Biology:Lysine—tRNA ligase
| Lysine—tRNA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 6.1.1.6 | ||||||||
| CAS number | 9031-26-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a lysine—tRNA ligase (EC 6.1.1.6) is an enzyme that catalyzes the chemical reaction
- ATP + L-lysine + tRNALys [math]\displaystyle{ \rightleftharpoons }[/math] 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
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
- "Incorporation of amino acids into ribonucleic acid. I. The role of activating enzymes". The Journal of Biological Chemistry 235: 1061–7. April 1960. PMID 13792726.
- "Purification and properties of lysyl transfer ribonucleic acid synthetase from bakers' yeast". The Journal of Biological Chemistry 244 (20): 5481–8. October 1969. PMID 4310598.
- "Some properties of crystals of lysine transfer ribonucleic acid ligase from yeast". The Journal of Biological Chemistry 247 (12): 3897–9. June 1972. PMID 4555953.
- "Lysyl-sRNA synthetase from Escherichia coli". Biochemische Zeitschrift 342 (4): 400–9. August 1965. PMID 4284804.
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