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Glutamate–tRNA ligase

In enzymology, a glutamate–tRNA ligase () is an enzyme that catalyzes the chemical reaction

ATP + -glutamate + tRNA AMP + diphosphate + -glutamyl-tRNA

The 3 substrates of this enzyme are ATP, -glutamate, and tRNA, whereas its 3 products are AMP, diphosphate, and -glutamyl-tRNA.

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 -glutamate:tRNA 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 .

References