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{{Infobox enzyme
| Name = TRNAIle-lysidine synthase
| EC_number = 6.3.4.19
| CAS_number = 635304-92-6
| IUBMB_EC_number = 6/3/4/19
| GO_code = 
| image = 
| width = 
| caption =
}}
'''TRNAIle-lysidine synthase''' ({{EC number|6.3.4.19}}, ''TilS'', ''mesJ (gene)'', ''yacA (gene)'', ''isoleucine-specific transfer ribonucleate lysidine synthetase'', ''tRNAIle-lysidine synthetase'') is an [[enzyme]] with system name ''L-lysine:(tRNAIle2)-cytidine34 ligase (AMP-forming)''.<ref>{{cite journal | title = molecular mechanism of lysidine synthesis that determines tRNA identity and codon recognition |author = Ikeuchi, Y., Soma, A., Ote, T., Kato, J., Sekine, Y. and Suzuki, T. |journal = Mol. Cell |year = 2005 |volume = 19 |pages = 235–246 |pmid = 16039592 |doi=10.1016/j.molcel.2005.06.007 |issue=2}}</ref><ref>{{cite journal | title = The catalytic flexibility of tRNA<sup>Ile</sup>-lysidine synthetase can generate alternative tRNA substrates for isoleucyl-tRNA synthetase |author = Salowe, S.P., Wiltsie, J., Hawkins, J.C. and Sonatore, L.M. |journal = J. Biol. Chem. |year = 2009 |volume = 284 |pages = 9656–9662 |pmid = 19233850 |doi=10.1074/jbc.M809013200 |pmc=2665086}}</ref><ref>{{cite journal | title = Structural basis for lysidine formation by ATP pyrophosphatase accompanied by a lysine-specific loop and a tRNA-recognition domain |author = Nakanishi, K., Fukai, S., Ikeuchi, Y., Soma, A., Sekine, Y., Suzuki, T. and Nureki, O. |journal = Proc. Natl. Acad. Sci. USA |year = 2005 |volume = 102 |pages = 7487–7492 |pmid = 15894617 |doi=10.1073/pnas.0501003102 |pmc=1140429}}</ref><ref>{{cite journal | title = An RNA-modifying enzyme that governs both the codon and amino acid specificities of isoleucine tRNA |author = Soma, A., Ikeuchi, Y., Kanemasa, S., Kobayashi, K., Ogasawara, N., Ote, T., Kato, J., Watanabe, K., Sekine, Y. and Suzuki, T. |journal = Mol. Cell |year = 2003 |volume = 12 |pages = 689–698 |pmid = 14527414 |issue=3}}</ref><ref>{{cite journal | title = Structural basis for translational fidelity ensured by transfer RNA lysidine synthetase |author = Nakanishi, K., Bonnefond, L., Kimura, S., Suzuki, T., Ishitani, R. and Nureki, O. |journal = Nature |year = 2009 |volume = 461 |pages = 1144–1148 |pmid = 19847269 |doi=10.1038/nature08474 |issue=7267}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]

: [tRNAIle2]-cytidine34 + L-[[lysine]] + ATP <math>\rightleftharpoons</math> [tRNAIle2]-lysidine<sup>34</sup> + AMP + [[diphosphate]] + H<sub>2</sub>O

The bacterial enzyme modifies the [[Wobble base pair|wobble base]] of the CAU [[anticodon]] of tRNAIle at the oxo group in position 2 of cytidine<sup>34</sup>.

== References ==
{{reflist}}

== External links ==
* {{MeshName|TRNAIle-lysidine+synthase}}

[[Category:EC 6.3.4]]