Serine-tRNA ligase

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


 * ATP + L-serine + tRNASer $$\rightleftharpoons$$ AMP + diphosphate + L-seryl-tRNASer

The 3 substrates of this enzyme are ATP, L-serine, and tRNA(Ser), whereas its 3 products are AMP, diphosphate, and L-seryl-tRNA(Ser).

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-serine:tRNASer 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.

Structural studies
As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , , , , , , and.