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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

General Stability

General Stability on EC 6.1.1.17 - glutamate-tRNA ligase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Mycobacterium tuberculosis GluRS is significantly more sensitive than the Escherichia coli form to tryptic and chymotryptic limited proteolysis. Chymotrypsin-sensitive sites are found in the predicted tRNA stem contact domain next to the ATP binding site. Enzyme is fully protected from proteolysis by ATP and glutamol-AMP
no stabilization by various sulfydryl reagents, glycerol and glutamic acid
-
tRNAGlu in presence of Mg2+ protects against heat inactivation, Mg2+ alone is much less effective
-