TRNAIle-lysidine synthase

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 [tRNAIle2]-lysidine34 + AMP + diphosphate + H2O
TRNAIle-lysidine synthase
Identifiers
EC no.6.3.4.19
CAS no.635304-92-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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

References
  1. 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.
  2. 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.
  3. 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.
  4. 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.
  5. 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.
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