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Literature summary extracted from

  • Reisch, C.R.
    Assay and analysis of dimethylsulfoniopropionate demethylase (2018), Methods Enzymol., 605, 325-333 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.269 gene dmdA, functional recombinant expression in Escherichia coli Candidatus Pelagibacter ubique
2.1.1.269 gene dmdA, functional recombinant expression in Escherichia coli Ruegeria pomeroyi

General Stability

EC Number General Stability Organism
2.1.1.269 salt solutions do not significantly stimulate activity nor are they required for enzyme stability during storage Candidatus Pelagibacter ubique
2.1.1.269 salt solutions do not significantly stimulate activity nor are they required for enzyme stability during storage Ruegeria pomeroyi

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.269 5.4
-
 S,S-dimethyl-beta-propiothetin pH 7.5, 30°C, cell extract Ruegeria pomeroyi
2.1.1.269 13.2
-
 S,S-dimethyl-beta-propiothetin pH 7.5, 30°C, cell extract Candidatus Pelagibacter ubique

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.1.269 additional information salt solutions do not significantly stimulate activity nor are they required for enzyme stability during storage Candidatus Pelagibacter ubique
2.1.1.269 additional information salt solutions do not significantly stimulate activity nor are they required for enzyme stability during storage Ruegeria pomeroyi

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.269 S,S-dimethyl-beta-propiothetin + tetrahydrofolate Candidatus Pelagibacter ubique
-
 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
 ?
2.1.1.269 S,S-dimethyl-beta-propiothetin + tetrahydrofolate Ruegeria pomeroyi
-
 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
 ?
2.1.1.269 S,S-dimethyl-beta-propiothetin + tetrahydrofolate Candidatus Pelagibacter ubique HTCC1062
-
 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
 ?
2.1.1.269 S,S-dimethyl-beta-propiothetin + tetrahydrofolate Ruegeria pomeroyi DSM 15171
-
 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
 ?
2.1.1.269 S,S-dimethyl-beta-propiothetin + tetrahydrofolate Ruegeria pomeroyi ATCC 700808
-
 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.269 Candidatus Pelagibacter ubique Q4FP21
-
-
2.1.1.269 Candidatus Pelagibacter ubique HTCC1062 Q4FP21
-
-
2.1.1.269 Ruegeria pomeroyi Q5LS57
-
-
2.1.1.269 Ruegeria pomeroyi ATCC 700808 Q5LS57
-
-
2.1.1.269 Ruegeria pomeroyi DSM 15171 Q5LS57
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.269 cell culture
-
 Candidatus Pelagibacter ubique
-
2.1.1.269 cell culture
-
 Ruegeria pomeroyi
-

Storage Stability

EC Number Storage Stability Organism
2.1.1.269 -20°C, enzyme in cell-free extract, in presence of EDTA and 20% glycerol, several weeks without significant loss of activity Candidatus Pelagibacter ubique
2.1.1.269 -20°C, enzyme in cell-free extract, in presence of EDTA and 20% glycerol, several weeks without significant loss of activity Ruegeria pomeroyi
2.1.1.269 4°C, enzyme in cell-free extract, in presence of EDTA, several weeks without significant loss of activity. Without addition of EDTA, the enzyme loses all activity over the course of several days Candidatus Pelagibacter ubique
2.1.1.269 4°C, enzyme in cell-free extract, in presence of EDTA, several weeks without significant loss of activity. Without addition of EDTA, the enzyme loses all activity over the course of several days Ruegeria pomeroyi

