EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
6.1.1.19 | 126 |
Isolation and electron microscopic characterization of the high molecular mass aminoacyl-tRNA synthetase complex from murine erythroleukemia cells |
J. Biol. Chem. |
264 |
15043-15051 |
1989 |
Mus musculus |
2768252 |
6.1.1.19 | 127 |
A role for lipids in the functional and structural properties of the rat liver aminoacyl-tRNA synthetase complex |
J. Biol. Chem. |
263 |
18891-18896 |
1988 |
Rattus norvegicus |
3058690 |
6.1.1.19 | 257 |
Arginyl-tRNA synthetase from brewer's yeast. Purification, properties, and steady-state mechanism |
Eur. J. Biochem. |
130 |
517-524 |
1983 |
Saccharomyces pastorianus |
6337851 |
6.1.1.19 | 257 |
Arginyl-tRNA synthetase from brewer's yeast. Purification, properties, and steady-state mechanism |
Eur. J. Biochem. |
130 |
517-524 |
1983 |
Saccharomyces pastorianus C836 |
6337851 |
6.1.1.19 | 258 |
Cloning and chracterization of cDNA encoding a human arginyl-tRNA synthetase |
Gene |
27 |
347-350 |
1995 |
Homo sapiens |
7590355 |
6.1.1.19 | 259 |
The NH2-terminal extension of rat liver arginyl-tRNA synthetase is responsible for its hydrophobic properties |
Biochem. Biophys. Res. Commun. |
180 |
702-708 |
1991 |
Rattus norvegicus |
1953742 |
6.1.1.19 | 260 |
Arginyl-tRNA synthetase from yeast. Discrimination between 20 amino acids in aminoacylation of tRNAArg-C-C-A and tRNAArg-C-C-A(3'NH2) |
Eur. J. Biochem. |
186 |
535-541 |
1989 |
Saccharomyces cerevisiae |
2691248 |
6.1.1.19 | 261 |
Comparison of the thermolability and hydrophobic properties of high- and low-molecular-weight forms of rabbit liver arginyl-tRNA synthetase |
Mol. Cell. Biochem. |
86 |
125-133 |
1989 |
Oryctolagus cuniculus |
2770710 |
6.1.1.19 | 262 |
Degradation of the arginyl-tRNA synthetase protein during purification by affinity chromatography on immobilized total tRNA and immobilized tRNA, specific for arginyl-tRNA synthetase |
Biochem. Mol. Biol. Int. |
31 |
219-228 |
1993 |
Mus musculus |
8275012 |
6.1.1.19 | 263 |
Structure-function relationship of arginyl-tRNA synthetase from Escherichia coli: isolation and characterization of the argS mutation MA5002 |
Nucleic Acids Res. |
18 |
1475-1479 |
1990 |
Escherichia coli |
2183195 |