Enzyme

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EC Tree
     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.269
Description:Dimethylsulfoniopropionate demethylase.
Alternative Name: Dimethylsulfoniopropionate-dependent demethylase A.
Cath: 3.30.1360.120;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.269
BRENDA Enzyme Link: BRENDA 2.1.1.269
KEGG Enzyme Link: KEGG2.1.1.269
BioCyc Enzyme Link: BioCyc 2.1.1.269
ExPASy Enzyme Link: ExPASy2.1.1.269
EC2PDB Enzyme Link: EC2PDB 2.1.1.269
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.269
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.269
IntEnz Enzyme Link: IntEnz 2.1.1.269
MEDLINE Enzyme Link: MEDLINE 2.1.1.269
MSA:

2.1.1.269;

Phylogenetic Tree:

2.1.1.269;

Uniprot:
M-CSA:
RHEA:35467 (6S)-5,6,7,8-tetrahydrofolate + S,S-dimethyl-beta-propiothetin = (6S)-5-methyl-5,6,7,8-tetrahydrofolate + 3-(methylsulfanyl)propanoate + H(+)
RULE(radius=1) [*:1]-[NH;+0:2]-[*:3].[*:4]-[S+;H0:5](-[*:6])-[CH3;+0:7]>>[*:1]-[N;H0;+0:2](-[*:3])-[CH3;+0:7].[*:4]-[S;H0;+0:5]-[*:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Tetrahydrofolate serves as a methyl acceptor in the demethylation of dimethylsulfoniopropionate in cell extracts of sulfate-reducing bacteria.Jansen M, Hansen TA1998 Jan9396840
Dimethylsulfoniopropionate-dependent demethylase (DmdA) from Pelagibacter ubique and Silicibacter pomeroyi.Reisch CR, Moran MA, Whitman WB2008 Dec18849431