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tyrosinyl-5'-AMP

Known as: (S)-5'-adenylic acid, mono(2-amino-3-(4-hydroxyphenyl)propyl) ester, adenylyl-tyrosine, tyrosyl adenylate 
National Institutes of Health

Related topics

Related topics

3 relations

Broader (2)

Adenosine MonophosphateTyrosine
analogs & derivatives

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
1988
Highly Cited
1988
Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: a mobile loop envelopes the transition state in an induced-fit…
Site-directed mutagenesis of the tyrosyl-tRNA synthetase followed by kinetic studies has shown that residues which are distant… 
Highly Cited
1987
Highly Cited
1987
Structure-activity relationships in engineered proteins: analysis of use of binding energy by linear free energy relationships.
The activity of mutant enzymes can be analyzed quantitatively by structure-activity relationships in a manner analogous to Br… 
Highly Cited
1986
Highly Cited
1986
A model of synthetase/transfer RNA interaction as deduced by protein engineering
The recognition of transfer-RNA by their cognate aminoacyl-tRNA synthetases is the crucial step in the translation of the genetic… 
Highly Cited
1986
Highly Cited
1986
Quantitative analysis of structure–activity relationships in engineered proteins by linear free-energy relationships
Protein engineering is being used increasingly to study the fine details of the structure and activity of enzymes. How can small… 
Highly Cited
1985
Highly Cited
1985
Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering.
The principal catalytic factor in the activation of tyrosine by the tyrosyl-tRNA synthetase is found to be improved binding of… 
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Highly Cited
1982
Highly Cited
1982
Tyrosyl-tRNA synthetase forms a mononucleotide-binding fold.
Abstract Tyrosyl-tRNA synthetase from Bacillus stearothermophilus is a dimeric molecule of approximately 90,000 M r . The crystal… 
Highly Cited
1976
Highly Cited
1976
Mechanism of aminoacylation of tRNA. Proof of the aminoacyl adenylate pathway for the isoleucyl- and tyrosyl-tRNA synthetases from Escherichia coli K12.
The following observations show that the formation of isoleucyl-tRNA catalyzed by the isoleucyl-tRNA synthetase from Escherichia… 
Highly Cited
1975
Highly Cited
1975
Demonstration of two reaction pathways for the aminoacylation of tRNA. Application of the pulsed quenched flow technique.
A rapid mixing and quenching device is described which operates efficiently in the range of 150 msec to several minutes as well… 
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Highly Cited
1975
Highly Cited
1975
Tyrosyl-tRNA synthetase from Escherichia coli. Stoichiometry of ligand binding and half-of-the-sites reactivity in aminoacylation.
The tyrosyl-tRNA synthetase from Escherichia coli binds only 1 mol of tRNA, tyrosine, and tyrosyl adenylate per mol of enzyme… 
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Highly Cited
1975
Highly Cited
1975
Ligand binding and enzymic catalysis coupled through subunits in tyrosyl-tRNA synthetase.
The interaction of the tyrosyl-tRNA synthetase from Bacillus stearothermophilus with its substrates in the aminoacyl adenylation… 
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