Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.290
Description:tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine(37)-O)-methyltransferase.
Alternative Name: tRNA-yW synthesizing enzyme-4.
Cath: 2.120.10.80; 3.40.50.150;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.290
BRENDA Enzyme Link: BRENDA 2.1.1.290
KEGG Enzyme Link: KEGG2.1.1.290
BioCyc Enzyme Link: BioCyc 2.1.1.290
ExPASy Enzyme Link: ExPASy2.1.1.290
EC2PDB Enzyme Link: EC2PDB 2.1.1.290
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.290
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.290
IntEnz Enzyme Link: IntEnz 2.1.1.290
MEDLINE Enzyme Link: MEDLINE 2.1.1.290
MSA:

2.1.1.290;

Phylogenetic Tree:

2.1.1.290;

Uniprot:
M-CSA:
RHEA:36903 7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + S-adenosyl-L-methionine = 7-[(3S)-(3-amino-3-methoxycarbonyl)propyl]wyosine(37) in tRNA(Phe) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Crystal structure of a novel JmjC-domain-containing protein, TYW5, involved in tRNA modification.Kato M, Araiso Y, Noma A, Nagao A, Suzuki T, Ishitani R, Nureki O2011 Mar20972222
Structural basis of tRNA modification with CO2 fixation and methylation by wybutosine synthesizing enzyme TYW4.Suzuki Y, Noma A, Suzuki T, Ishitani R, Nureki O2009 May19287006
Biosynthesis of wybutosine, a hyper-modified nucleoside in eukaryotic phenylalanine tRNA.Noma A, Kirino Y, Ikeuchi Y, Suzuki T2006 May 1716642040