Aspartate—tRNA(Asn) ligase

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

ATP + L-aspartate + tRNAAsx 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, to be specific 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.

References

• 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 (17): 5227–37. doi:10.1093/emboj/17.17.5227. PMC 1170850. PMID 9724658. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170850. 
• 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 (22): 12832–7. doi:10.1073/pnas.95.22.12832. PMC 23616. PMID 9789000. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=23616.