ExplorEnz: EC 6.3.4.19

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6.3.4.19

Accepted name:

tRNA^Ile-lysidine synthase

Reaction:

[tRNA^Ile²]-cytidine³⁴ + L-lysine + ATP = [tRNA^Ile²]-lysidine³⁴ + AMP + diphosphate + H₂O

Glossary:

lysidine = N⁶-(4-amino-1-β-D-ribofuranosylpyrimidin-2-ylidene)-L-lysine

Other name(s):

TilS; mesJ (gene name); yacA (gene name); isoleucine-specific transfer ribonucleate lysidine synthetase; tRNA^Ile-lysidine synthetase

Systematic name:

L-lysine:[tRNA^Ile²]-cytidine³⁴ ligase (AMP-forming)

Comments:

The bacterial enzyme modifies the wobble base of the CAU anticodon of tRNA^Ile at the oxo group in position 2 of cytidine³⁴. This modification determines both codon and amino acid specificities of tRNA^Ile.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 635304-92-6

References:

1.	Ikeuchi, Y., Soma, A., Ote, T., Kato, J., Sekine, Y. and Suzuki, T. molecular mechanism of lysidine synthesis that determines tRNA identity and codon recognition. Mol. Cell 19 (2005) 235–246. [DOI] [PMID: 16039592]
2.	Salowe, S.P., Wiltsie, J., Hawkins, J.C. and Sonatore, L.M. The catalytic flexibility of tRNA^Ile-lysidine synthetase can generate alternative tRNA substrates for isoleucyl-tRNA synthetase. J. Biol. Chem. 284 (2009) 9656–9662. [DOI] [PMID: 19233850]
3.	Nakanishi, K., Fukai, S., Ikeuchi, Y., Soma, A., Sekine, Y., Suzuki, T. and Nureki, O. 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 (2005) 7487–7492. [DOI] [PMID: 15894617]
4.	Soma, A., Ikeuchi, Y., Kanemasa, S., Kobayashi, K., Ogasawara, N., Ote, T., Kato, J., Watanabe, K., Sekine, Y. and Suzuki, T. An RNA-modifying enzyme that governs both the codon and amino acid specificities of isoleucine tRNA. Mol. Cell 12 (2003) 689–698. [DOI] [PMID: 14527414]
5.	Nakanishi, K., Bonnefond, L., Kimura, S., Suzuki, T., Ishitani, R. and Nureki, O. Structural basis for translational fidelity ensured by transfer RNA lysidine synthetase. Nature 461 (2009) 1144–1148. [DOI] [PMID: 19847269]

[EC 6.3.4.19 created 2011]