Article
Amino acid substrate specificity of Escherichia coli phenylalanyl-tRNA synthetase altered by distinct mutations.
Journal of molecular biology - 5 Nov 1991
Kast P, Hennecke H
Abstract excerpt
Neither the tertiary structure nor the location of active sites are known for phenylalanyl-tRNA synthetase (PheRS; alpha 2 beta 2 structure), a member of class II aminoacyl-tRNA synthetases. In an attempt to detect the phenylalanine (Phe) binding site, two Escherichia coli PheRS mutant strains (p...
Topics
- Acylation
- Amino Acid Sequence
- Amino Acids
- Base Sequence
- Cloning, Molecular
- DNA, Bacterial
- Escherichia coli
- Genetic Complementation Test
- Kinetics
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Phenylalanine-tRNA Ligase
- Sequence Alignment
- Substrate Specificity