EC 6.3.4.22 - TRNAIle2-agmatinylcytidine synthase

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IntEnz Enzyme Nomenclature
EC 6.3.4.22

Names

Accepted name:
tRNAIle2-agmatinylcytidine synthase
Other names:
TiaS
AF2259
tRNAIle-2-agmatinylcytidine synthetase
tRNAIle-agm2C synthetase
tRNAIle-agmatidine synthetase
Systematic name:
agmatine:[tRNAIle]-cytidine34 ligase

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (22) [show] [UniProt]

References

  1. Ikeuchi, Y., Kimura, S., Numata, T., Nakamura, D., Yokogawa, T., Ogata, T., Wada, T., Suzuki, T., Suzuki, T.
    Agmatine-conjugated cytidine in a tRNA anticodon is essential for AUA decoding in archaea.
    Nat. Chem. Biol. 6: 277-282 (2010). [PMID: 20139989]
  2. Terasaka, N., Kimura, S., Osawa, T., Numata, T., Suzuki, T.
    Biogenesis of 2-agmatinylcytidine catalyzed by the dual protein and RNA kinase TiaS.
    Nat. Struct. Mol. Biol. 18: 1268-1274 (2011). [PMID: 22002222]
  3. Osawa, T., Inanaga, H., Kimura, S., Terasaka, N., Suzuki, T., 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: 1414-1416 (2011). [PMID: 22102245]

[EC 6.3.4.22 created 2013]