EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
6.1.1.9 | 744659 |
A conserved proline triplet in Val-tRNA synthetase and the origin of elongation factor P |
Cell Rep. |
9 |
476-483 |
2014 |
Escherichia coli |
25310979 |
6.1.1.9 | 745020 |
Caenorhabditis elegans glp-4 encodes a valyl aminoacyl tRNA synthetase |
G3 (Bethesda) |
5 |
2719-2728 |
2015 |
Caenorhabditis elegans |
26464357 |
6.1.1.9 | 744977 |
Sub-cellular localization and complex formation by aminoacyl-tRNA synthetases in cyanobacteria evidence for interaction of membrane-anchored ValRS with ATP synthase |
Front. Microbiol. |
7 |
857 |
2016 |
Nostoc sp. PCC 7120 = FACHB-418 |
27375579 |
6.1.1.9 | 746112 |
White panicle1, a Val-tRNA synthetase regulating chloroplast ribosome biogenesis in rice, is essential for early chloroplast development |
Plant Physiol. |
170 |
2110-2123 |
2016 |
Oryza sativa Japonica Group |
26839129 |
6.1.1.9 | 542 |
A novel thiol-dependent arsenite-sensitive valyl-tRNA synthetase activity from yeast |
J. Biol. Chem. |
258 |
2112-2114 |
1983 |
Saccharomyces cerevisiae |
6337152 |
6.1.1.9 | 527 |
Affinity labeling of aminoacyl-tRNA synthetases with adenosine triphosphopyridoxal. Probing the Lys-Met-Ser-Lys-Ser signature sequence as the ATP-binding site in Escherichia coli methionyl- and valyl-tRNA synthetases |
Biochemistry |
29 |
11266-11273 |
1990 |
Escherichia coli |
2271710 |
6.1.1.9 | 714322 |
Aminoacyl-tRNA synthetases are multivalent suppressors of defects due to human equivalent mutations in yeast mt tRNA genes |
Biochim. Biophys. Acta |
1803 |
1050-1057 |
2010 |
Homo sapiens |
20471434 |
6.1.1.9 | 673963 |
Basic faced alpha-helices are widespread in the peptide extensions of the eukaryotic aminoacyl-tRNA synthetases |
In Silico Biol. |
6 |
259-273 |
2006 |
Saccharomyces cerevisiae |
16922690 |
6.1.1.9 | 673963 |
Basic faced alpha-helices are widespread in the peptide extensions of the eukaryotic aminoacyl-tRNA synthetases |
In Silico Biol. |
6 |
259-273 |
2006 |
Homo sapiens |
16922690 |
6.1.1.9 | 673963 |
Basic faced alpha-helices are widespread in the peptide extensions of the eukaryotic aminoacyl-tRNA synthetases |
In Silico Biol. |
6 |
259-273 |
2006 |
Takifugu rubripes |
16922690 |