Lysine—tRNA ligase - Misplaced Pages

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Lysine—tRNA ligase

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In enzymology, a lysine—tRNA ligase (EC 6.1.1.6) is an enzyme that catalyzes the chemical reaction

ATP + L-lysine + tRNALys

\rightleftharpoons

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

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.

v t e Enzymes: CO CS and CN ligases (EC 6.1-6.3)
6.1: Carbon-Oxygen	Aminoacyl tRNA synthetase Alanine Arginine Asparagine Aspartate Cysteine D-alanine—poly(phosphoribitol) ligase Glutamate Glutamine Glycine Histidine Isoleucine Leucine Lysine Methionine Phenylalanine Proline Serine Threonine Tryptophan Tyrosine Valine
6.2: Carbon-Sulfur	Succinyl coenzyme A synthetase Acetyl—CoA synthetase Long-chain-fatty-acid—CoA ligase
6.3: Carbon-Nitrogen	Glutamine synthetase Ubiquitin ligase Cullin Von Hippel–Lindau tumor suppressor UBE3A Mdm2 Anaphase-promoting complex UBR1 Glutathione synthetase CTP synthetase Adenylosuccinate synthase Argininosuccinate synthase Holocarboxylase synthetase GMP synthase Asparagine synthetase Carbamoyl phosphate synthetase I II Glutamate–cysteine ligase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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