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 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.
Katze JR, Konigsberg W (1970). "Purification and properties of seryl transfer ribonucleic acid synthetase from Escherichia coli". J. Biol. Chem. 245 (5): 923–30. PMID4906848.
Makman MH; Cantoni GL (1965). "Isolation of seryl and phenylalanyl ribonucleic acid synthetases from baker's yeast". Biochemistry. 4: 1434–1442. doi:10.1021/bi00883a031.
Webster LT; Davie EW (1961). "Purification and properties of serine-activating enzyme from beef pancreas". J. Biol. Chem. 236: 479–484. PMID13783661.
Ohama T, Yang DC, Hatfield DL (1994). "Selenocysteine tRNA and serine tRNA are aminoacylated by the same synthetase, but may manifest different identities with respect to the long extra arm". Arch. Biochem. Biophys. 315 (2): 293–301. doi:10.1006/abbi.1994.1503. PMID7986071.