ExplorEnz: EC 2.1.1.290

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2.1.1.290

Accepted name:

tRNA^Phe [7-(3-amino-3-carboxypropyl)wyosine³⁷-O]-methyltransferase

Reaction:

S-adenosyl-L-methionine + 7-[(3S)-3-amino-3-carboxypropyl]wyosine³⁷ in tRNA^Phe = S-adenosyl-L-homocysteine + 7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine³⁷ in tRNA^Phe

For diagram of wyosine biosynthesis, click here

Glossary:

wyosine = 4,6-dimethyl-3-(β-D-ribofuranosyl)-3,4-dihydro-9H-imidazo[1,2-a]purin-9-one
wybutosine = yW = 7-[(3S)-3-(methoxycarbonyl)-3-(methoxycarbonylamino)propyl]-4,5-dimethyl-3-(β-D-ribofuranosyl)-3,4-dihydro-9H-imidazo[1,2-a]purin-9-one

Other name(s):

TYW4 (ambiguous); tRNA-yW synthesizing enzyme-4 (ambiguous)

Systematic name:

S-adenosyl-L-methionine:tRNA^Phe {7-[(3S)-3-amino-3-carboxypropyl]wyosine³⁷-O}-methyltransferase

Comments:

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-carboxypropyl)wyosine³⁷ in tRNA^Phe as substrate. The enzyme also has the activity of EC 2.3.1.231, tRNA^Phe 7-[(3S)-4-methoxy-(3-amino-3-carboxypropyl)wyosine³⁷-O]-carbonyltransferase [2].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

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

[EC 2.1.1.290 created 2013]