Article
Cocrystallization of a mutant aspartate aminotransferase with a C5-dicarboxylic substrate analog: structural comparison with the enzyme-C4-dicarboxylic analog complex.
Journal of biochemistry - 1 Feb 2000
Oue S, Okamoto A, Yano T, Kagamiyama H
Abstract excerpt
A mutant Escherichia coil aspartate aminotransferase with 17 amino acid substitutions (ATB17), previously created by directed evolution, shows increased activity for beta-branched amino acids and decreased activity for the native substrates, aspartate and glutamate. A new mutant (ATBSN) was generated by changing two of the 17 mutated residues back to the original ones. ATBSN recovered the activities for aspartate...
Topics
- Aspartate Aminotransferases
- Binding Sites
- Catalytic Domain
- Crystallization
- Crystallography, X-Ray
- Glutarates
- Kinetics
- Maleates
- Models, Molecular
- Mutation
- Protein Conformation
- Spectrum Analysis
- Substrate Specificity
- Succinic Acid