Lysine—tRNA ligase
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 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).
References
- 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.
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| 6.1: Carbon-Oxygen | |
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| 6.2: Carbon-Sulfur | |
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| 6.3: Carbon-Nitrogen | |
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