Correlation between cellulose binding and activity of cellulose-binding domain mutants of Humicola grisea cellobiohydrolase 1

被引：38

作者：

Takashima, Shou ^{[1
]}

Ohno, Mitsuhiro ^{[1
]}

Hidaka, Makoto ^{[1
]}

Nakamura, Akira ^{[1
]}

Masaki, Haruhiko ^{[1
]}

机构：

[1] Univ Tokyo, Grad Sch Agr & Life Sci, Dept Biotechnol, Bunkyo Ku, Tokyo 1138657, Japan

来源：

FEBS LETTERS | 2007年 / 581卷 / 30期

关键词：

cellulose-binding domain; cellobiohydrolase; crystalline cellulose; Humicola grisea;

D O I：

10.1016/j.febslet.2007.11.068

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：

The cellulose-binding domains (CBDs) of fungal cellulases interact with crystalline cellulose through their hydrophobic. at surface formed by three conserved aromatic amino acid residues. To analyze the functional importance of these residues, we constructed CBD mutants of cellobiohydrolase 1 (CBH1) of the thermophilic fungus Humicola grisea, and examined their cellulose-binding ability and enzymatic activities. High activity on crystalline cellulose correlated with high cellulose-binding ability and was dependent on the combination and configuration of the three aromatic residues. Tyrosine works best in the middle of the. at surface, while tryptophan is the best residue in the two outer positions. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：5891 / 5896

页数：6

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