In enzymology, a serine–tRNA ligase () is an enzyme that catalyzes the chemical reaction
ATP + -serine + tRNA AMP + diphosphate + -seryl-tRNA
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 carbon–oxygen 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.
Structural studies
As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , and .
See also Serine–tRNA ligase, cytoplasmic (SARS1) Serine–tRNA ligase, mitochondrial (SARS2)
References