Lysine—tRNA ligase

Source: Wikipedia, the free encyclopedia.
Lysine—tRNA ligase
Identifiers
ExPASy
NiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
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

.

This enzyme participates in 3

.

Nomenclature

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

Further reading

  • 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: 1061–7.
    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. .
  • 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. .
  • Stern R, Mehler AH (August 1965). "Lysyl-sRNA synthetase from Escherichia coli". Biochemische Zeitschrift. 342 (4): 400–9. .