| EC |
6.3.4.19 |
| Accepted name: |
tRNAIle-lysidine synthase |
| Reaction: |
[tRNAIle2]-cytidine34 + L-lysine + ATP = [tRNAIle2]-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; tRNAIle-lysidine synthetase |
| Systematic name: |
L-lysine:[tRNAIle2]-cytidine34 ligase (AMP-forming) |
| Comments: |
The bacterial enzyme modifies the wobble base of the CAU anticodon of tRNAIle at the oxo group in position 2 of cytidine34. This modification determines both codon and amino acid specificities of tRNAIle. |
| Links to other databases: |
BRENDA, EXPASY, 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 tRNAIle-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] |
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| [EC 6.3.4.19 created 2011] |
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| EC |
6.3.4.22 |
| Accepted name: |
tRNAIle2-agmatinylcytidine synthase |
| Reaction: |
ATP + agmatine + [tRNAIle2]-cytidine34 + H2O = [tRNAIle2]-2-agmatinylcytidine34 + AMP + 2 phosphate
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| Other name(s): |
TiaS; AF2259; tRNAIle-2-agmatinylcytidine synthetase; tRNAIle-agm2C synthetase; tRNAIle-agmatidine synthetase |
| Systematic name: |
agmatine:[tRNAIle]-cytidine34 ligase |
| Comments: |
The enzyme from the archaeon Archaeoglobus fulgidus modifies the wobble base of the CAU anticodon of the archaeal tRNAIle2 at the oxo group in position 2 of cytidine34. This modification is crucial for accurate decoding of the genetic code. In bacteria EC 6.3.4.19, tRNAIle-lysidine synthase, catalyses the modification of [tRNAIle2]-cytidine34 to [tRNAIle2]-lysidine34 . |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Ikeuchi, Y., Kimura, S., Numata, T., Nakamura, D., Yokogawa, T., Ogata, T., Wada, T., Suzuki, T. and Suzuki, T. Agmatine-conjugated cytidine in a tRNA anticodon is essential for AUA decoding in archaea. Nat. Chem. Biol. 6 (2010) 277–282. [DOI] [PMID: 20139989] |
| 2. |
Terasaka, N., Kimura, S., Osawa, T., Numata, T. and Suzuki, T. Biogenesis of 2-agmatinylcytidine catalyzed by the dual protein and RNA kinase TiaS. Nat. Struct. Mol. Biol. 18 (2011) 1268–1274. [DOI] [PMID: 22002222] |
| 3. |
Osawa, T., Inanaga, H., Kimura, S., Terasaka, N., Suzuki, T. and Numata, T. Crystallization and preliminary X-ray diffraction analysis of an archaeal tRNA-modification enzyme, TiaS, complexed with tRNA(Ile2) and ATP. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 (2011) 1414–1416. [DOI] [PMID: 22102245] |
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| [EC 6.3.4.22 created 2013] |
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