Glutamate—tRNA(Gln) ligase

In enzymology, a glutamate-tRNAGln ligase (EC 6.1.1.24) is an enzyme that catalyzes the chemical reaction

ATP + L-glutamate + tRNAGlx AMP + diphosphate + glutamyl-tRNAGlx

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

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:tRNAGlx ligase (AMP-forming). This enzyme is also called glutamyl-tRNA synthetase. This enzyme participates in glutamate metabolism.

References

• Ibba M, Soll D (2000). "Aminoacyl-tRNA synthesis". Annu. Rev. Biochem. 69: 617–50. doi:10.1146/annurev.biochem.69.1.617. PMID 10966471. 
• Schmitt E, Moulinier L, Fujiwara S, Imanaka T, Thierry JC, Moras D (1998). "Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: archaeon specificity and catalytic mechanism of adenylate formation". EMBO J. 17 (17): 5227–37. doi:10.1093/emboj/17.17.5227. PMC 1170850. PMID 9724658. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170850. 
• Kim SI, Soll D (1998). "Major identity element of glutamine tRNAs from Bacillus subtilis and Escherichia coli in the reaction with B. subtilis glutamyl-tRNA synthetase". Mol. Cells. 8 (4): 459–65. PMID 9749534.