Serine—tRNA ligase

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serine-tRNA ligase
Identifiers
EC number 6.1.1.11
CAS number 9023-48-7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

In enzymology, a serine-tRNA ligase (EC 6.1.1.11) 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, 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.

Structural studies[edit]

As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes 1SER, 1SES, 1SET, 1SRY, 1WLE, 2CIM, 2CJ9, 2CJA, 2CJB, 2DQ0, 2DQ1, 2DQ2, and 2DQ3.

References[edit]

  • Katze JR, Konigsberg W (1970). "Purification and properties of seryl transfer ribonucleic acid synthetase from Escherichia coli". J. Biol. Chem. 245 (5): 923–30. PMID 4906848. 
  • Makman MH and 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 and Davie EW (1961). "Purification and properties of serine-activating enzyme from beef pancreas". J. Biol. Chem. 236: 479–484. PMID 13783661. 
  • 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. PMID 7986071.