EC - TRNAPhe {7-[3-amino-3-(methoxycarbonyl)propyl]wyosine37-N}-methoxycarbonyltransferase

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IntEnz Enzyme Nomenclature


Accepted name:
tRNAPhe {7-[3-amino-3-(methoxycarbonyl)propyl]wyosine37-N}-methoxycarbonyltransferase
Other names:
TYW4 [ambiguous]
tRNA-yW synthesizing enzyme-4 [ambiguous]
Systematic name:
S-adenosyl-L-methionine:tRNAPhe {7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine37-N}-methyltransferase (carbon dioxide-adding)



The enzyme is found only in eukaryotes, where it is involved in the biosynthesis of wybutosine, a hypermodified tricyclic base found at position 37 of certain tRNAs. The modification is important for translational reading-frame maintenance. In some species that produce hydroxywybutosine the enzyme uses 7-[2-hydroxy-3-amino-3-(methoxycarbonyl)propyl]wyosine37 in tRNAPhe as substrate. The enzyme also has the activity of EC, tRNAPhe [7-(3-amino-3-carboxypropyl)wyosine37-O]-methyltransferase [2].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (15) [show] [UniProt]


  1. Noma, A., Kirino, Y., Ikeuchi, Y., Suzuki, T.
    Biosynthesis of wybutosine, a hyper-modified nucleoside in eukaryotic phenylalanine tRNA.
    EMBO J. 25 : 2142-2154 (2006). [PMID: 16642040]
  2. Suzuki, Y., Noma, A., Suzuki, T., Ishitani, R., Nureki, O.
    Structural basis of tRNA modification with CO2 fixation and methylation by wybutosine synthesizing enzyme TYW4.
    Nucleic Acids Res. 37 : 2910-2925 (2009). [PMID: 19287006]
  3. Kato, M., Araiso, Y., Noma, A., Nagao, A., Suzuki, T., Ishitani, R., Nureki, O.
    Crystal structure of a novel JmjC-domain-containing protein, TYW5, involved in tRNA modification.
    Nucleic Acids Res. 39 : 1576-1585 (2011). [PMID: 20972222]

[EC created 2013]