In a previous study, a mutant of tyrosyl-tRNA synthetase in which a threonine residue
(Thr51) was converted to proline dramatically improved the aff inity of the enzyme for its ATP …

Anthony J. Wilkinson, Alan R. Fersht,* David M. Blow, and Greg Winter* abstract:
Oligodeoxynucleotide-directed mutagenesis has been used on the gene of tyrosyl-tRNA …

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 …

Tyrosyl-tRNA synthetase from Bacillus stearothermophilus is a dimeric molecule of
approximately 90,000 M r. The crystal structure originally reported by Irwin et al.(1976) has …

The crystal structure of a deletion mutant of tyrosyl-tRNA synthetase from Bacillus
stearothermophilus has been determined at 2.5 Å resolution using molecular replacement …

Department of Chemistry, Imperial College of Science and Technology, London SW7 2 AY,
UK Received August 6, 1987; Revised Manuscript Received September 15, 1987 abstract …

The tyrosyl-tRNA synthetase from Escherichia coli binds only 1 mol of tRNA, tyrosine, and
tyrosyl ade-nylate per mol of enzyme dimer. However, like the enzyme from Bacillus …

Department of Chemistry, Imperial College of Science and Technology, LondonSW7 2AY,
UK Received August 14, 1985 abstract: The utilization of enzyme-substrate binding energy …

The structure of a recombinant protein, TyrRS (Δ4), corresponding to the anticodon arm
binding domain of Bacillus stearothermophilus tyrosyl-tRNA synthetase, has been solved …

With the technical assistance of Jeremy Ashford abstract: The dimeric tyrosyl-tRNA
synthetase from Bacillus stearothermophiluswhich binds (tightly) only one tyrosyl adenylate …