In enzymology, a serineâÂÂtRNA ligase () is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are ATP, -serine, and tRNA, whereas its 3 products are AMP, diphosphate, and -seryl-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 -serine:tRNA ligase (AMP-forming). Other names in common use include seryl-tRNA synthetase, SerRS, seryl-transfer ribonucleate synthetase, seryl-transfer RNA synthetase, seryl-transfer ribonucleic acid synthetase, and serine translase. This enzyme participates in glycine, serine and threonine metabolism, and aminoacyl-tRNA biosynthesis.
As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , and .