Article
Structure of a mutant of tyrosyl-tRNA synthetase with enhanced catalytic properties.
Nature - 1 Jan 2000
Brown K A, Brick P, Blow D M
Abstract excerpt
One surprising outcome of applying the techniques of protein engineering to the enzyme tyrosyl-transfer RNA synthetase was that the enzyme's activity could actually be increased by a specific sequence change. In particular, altering residue threonine 51 to a proline (mutant TP51) increased the enzyme's affinity for tyrosyl adenylate complexes. The non-additive effect of combining the TP51 mutation with a second...
Topics
- Adenosine Monophosphate
- Amino Acid Sequence
- Amino Acyl-tRNA Synthetases
- Catalysis
- Geobacillus stearothermophilus
- Histidine
- Mutation
- Protein Conformation
- Structure-Activity Relationship
- Thermodynamics
- Threonine