TRNAIle-lysidine synthase

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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).^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical reaction

[tRNAIle2]-cytidine34 + L-lysine + ATP

\rightleftharpoons

[tRNAIle2]-lysidine³⁴ + AMP + diphosphate + H₂O

The bacterial enzyme modifies the wobble base of the CAU anticodon of tRNAIle at the oxo group in position 2 of cytidine³⁴.

References

↑ Ikeuchi, Y.; Soma, A.; Ote, T.; Kato, J.; Sekine, Y.; Suzuki, T. (2005). "molecular mechanism of lysidine synthesis that determines tRNA identity and codon recognition". Mol. Cell. 19 (2): 235–246. PMID 16039592. doi:10.1016/j.molcel.2005.06.007.
↑ Salowe, S.P.; Wiltsie, J.; Hawkins, J.C.; Sonatore, L.M. (2009). "The catalytic flexibility of tRNA^Ile-lysidine synthetase can generate alternative tRNA substrates for isoleucyl-tRNA synthetase". J. Biol. Chem. 284: 9656–9662. PMC 2665086 . PMID 19233850. doi:10.1074/jbc.M809013200.
↑ Nakanishi, K.; Fukai, S.; Ikeuchi, Y.; Soma, A.; Sekine, Y.; Suzuki, T.; Nureki, O. (2005). "Structural basis for lysidine formation by ATP pyrophosphatase accompanied by a lysine-specific loop and a tRNA-recognition domain". Proc. Natl. Acad. Sci. USA. 102: 7487–7492. PMC 1140429 . PMID 15894617. doi:10.1073/pnas.0501003102.
↑ Soma, A.; Ikeuchi, Y.; Kanemasa, S.; Kobayashi, K.; Ogasawara, N.; Ote, T.; Kato, J.; Watanabe, K.; Sekine, Y.; Suzuki, T. (2003). "An RNA-modifying enzyme that governs both the codon and amino acid specificities of isoleucine tRNA". Mol. Cell. 12 (3): 689–698. PMID 14527414. doi:10.1016/s1097-2765(03)00346-0.
↑ Nakanishi, K.; Bonnefond, L.; Kimura, S.; Suzuki, T.; Ishitani, R.; Nureki, O. (2009). "Structural basis for translational fidelity ensured by transfer RNA lysidine synthetase". Nature. 461 (7267): 1144–1148. PMID 19847269. doi:10.1038/nature08474.

External links

TRNAIle-lysidine synthase at the US National Library of Medicine Medical Subject Headings (MeSH)

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

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor
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)

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