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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

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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
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… 
Highly Cited
1984
Highly Cited
1984
Fast kinetic study of yeast phenylalanyl-tRNA synthetase: role of tRNAPhe in the discrimination between tyrosine and phenylalanine.
An extensive study of the discrimination between phenylalanine and tyrosine by yeast phenylalanyl-tRNA synthetase was carried out… 
Highly Cited
1983
Highly Cited
1983
Deletion mutagenesis using an ‘M13 splint’: the N‐terminal structural domain of tyrosyl‐tRNA synthetase (B. stearothermophilus) catalyses the formation of tyrosyl adenylate.
The X‐ray crystallographic structure of tyrosyl‐tRNA synthetase (TyrTS) comprises only the N‐terminal 320 amino acids of the… 
Highly Cited
1982
Highly Cited
1982
Tyrosyl-tRNA synthetase forms a mononucleotide-binding fold.
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… 
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… 
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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