Lysine—tRNA ligase

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lysine-tRNA ligase
EC number
CAS number 9031-26-9
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

In enzymology, a lysine-tRNA ligase (EC is an enzyme that catalyzes the chemical reaction

ATP + L-lysine + tRNALys AMP + diphosphate + L-lysyl-tRNALys

The 3 substrates of this enzyme are ATP, L-lysine, and tRNA(Lys), whereas its 3 products are AMP, diphosphate, and L-lysyl-tRNA(Lys).

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-lysine:tRNALys ligase (AMP-forming). Other names in common use include lysyl-tRNA synthetase, lysyl-transfer ribonucleate synthetase, lysyl-transfer RNA synthetase, L-lysine-transfer RNA ligase, lysine-tRNA synthetase, and lysine translase. This enzyme participates in 3 metabolic pathways: lysine biosynthesis, aminoacyl-trna biosynthesis, and amyotrophic lateral sclerosis (als).


  • Allen, E. H.; Glassman, E; Schweet, R. S. (1960). "Incorporation of amino acids into ribonucleic acid. I. The role of activating enzymes". J. Biol. Chem. 235: 1061–7. PMID 13792726. 
  • Chlumecka, V.; Von Tigerstrom, M.; D'Obrenan, P; Smith, C. J. (1969). "Purification and properties of lysyl transfer ribonucleic acid synthetase from baker's yeast". J. Biol. Chem. 244 (20): 5481–8. PMID 4310598. 
  • Lagerkvist, U.; Rymo, L.; Lindqvist, O.; Andersson, E. (1972). "Some properties of crystals of lysine transfer ribonucleic acid ligase from yeast". J. Biol. Chem. 247 (12): 3897–9. PMID 4555953. 
  • Stern, R.; Mehler, A. H. (1965). "Lysyl-sRNA synthetase from Escherichia coli". Biochem. Z. 342 (4): 400–9. PMID 4284804.