHI;    cellobiohydrolase I;    CBHII;    cellobiohydrolase II;    EGI;    endoglucanase I;    Y31A;    CBDCBHI where tyrosine 31 is replaced by alanine;   

DOI  :  10.1016/S0014-5793(97)00356-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown