The Enzyme Database

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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]
[EC 2.1.1.3 created 1961]
 
 
EC 2.1.1.269     
Accepted name: dimethylsulfoniopropionate demethylase
Reaction: S,S-dimethyl-β-propiothetin + tetrahydrofolate = 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
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
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]
[EC 2.1.1.269 created 2013]
 
 
EC 4.4.1.3     
Accepted name: dimethylpropiothetin dethiomethylase
Reaction: S,S-dimethyl-β-propiothetin = dimethyl sulfide + acrylate
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, 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]
[EC 4.4.1.3 created 1961]
 
 


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