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Lysine—tRNA ligase

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Lysine—tRNA ligase
Identifiers
EC no.6.1.1.6
CAS no.9031-26-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a lysine—tRNA ligase (EC 6.1.1.6) 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 participates in 3 metabolic pathways: lysine biosynthesis, aminoacyl-trna biosynthesis, and amyotrophic lateral sclerosis (als).

Nomenclature

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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.

References

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Further reading

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  • Allen EH, Glassman E, Schweet RS (April 1960). "Incorporation of amino acids into ribonucleic acid. I. The role of activating enzymes". The Journal of Biological Chemistry. 235 (4): 1061–7. doi:10.1016/S0021-9258(18)69479-7. PMID 13792726.
  • Chlumecká V, Von Tigerstrom M, D'Obrenan P, Smith CJ (October 1969). "Purification and properties of lysyl transfer ribonucleic acid synthetase from bakers' yeast". The Journal of Biological Chemistry. 244 (20): 5481–8. doi:10.1016/S0021-9258(18)63589-6. PMID 4310598.
  • Lagerkvist U, Rymo L, Lindqvist O, Andersson E (June 1972). "Some properties of crystals of lysine transfer ribonucleic acid ligase from yeast". The Journal of Biological Chemistry. 247 (12): 3897–9. doi:10.1016/S0021-9258(19)45119-3. PMID 4555953.
  • Stern R, Mehler AH (August 1965). "Lysyl-sRNA synthetase from Escherichia coli". Biochemische Zeitschrift. 342 (4): 400–9. PMID 4284804.