The difference in affinity between two fungal cellulose‐binding domains is dominated by a single amino acid substitution

FEBS Letters

Reinikainen, Tapani¹  Lindeberg, Gunnar³  Pettersson, Göran²  Teeri, Tuula T.¹  Linder, Markus¹ 

[1] VTT Biotechnology and Food Research, Box 1500, FIN-02044 VTT, Espoo, Finland;Department of Biochemistry, University of Uppsala, Box 576, S-751 23 Uppsala, Sweden;Department of Medical and Physiological Chemistry, University of Uppsala, Box 575, S-751 23 Uppsala, Sweden

关键词: Cellulose-binding domain;    Synthetic peptide;    Protein-carbohydrate interaction;    Cellulase;    Trichoderma reesei;    CBD;    cellulose-binding domain;    CBHI;    cellobiohydrolase I;    EGI;    endoglucanase I;   

DOI  :  10.1016/0014-5793(95)00961-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Cellulose-binding domains (CBDs) form distinct functional units of most cellulolytic enzymes. We have compared the cellulose-binding affinities of the CBDs of cellobiohydrolase I (CBHI) and endoglucanase I (EGI) from the fungus Trichoderma reesei. The CBD of EGI had significantly higher affinity than that of CBHI. Four variants of the CBHI CBD were made in order to identify the residues responsible for the increased affinity in EGI. Most of the difference could be ascribed to a replacement of a tyrosine by a tryptophan on the flat cellulose-binding face.

【 授权许可】

Unknown