EC number:2.1.1.96

Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.96
Description:Thioether S-methyltransferase.
Prosite: PDOC00844;
PDB:
PDBScop
Cath: 3.40.50.150;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.96
BRENDA Enzyme Link: BRENDA 2.1.1.96
KEGG Enzyme Link: KEGG2.1.1.96
BioCyc Enzyme Link: BioCyc 2.1.1.96
ExPASy Enzyme Link: ExPASy2.1.1.96
EC2PDB Enzyme Link: EC2PDB 2.1.1.96
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.96
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.96
IntEnz Enzyme Link: IntEnz 2.1.1.96
MEDLINE Enzyme Link: MEDLINE 2.1.1.96

EC number:2.1.1.96

MSA:

2.1.1.96;
Phylogenetic Tree:

2.1.1.96;
Uniprot:
M-CSA:
RHEA:19613 dimethyl sulfide + S-adenosyl-L-methionine = S-adenosyl-L-homocysteine + trimethylsulfonium
RULE(radius=1) [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]-[S;H0;+0:6]-[*:7]>>[*:5]-[S+;H0:6](-[*:7])-[CH3;+0:4].[*:1]-[S;H0;+0:2]-[*:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
S-adenosyl-L-methionine:thioether S-methyltransferase, a new enzyme in sulfur and selenium metabolism.Mozier NM, McConnell KP, Hoffman JL1988 Apr 53350800
Human indolethylamine N-methyltransferase: cDNA cloning and expression, gene cloning, and chromosomal localization.Thompson MA, Moon E, Kim UJ, Xu J, Siciliano MJ, Weinshilboum RM1999 Nov 110552930