Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups
BRITE hierarchy

S-adenosyl-L-methionine:tRNAPhe {7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine37-N}-methyltransferase (carbon dioxide-adding)

S-adenosyl-L-methionine + 7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine37 in tRNAPhe + CO2 = S-adenosyl-L-homocysteine + wybutosine37 in tRNAPhe [RN:R10587]

R10587
Reaction

S-adenosyl-L-methionine [CPD:C00019];
7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine37 in tRNAPhe;
CO2 [CPD:C00011]

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 2.1.1.290, tRNAPhe [7-(3-amino-3-carboxypropyl)wyosine37-O]-methyltransferase [2].

EC 2.3.1.231 created 2013

1  [PMID:16642040]

Noma A, Kirino Y, Ikeuchi Y, Suzuki T

Biosynthesis of wybutosine, a hyper-modified nucleoside in eukaryotic phenylalanine tRNA.

EMBO J 25:2142-54 (2006)
DOI:10.1038/sj.emboj.7601105

[sce:YOL141W]

2  [PMID:19287006]

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 37:2910-25 (2009)
DOI:10.1093/nar/gkp158

[sce:YOL141W]

3  [PMID:20972222]

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 39:1576-85 (2011)
DOI:10.1093/nar/gkq919