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Glutamate–tRNA ligase

Class of enzymes From Wikipedia, the free encyclopedia

In enzymology, a glutamate–tRNA ligase (EC 6.1.1.17) 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 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.


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