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Correlation between cellulose binding and activity of cellulose‐binding domain mutants of Humicola grisea cellobiohydrolase 1
Author(s) -
Takashima Shou,
Ohno Mitsuhiro,
Hidaka Makoto,
Nakamura Akira,
Masaki Haruhiko,
Uozumi Takeshi
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.11.068
Subject(s) - cellulose , cellulase , tryptophan , residue (chemistry) , mutant , chemistry , thermophile , tyrosine , biochemistry , binding site , aromatic amino acids , stereochemistry , amino acid , enzyme , gene
The cellulose‐binding domains (CBDs) of fungal cellulases interact with crystalline cellulose through their hydrophobic flat 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 flat surface, while tryptophan is the best residue in the two outer positions.