TRNAIle-lysidine synthase - Misplaced Pages

TRNAIle-lysidine synthase (EC 6.3.4.19, TilS, mesJ (gene), yacA (gene), isoleucine-specific transfer ribonucleate lysidine synthetase, tRNAIle-lysidine synthetase) is an enzyme with systematic name L-lysine:(tRNAIle2)-cytidine34 ligase (AMP-forming). This enzyme catalyses the following chemical reaction

-cytidine34 + L-lysine + ATP

\rightleftharpoons

-lysidine + AMP + diphosphate + H₂O

The bacterial enzyme modifies the wobble base of the CAU anticodon of tRNAIle at the oxo group in position 2 of cytidine.

References

Ikeuchi Y, Soma A, Ote T, Kato J, Sekine Y, Suzuki T (July 2005). "molecular mechanism of lysidine synthesis that determines tRNA identity and codon recognition". Molecular Cell. 19 (2): 235–46. doi:10.1016/j.molcel.2005.06.007. PMID 16039592.
Salowe SP, Wiltsie J, Hawkins JC, Sonatore LM (April 2009). "The catalytic flexibility of tRNAIle-lysidine synthetase can generate alternative tRNA substrates for isoleucyl-tRNA synthetase". The Journal of Biological Chemistry. 284 (15): 9656–62. doi:10.1074/jbc.M809013200. PMC 2665086. PMID 19233850.
Nakanishi K, Fukai S, Ikeuchi Y, Soma A, Sekine Y, Suzuki T, Nureki O (May 2005). "Structural basis for lysidine formation by ATP pyrophosphatase accompanied by a lysine-specific loop and a tRNA-recognition domain". Proceedings of the National Academy of Sciences of the United States of America. 102 (21): 7487–92. doi:10.1073/pnas.0501003102. PMC 1140429. PMID 15894617.
Soma A, Ikeuchi Y, Kanemasa S, Kobayashi K, Ogasawara N, Ote T, Kato J, Watanabe K, Sekine Y, Suzuki T (September 2003). "An RNA-modifying enzyme that governs both the codon and amino acid specificities of isoleucine tRNA". Molecular Cell. 12 (3): 689–98. doi:10.1016/s1097-2765(03)00346-0. PMID 14527414.
Nakanishi K, Bonnefond L, Kimura S, Suzuki T, Ishitani R, Nureki O (October 2009). "Structural basis for translational fidelity ensured by transfer RNA lysidine synthetase". Nature. 461 (7267): 1144–8. doi:10.1038/nature08474. PMID 19847269. S2CID 4426738.

External links

TRNAIle-lysidine+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

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)

Portal:

Biology

Category:

EC 6.3.4