In enzymology, a glutamate—tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + L-glutamate + tRNAGlu AMP + diphosphate + L-glutamyl-tRNAGlu
The 3 substrates of this enzyme are ATP, L-glutamate, and tRNA(Glu), whereas its 3 products are AMP, diphosphate, and L-glutamyl-tRNA(Glu).
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-glutamate:tRNAGlu ligase (AMP-forming). Other names in common use include glutamyl-tRNA synthetase, glutamyl-transfer ribonucleate synthetase, glutamyl-transfer RNA synthetase, glutamyl-transfer ribonucleic acid synthetase, glutamate-tRNA synthetase, and glutamic acid translase. This enzyme participates in 3 metabolic pathways: glutamate metabolism, porphyrin and chlorophyll metabolism, and aminoacyl-trna biosynthesis.
Structural studies
As of late 2007, 16 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , and .