Transferases;
Transferring alkyl or aryl groups, other than methyl groups;
Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
BRITE hierarchy

S-adenosyl-L-methionine:tRNAPhe (4-demethylwyosine37-C7)-[(3S)-3-amino-3-carboxypropyl]transferase

S-adenosyl-L-methionine + 4-demethylwyosine37 in tRNAPhe = S-methyl-5'-thioadenosine + 7-[(3S)-3-amino-3-carboxypropyl]-4-demethylwyosine37 in tRNAPhe [RN:R10611]

R10611
Reaction

S-adenosyl-L-methionine [CPD:C00019];
4-demethylwyosine37 in tRNAPhe

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.

EC 2.5.1.114 created 2013

1  [PMID:19717466]

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 106:15616-21 (2009)
DOI:10.1073/pnas.0905270106

[mja:MJ_1557]

2  [PMID:22761755]

Rodriguez V, Vasudevan S, Noma A, Carlson BA, Green JE, Suzuki T, Chandrasekharappa SC

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)
DOI:10.1371/journal.pone.0039297

3  [PMID:20382657]

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 27:2062-77 (2010)
DOI:10.1093/molbev/msq096