Lysine–tRNA ligase
| Lysine–tRNA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.1.1.6 | ||||||||
| CAS no. | 9031-26-9 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, lysine–tRNA ligases (EC 6.1.1.6) are a type of enzyme. In humans the known enzyme of this type is encoded by the gene KARS1.[1] More generally, lysine–tRNA ligases catalyze the chemical reaction[2]
- ATP + L-lysine + tRNALys AMP + diphosphate + L-lysyl-tRNALys
The 3 substrates of this enzyme are ATP, L-lysine, and tRNALys, whereas its 3 products are AMP, diphosphate, and L-lysyl-tRNALys.[2] Besides the enzyme encoded by KARS, the lysX protein found in some bacteria, and the cla4 protein found in the fungus Cladosporium cladosporioides are also able to catalyze this type of reaction.[2]
This enzyme participates in 3 metabolic pathways: lysine biosynthesis, aminoacyl-trna biosynthesis, and amyotrophic lateral sclerosis (als).
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
- ↑ "KARS1 lysyl-tRNA synthetase 1". ncbi.nlm.nih.gov. Retrieved 2026-08-01.
- 1 2 3 "ENZYME entry: EC 6.1.1.6". expasy.org. SIB Swiss Institute of Bioinformatics. Retrieved 2026-08-01.
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 (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.