EC - TRNAPhe (4-demethylwyosine37-C7) aminocarboxypropyltransferase

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IntEnz Enzyme Nomenclature


Accepted name:
tRNAPhe (4-demethylwyosine37-C7) aminocarboxypropyltransferase
Other names:
tRNA-yW synthesizing enzyme-2
TRM12 (gene name)
taw2 (gene name)
Systematic name:
S-adenosyl-L-methionine:tRNAPhe (4-demethylwyosine37-C7)-[(3S)-3-amino-3-carboxypropyl]transferase



The enzyme, which is found in all eukaryotes and in the majority of Euryarchaeota (but not in the Crenarchaeota), is involved in the hypermodification of the guanine nucleoside at position 37 of tRNA leading to formation of assorted wye bases. This modification is essential for translational reading-frame maintenance. The eukaryotic enzyme is involved in biosynthesis of the tricyclic base wybutosine, which is found only in tRNAPhe.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0102522
UniProtKB/Swiss-Prot: (12) [show] [UniProt]


  1. Umitsu, M., Nishimasu, H., Noma, A., Suzuki, T., Ishitani, R., Nureki, O.
    Structural basis of AdoMet-dependent aminocarboxypropyl transfer reaction catalyzed by tRNA-wybutosine synthesizing enzyme, TYW2.
    Proc. Natl. Acad. Sci. U.S.A. 106 : 15616-15621 (2009). [PMID: 19717466]
  2. Rodriguez, V., Vasudevan, S., Noma, A., Carlson, B. A., Green, J. E., Suzuki, T., Chandrasekharappa, S. C.
    Structure-function analysis of human TYW2 enzyme required for the biosynthesis of a highly modified Wybutosine (yW) base in phenylalanine-tRNA.
    PLoS ONE 7 : e39297 (2012). [PMID: 22761755]
  3. de Crecy-Lagard, V., Brochier-Armanet, C., Urbonavicius, J., Fernandez, B., Phillips, G., Lyons, B., Noma, A., Alvarez, S., Droogmans, L., Armengaud, J., Grosjean, H.
    Biosynthesis of wyosine derivatives in tRNA: an ancient and highly diverse pathway in Archaea.
    Mol. Biol. Evol. 27 : 2062-2077 (2010). [PMID: 20382657]

[EC created 2013]