2.1.1.269: dimethylsulfoniopropionate demethylase

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For detailed information about dimethylsulfoniopropionate demethylase, go to the full flat file.

Reaction

Synonyms

dimethylsufoniopropionate-dependent demethylase A, dimethylsulfoniopropionate demethylase, dimethylsulfoniopropionate methyltransferase, dimethylsulfoniopropionate-dependent demethylase, dimethylsulfoniumpropionate:tetrahydrofolate S-methyltransferase, DmdA, DMSP demethylase, DMSP methyltransferase, DMSP:THF demethylase

ECTree

     2 Transferases

         2.1 Transferring one-carbon groups

             2.1.1 Methyltransferases

                2.1.1.269 dimethylsulfoniopropionate demethylase

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Results	in table
114	AA Sequence
21	Cloned(Commentary)
12	Cofactor
2	Crystallization (Commentary)
5	Expression
53	General Information
2	General Stability
10	Inhibitors
2	kcat/KM [mM/s]
2	Ki Value [mM]
9	KM Value [mM]
2	Metals/Ions
5	Molecular Weight [Da]
14	Natural Substrates/ Products (Substrates)
54	Organism
3	Pathway
7	pH Optimum
4	pH Range
5	Purification (Commentary)
4	Reaction
2	Reaction Type
38	Reference
5	Source Tissue
4	Storage Stability
40	Substrates and Products (Substrate)
6	Subunits
80	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
4	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.1.1.269 - dimethylsulfoniopropionate demethylase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

purified recombinant DmdA alone or in complex with substrate 2-(dimethylsulfonio)propanoate or cofactor tetrahydrofolate, mother liquor consists of 325 mM NaCl, 30% PEG 2000, 25 mM HEPES, pH 6.8. method optimization, soaking in solution containing 2 mM DMSP or 2 mM tetrahydrofolate, X-ray diffraction structure determination and analysis at 2.1 A and 1.6 A resolution, respectively, modeling

Candidatus Pelagibacter ubique

Q4FP21

720998

structure of the apoenzyme DmdA to 2.1 A, as well as for co-crystals soaked with substrate dimethylsulfoniopropionate to 1.6 A or the cofactor tetrahydrofolate to 1.6 A. The overall fold is a triple domain structure similar to what has been observed for the glycine cleavage T protein or sarcosine oxidase. The tetrahydrofolate binding fold appears conserved

Candidatus Pelagibacter ubique

Q4FP21

720998