Article
Analysis of the role of the KMSKS loop in the catalytic mechanism of the tyrosyl-tRNA synthetase using multimutant cycles.
Biochemistry - 18 Apr 1995
First E A, Fersht A R
Abstract excerpt
A mobile loop in tyrosyl-tRNA synthetase, which corresponds to the KMSKS signature sequence of class I aminoacyl-tRNA synthetases, destabilizes the E.Tyr.ATP complex but stabilizes the following E.[Tyr-ATP]not equal to transition state for the formation of E.Tyr-AMP. Three amino acid residues in the mobile loop, K230, K233, and T234, are known to be primarily responsible for these effects. We now analyze the...
Topics
- Adenosine Triphosphate
- Amino Acid Sequence
- Base Sequence
- Catalysis
- Enzyme Stability
- Geobacillus stearothermophilus
- Kinetics
- Models, Chemical
- Molecular Sequence Data
- Mutation
- Protein Conformation