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.269 additional information assay metod, overview. The substrate THF and product 5-methyl-THF are labile under aerobic conditions, oxidation of THF is irreversible and results in the release of 4-aminobenzoyl glutamate, essentially breaking the molecule in half. Half-life of THF in solution at pH 7.0 is about 40 min. DTT can stabilize THF in solution Candidatus Pelagibacter ubique ?
-
-
2.1.1.269 additional information assay metod, overview. The substrate THF and product 5-methyl-THF are labile under aerobic conditions, oxidation of THF is irreversible and results in the release of 4-aminobenzoyl glutamate, essentially breaking the molecule in half. Half-life of THF in solution at pH 7.0 is about 40 min. DTT can stabilize THF in solution Ruegeria pomeroyi ?
-
-
2.1.1.269 additional information assay metod, overview. The substrate THF and product 5-methyl-THF are labile under aerobic conditions, oxidation of THF is irreversible and results in the release of 4-aminobenzoyl glutamate, essentially breaking the molecule in half. Half-life of THF in solution at pH 7.0 is about 40 min. DTT can stabilize THF in solution Candidatus Pelagibacter ubique HTCC1062 ?
-
-
2.1.1.269 additional information assay metod, overview. The substrate THF and product 5-methyl-THF are labile under aerobic conditions, oxidation of THF is irreversible and results in the release of 4-aminobenzoyl glutamate, essentially breaking the molecule in half. Half-life of THF in solution at pH 7.0 is about 40 min. DTT can stabilize THF in solution Ruegeria pomeroyi DSM 15171 ?
-
-
2.1.1.269 additional information assay metod, overview. The substrate THF and product 5-methyl-THF are labile under aerobic conditions, oxidation of THF is irreversible and results in the release of 4-aminobenzoyl glutamate, essentially breaking the molecule in half. Half-life of THF in solution at pH 7.0 is about 40 min. DTT can stabilize THF in solution Ruegeria pomeroyi ATCC 700808 ?
-
-
2.1.1.269 S,S-dimethyl-beta-propiothetin + tetrahydrofolate
-
 Candidatus Pelagibacter ubique 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
 ?
2.1.1.269 S,S-dimethyl-beta-propiothetin + tetrahydrofolate
-
 Ruegeria pomeroyi 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
 ?
2.1.1.269 S,S-dimethyl-beta-propiothetin + tetrahydrofolate
-
 Candidatus Pelagibacter ubique HTCC1062 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
 ?
2.1.1.269 S,S-dimethyl-beta-propiothetin + tetrahydrofolate
-
 Ruegeria pomeroyi DSM 15171 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
 ?
2.1.1.269 S,S-dimethyl-beta-propiothetin + tetrahydrofolate
-
 Ruegeria pomeroyi ATCC 700808 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.269 DmdA
-
 Candidatus Pelagibacter ubique
2.1.1.269 DmdA
-
 Ruegeria pomeroyi
2.1.1.269 DMSP demethylase
-
 Candidatus Pelagibacter ubique
2.1.1.269 DMSP demethylase
-
 Ruegeria pomeroyi

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.269 30
-
 assay at Candidatus Pelagibacter ubique
2.1.1.269 30
-
 assay at Ruegeria pomeroyi

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.269 7.5
-
 assay at Candidatus Pelagibacter ubique
2.1.1.269 7.5
-
 assay at Ruegeria pomeroyi

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.269 tetrahydrofolate (DMSP) demethylase is a tetrahydrofolate-dependent enzyme Candidatus Pelagibacter ubique
2.1.1.269 tetrahydrofolate (DMSP) demethylase is a tetrahydrofolate-dependent enzyme Ruegeria pomeroyi

Expression

EC Number Organism Comment Expression
2.1.1.269 Candidatus Pelagibacter ubique dimethylsulfoniopropionate (DMSP) induces gene dmdA transcription up
2.1.1.269 Ruegeria pomeroyi dimethylsulfoniopropionate (DMSP) induces gene dmdA transcription up

General Information

EC Number General Information Comment Organism
2.1.1.269 evolution though DmdA is homologous to the glycine cleavage T-protein and shares structural similarity, the mechanism of carbon transfer is more similar to S-adenosyl-methionine (SAM)-dependent methyl-transfer enzymes. DmdA catalyzes the transfer of a methyl group to form 5-methyl-THF, which is analogous to SAM-dependent reactions. The gene dmdA is abundant in marine waters Candidatus Pelagibacter ubique
2.1.1.269 evolution though DmdA is homologous to the glycine cleavage T-protein and shares structural similarity, the mechanism of carbon transfer is more similar to S-adenosyl-methionine (SAM)-dependent methyl-transfer enzymes. DmdA catalyzes the transfer of a methyl group to form 5-methyl-THF, which is analogous to SAM-dependent reactions. The gene dmdA is abundant in marine waters Ruegeria pomeroyi
2.1.1.269 physiological function dimethylsulfoniopropionate (DMSP) demethylase is a tetrahydrofolate-dependent enzyme that initiates the DMSP demethylation pathway in marine bacteria. This enzyme is important for understanding of organic sulfur flux from the oceans because it directs the sulfur from DMSP away from dimethylsulfide Candidatus Pelagibacter ubique
2.1.1.269 physiological function dimethylsulfoniopropionate (DMSP) demethylase is a tetrahydrofolate-dependent enzyme that initiates the DMSP demethylation pathway in marine bacteria. This enzyme is important for understanding of organic sulfur flux from the oceans because it directs the sulfur from DMSP away from dimethylsulfide Ruegeria pomeroyi