Journal
FEBS LETTERS
Volume 581, Issue 30, Pages 5891-5896Publisher
WILEY
DOI: 10.1016/j.febslet.2007.11.068
Keywords
cellulose-binding domain; cellobiohydrolase; crystalline cellulose; Humicola grisea
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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.
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