Glutamate-tRNAGln ligase

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

ATP + L-glutamate + tRNAGlx $\rightleftharpoons$ 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, specifically 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 nondiscriminating glutamyl-tRNA synthetase. This enzyme participates in glutamate metabolism.

[edit] References

IUBMB entry for 6.1.1.24
BRENDA references for 6.1.1.24 (Recommended.)
PubMed references for 6.1.1.24
PubMed Central references for 6.1.1.24
Google Scholar references for 6.1.1.24
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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: 5227–37. doi:10.1093/emboj/17.17.5227. PMID 9724658.
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: 459–65. PMID 9749534.