Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

6.1.1.17: glutamate-tRNA ligase

This is an abbreviated version!
For detailed information about glutamate-tRNA ligase, go to the full flat file.

Word Map on EC 6.1.1.17

Reaction

ATP
+
L-glutamate
 +
tRNAGlu
=
AMP
 +
diphosphate
 +
L-glutamyl-tRNAGlu

Synonyms

bifunctional aminoacyl-tRNA synthetase, bifunctional glutamate/proline-tRNA ligase, D-GluRS, discriminating GluRS, EC 2.7.2.13, Ec-GluRS, EPRS, ERS, Ers2, GltX, GluRS, GluRS1, GluRS2, GluRSAt, Glutamate--tRNA ligase, Glutamate-tRNA synthetase, Glutamic acid translase, Glutamic acid tRNA ligase, Glutaminyl-tRNA synthetase, Glutamyl tRNA synthetase, glutamyl-prolyl tRNA synthetase, glutamyl-prolyl-tRNA synthetase, glutamyl-Q tRNAASp synthetase, Glutamyl-transfer ribonucleate synthetase, Glutamyl-transfer ribonucleic acid synthetase, Glutamyl-transfer RNA synthetase, Glutamyl-tRNA synthetase, glutamyl-tRNAsynthetase, GtS, More, P85, surface-exposed glutamyl tRNA synthetase, TM1351, tRNA modifying enzyme, YadB

ECTree

     6 Ligases
         6.1 Forming carbon-oxygen bonds
             6.1.1 Ligases forming aminoacyl-tRNA and related compounds
                6.1.1.17 glutamate-tRNA ligase

Expression

Expression on EC 6.1.1.17 - glutamate-tRNA ligase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
construction of an anticodon-binding domain truncated GluRS catalytic domain and a chimeric protein, constructed from the catalytic domain of Escherichia coli GluRS and the anticodon-binding domain of glutaminyl-tRNA synthetase GlnRS. Both proteins discriminate against tRNAGln. In addition to the anticodon-binding domain, tRNAGln discriminatory elements may be present in the catalytic domain in Escherichia coli GluRS as well
-
requirement for sensing by the immune system in the induction of EPRS expression during infection with an RNA virus
requirement for sensing by the immune system in the induction of EPRS expression during infection with an RNA virus, VSV Indiana strain
the translation of the glutamyl-prolyl-tRNA synthetase gene EPRS is enhanced in response to phosphorylated eukaryotic initiation factor 2, eIF2alpha-P, mechanism of translation control involving increased translation initiation stringency during stress-induced eIF2alpha-P, facilitated ribosome bypass of upstream ORFs, allowing for increased translation of the EPRS coding region, overview. Both halofuginone and thapsigargin treatment result in a 2.5fold induction of EPRS expression
-
UUG1 and CUG2 are overall repressing elements in EPRS translation control
-