We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Correlation between cellulose binding and activity of cellulose-binding domain mutants of Humicola grisea cellobiohydrolase 1
- Authors
Takashima, Shou; Ohno, Mitsuhiro; Hidaka, Makoto; Nakamura, Akira; Masaki, Haruhiko; Uozumi, Takeshi
- Abstract
Abstract: 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.
- Subjects
CELLULOSE; AMINO acids; CELLULOSE 1,4-beta-cellobiosidase; THERMOPHILIC microorganisms
- Publication
FEBS Letters, 2007, Vol 581, Issue 30, p5891
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2007.11.068