The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: tRNAIle2-agmatinylcytidine synthase
Reaction: ATP + agmatine + [tRNAIle2]-cytidine34 + H2O = [tRNAIle2]-2-agmatinylcytidine34 + AMP + 2 phosphate
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, tRNAIle-lysidine synthase, catalyses the modification of [tRNAIle2]-cytidine34 to [tRNAIle2]-lysidine34 .
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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]
[EC created 2013]

Data © 2001–2023 IUBMB
Web site © 2005–2023 Andrew McDonald