ID: | 2.1.1.269 |
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Description: | Dimethylsulfoniopropionate demethylase. |
Alternative Name: |
Dimethylsulfoniopropionate-dependent demethylase A. |
Cath: | 3.30.1360.120; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.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: | |
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Phylogenetic Tree: | |
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 |
Title | Authors | Date | PubMed ID |
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Tetrahydrofolate serves as a methyl acceptor in the demethylation of dimethylsulfoniopropionate in cell extracts of sulfate-reducing bacteria. | Jansen M, Hansen TA | 1998 Jan | 9396840 |
Dimethylsulfoniopropionate-dependent demethylase (DmdA) from Pelagibacter ubique and Silicibacter pomeroyi. | Reisch CR, Moran MA, Whitman WB | 2008 Dec | 18849431 |