1. Structural studies

2. References

In enzymology, a glutamate-tRNA ligase ({{EC number|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 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 {{PDB link|1FYJ}}, {{PDB link|1G59}}, {{PDB link|1J09}}, {{PDB link|1N75}}, {{PDB link|1N77}}, {{PDB link|1N78}}, {{PDB link|2CFO}}, {{PDB link|2CUZ}}, {{PDB link|2CV0}}, {{PDB link|2CV1}}, {{PDB link|2CV2}}, {{PDB link|2DXI}}, {{PDB link|2HRA}}, {{PDB link|2HRK}}, {{PDB link|2HSM}}, and {{PDB link|2O5R}}.

References

• {{cite journal | vauthors = Ravel JM, Wang S, Heinemeyer C, Shive W | year = 1965 | title = Glutamyl and glutaminyl ribonucleic acid synthetases of Escherichia coli W. Separation, properties, and stimulation of adenosine triphosphate-pyrophosphate exchange by acceptor ribonucleic acid | journal = J. Biol. Chem. | volume = 240 | pages = 432–438 | pmid=14253448}}

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