Article
A large increase in enzyme-substrate affinity by protein engineering.
Nature - 1 Jan 2000
Wilkinson A J, Fersht A R, Blow D M, Carter P, Winter G
Abstract excerpt
A single point mutation has been engineered in the tyrosyl-tRNA synthetase that improves its affinity (KM) for its substrate ATP by a factor of 100. In the crystal structure of the tyrosyl tRNA synthetase (of Bacillus stearothermophilus), the side-chain hydroxyl of Thr 51 appears to make a weak hydrogen bond with the AMP moiety of the substrate intermediate, tyrosyl adenylate. In the absence of substrate,...
Topics
- Amino Acyl-tRNA Synthetases
- Binding Sites
- Catalysis
- Genes
- Geobacillus stearothermophilus
- Hydrogen Bonding
- Kinetics
- Mutation
- Protein Binding
- Structure-Activity Relationship
- Tyrosine-tRNA Ligase