EC number:2.1.1.106

Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.106
Description:Tryptophan 2-C-methyltransferase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.106
BRENDA Enzyme Link: BRENDA 2.1.1.106
KEGG Enzyme Link: KEGG2.1.1.106
BioCyc Enzyme Link: BioCyc 2.1.1.106
ExPASy Enzyme Link: ExPASy2.1.1.106
EC2PDB Enzyme Link: EC2PDB 2.1.1.106
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.106
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.106
IntEnz Enzyme Link: IntEnz 2.1.1.106
MEDLINE Enzyme Link: MEDLINE 2.1.1.106

EC number:2.1.1.106

MSA:

2.1.1.106;
Phylogenetic Tree:

2.1.1.106;
Uniprot:
M-CSA:
RHEA:17321 L-tryptophan + S-adenosyl-L-methionine = 2-methyl-L-tryptophan + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]:[cH;+0:6]:[*:7]>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]:[c;H0;+0:6](:[*:7])-[CH3;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Formation of 2-methyltryptophan in the biosynthesis of thiostrepton: isolation of S-adenosylmethionine:tryptophan 2-methyltransferase.Frenzel T, Zhou P, Floss HG1990 Apr2321967
Thiostrepton tryptophan methyltransferase expands the chemistry of radical SAM enzymes.Pierre S, Guillot A, Benjdia A, Sandström C, Langella P, Berteau O2012 Dec23064318