EC |
2.1.1.3 |
Accepted name: |
thetin—homocysteine S-methyltransferase |
Reaction: |
dimethylsulfonioacetate + L-homocysteine = (methylsulfanyl)acetate + L-methionine |
Glossary: |
thetin = sulfobetaine = dimethylsulfonioacetate |
Other name(s): |
dimethylthetin-homocysteine methyltransferase; thetin-homocysteine methylpherase |
Systematic name: |
dimethylsulfonioacetate:L-homocysteine S-methyltransferase |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9029-76-9 |
References: |
1. |
Klee, W.A., Richards, H.H. and Cantoni, G.L. The synthesis of methionine by enzymic transmethylation. VII. Existence of two separate homocysteine methylpherases on mammalian liver. Biochim. Biophys. Acta 54 (1961) 157–164. [DOI] [PMID: 14456704] |
2. |
Maw, G.A. Thetin-homocysteine transmethylase. A preliminary manometric study of the enzyme from rat liver. Biochem. J. 63 (1956) 116–124. [PMID: 13315256] |
3. |
Maw, G.A. Thetin-homocysteine transmethylase. Some further characteristics of the enzyme from rat liver. Biochem. J. 70 (1958) 168–173. [PMID: 13584318] |
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[EC 2.1.1.3 created 1961] |
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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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EC |
4.4.1.3 |
Accepted name: |
dimethylpropiothetin dethiomethylase |
Reaction: |
S,S-dimethyl-β-propiothetin = dimethyl sulfide + acrylate |
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For diagram of 3-(dimethylsulfonio)propanoate metabolism, click here |
Other name(s): |
desulfhydrase; S,S-dimethyl-β-propiothetin dimethyl-sulfide-lyase |
Systematic name: |
S,S-dimethyl-β-propiothetin dimethyl-sulfide-lyase (acrylate-forming) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9026-85-1 |
References: |
1. |
Cantoni, G.L. and Anderson, D.G. Enzymatic cleavage of dimethylpropiothetin by Polysiphonia lanosa. J. Biol. Chem. 222 (1956) 171–177. [PMID: 13366990] |
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[EC 4.4.1.3 created 1961] |
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