Aspartate-tRNAAsn ligase

From Wikipedia, the free encyclopedia

In enzymology, an aspartate-tRNAAsn ligase (EC 6.1.1.23) is an enzyme that catalyzes the chemical reaction

ATP + L-aspartate + tRNAAsx $\rightleftharpoons$ AMP + diphosphate + aspartyl-tRNAAsx

The 3 substrates of this enzyme are ATP, L-aspartate, and tRNAAsx, whereas its 3 products are AMP, diphosphate, and aspartyl-tRNAAsx.

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-aspartate:tRNAAsx ligase (AMP-forming). This enzyme is also called nondiscriminating aspartyl-tRNA synthetase. This enzyme participates in alanine and aspartate metabolism.

[edit] References

IUBMB entry for 6.1.1.23
BRENDA references for 6.1.1.23 (Recommended.)
PubMed references for 6.1.1.23
PubMed Central references for 6.1.1.23
Google Scholar references for 6.1.1.23
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: 5227–37. doi:10.1093/emboj/17.17.5227. PMID 9724658.
Becker HD, Kern D (1998). "Thermus thermophilus: a link in evolution of the tRNA-dependent amino acid amidation pathways". Proc. Natl. Acad. Sci. U. S. A. 95: 12832–7. doi:10.1073/pnas.95.22.12832. PMID 9789000.