Article
Effects of noncatalytic residue mutations on substrate specificity and ligand binding of Thermobifida fusca endocellulase cel6A.
European journal of biochemistry - 1 Jan 2000
Zhang S, Barr B K, Wilson D B
Abstract excerpt
The availability of a high-resolution structure of the Thermobifida fusca endocellulase Cel6A catalytic domain makes this enzyme ideal for structure-based efforts to engineer cellulases with high activity on native cellulose. In order to determine the role of conserved, noncatalytic residues in cellulose hydrolysis, 14 mutations of six conserved residues in or near the Cel6A active-site cleft were studied for...
Topics
- Actinomycetales
- Amino Acid Substitution
- Binding Sites
- Catalytic Domain
- Cellulase
- Cellulose
- Cellulose 1,4-beta-Cellobiosidase
- Conserved Sequence
- Dimerization
- Enzyme Stability
- Escherichia coli
- Hydrogen Bonding
- Hydrogen-Ion Concentration
- Kinetics