Glutamate—tRNA ligase

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 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 1FYJ, 1G59, 1J09, 1N75, 1N77, 1N78, 2CFO, 2CUZ, 2CV0, 2CV1, 2CV2, 2DXI, 2HRA, 2HRK, 2HSM, and 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. PMID 14253448.

This page was last edited on 26 August 2023, at 14:17