In enzymology, a glutamate–tRNA ligase (EC 6.1.1.17) is an enzyme that catalyzes the chemical reaction
ATP + L-glutamate + tRNAGlu ⇌ {\displaystyle \rightleftharpoons } AMP + diphosphate + L-glutamyl-tRNAGlu The 3 substrates of this enzyme are ATP, L-glutamate, and tRNAGlu, whereas its 3 products are AMP, diphosphate, and L-glutamyl-tRNAGlu. 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 PDB: 1FYJ, PDB: 1G59, PDB: 1J09, PDB: 1N75, PDB: 1N77, PDB: 1N78, PDB: 2CFO, PDB: 2CUZ, PDB: 2CV0, PDB: 2CV1, PDB: 2CV2, PDB: 2DXI, PDB: 2HRA, PDB: 2HRK, PDB: 2HSM, and PDB: 2O5R.
References
Ravel JM, Wang S, Heinemeyer C, Shive W (1965). "Glutamyl and glutaminyl ribonucleic acid synthetases of Escherichia coli W. Separation, properties, and stimulation of adenosine triphosphate-pyrophosphate exchange by acceptor ribonucleic acid". J. Biol. Chem. 240: 432–438. doi:10.1016/S0021-9258(18)97667-2. PMID 14253448.
