Aspartate-tRNA ligase

In enzymology, an aspartate-tRNA ligase is an enzyme that catalyzes the chemical reaction


 * ATP + L-aspartate + tRNAAsp $$\rightleftharpoons$$ AMP + diphosphate + L-aspartyl-tRNAAsp

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

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:tRNAAsp ligase (AMP-forming). Other names in common use include aspartyl-tRNA synthetase, aspartyl ribonucleic synthetase, aspartyl-transfer RNA synthetase, aspartic acid translase, aspartyl-transfer ribonucleic acid synthetase, and aspartyl ribonucleate synthetase. This enzyme participates in alanine and aspartate metabolism and aminoacyl-trna biosynthesis.

Structural studies
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , , , and.