In enzymology, an aspartateâÂÂtRNA ligase () is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are ATP, -aspartate, and tRNA, whereas its 3 products are AMP, diphosphate, and -aspartyl-tRNA.
This enzyme belongs to the family of ligases, to be specific those forming carbonâÂÂoxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is -aspartate:tRNA 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.
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , and .