| EC |
2.1.1.269 |
| Accepted name: |
dimethylsulfoniopropionate demethylase |
| Reaction: |
S,S-dimethyl-β-propiothetin + tetrahydrofolate = 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate |
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For diagram of 3-(dimethylsulfonio)propanoate metabolism, click here |
| Glossary: |
S,S-dimethyl-β-propiothetin = 3-(S,S-dimethylsulfonio)propanoate |
| Other name(s): |
dmdA (gene name); dimethylsulfoniopropionate-dependent demethylase A |
| Systematic name: |
S,S-dimethyl-β-propiothetin:tetrahydrofolate S-methyltransferase |
| Comments: |
The enzyme from the marine bacteria Pelagibacter ubique and Ruegeria pomeroyi are specific towards S,S-dimethyl-β-propiothetin. They do not demethylate glycine-betaine [1,2]. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Jansen, M. and Hansen, T.A. Tetrahydrofolate serves as a methyl acceptor in the demethylation of dimethylsulfoniopropionate in cell extracts of sulfate-reducing bacteria. Arch. Microbiol. 169 (1998) 84–87. [PMID: 9396840] |
| 2. |
Reisch, C.R., Moran, M.A. and Whitman, W.B. Dimethylsulfoniopropionate-dependent demethylase (DmdA) from Pelagibacter ubique and Silicibacter pomeroyi. J. Bacteriol. 190 (2008) 8018–8024. [DOI] [PMID: 18849431] |
| 3. |
Schuller, D.J., Reisch, C.R., Moran, M.A., Whitman, W.B. and Lanzilotta, W.N. Structures of dimethylsulfoniopropionate-dependent demethylase from the marine organism Pelagibacter ubique. Protein Sci. 21 (2012) 289–298. [DOI] [PMID: 22162093] |
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| [EC 2.1.1.269 created 2013] |
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