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Information on EC 1.14.13.131 - dissimilatory dimethyl sulfide monooxygenase for references in articles please use BRENDA:EC1.14.13.131
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EC Tree
IUBMB Comments The enzyme participates exclusively in sulfur dissimilation. It has lower activity with diethyl sulfide and other short-chain alkyl methyl sulfides. Its activity is stimulated by combined addition of FMN, and, after depletion of cations, of Mg2+ and Fe2+. The enzymes from bacteria of the Hyphomicrobium genus are a two component system that includes an FMN-dependent reductase subunit and a monooxygenase subunit.
The enzyme appears in viruses and cellular organisms
Synonyms
dimethylsulfide monooxygenase, DMS monooxygenase,
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dimethylsulfide monooxygenase
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dimethyl sulfide + O2 + NADH + H+ = methanethiol + formaldehyde + NAD+ + H2O
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dimethyl sulfide,NADH:oxygen oxidoreductase
The enzyme participates exclusively in sulfur dissimilation. It has lower activity with diethyl sulfide and other short-chain alkyl methyl sulfides. Its activity is stimulated by combined addition of FMN, and, after depletion of cations, of Mg2+ and Fe2+. The enzymes from bacteria of the Hyphomicrobium genus are a two component system that includes an FMN-dependent reductase subunit and a monooxygenase subunit.
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diethyl sulfide + O2 + NADH
ethanethiol + acetaldehyde + NAD+ + H2O
about 35% of the activity with dimethyl sulfide
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dimethyl sulfide + O2 + NADH
methanethiol + formaldehyde + NAD+ + H2O
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dimethyl sulfide + O2 + NADH + H+
methanethiol + formaldehyde + NAD+ + H2O
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ethylmethyl sulfide + O2 + NADH
? + NAD+ + H2O
about 50% of the activity with dimethyl sulfide
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propylmethyl sulfide + O2 + NADH
? + NAD+ + H2O
about 35% of the activity with dimethyl sulfide
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additional information
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additional information
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no activity with alkanesulfonates, aldehydes, nitrilotriacetate, or dibenzothiophenesulfone
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additional information
?
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no activity with alkanesulfonates, aldehydes, nitrilotriacetate, or dibenzothiophenesulfone
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FMN
highest activity with cofactors FMN and NADH
NADH
highest activity with cofactors FMN and NADH. NADH plus FAD show 64% of the activity with NADH and FMN
NADPH
plus FMN, 4% of the activity with cofactors FMN and NADH
additional information
little or no activity is observed with FAD, lumiflavin, riboflavin, or lumichrome in the presence of NADPH
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additional information
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little or no activity is observed with FAD, lumiflavin, riboflavin, or lumichrome in the presence of NADPH
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Fe2+
18% restauration of activity in preparations previously depleted of cations, Mg2+ and Fe2+ together lead to 63% restauration
Mg2+
10% restauration of activity in preparations previously depleted of cations, Mg2+ and Fe2+ together lead to 63% restauration
additional information
divalent cation required, no residual monooxygenase activity in preparations previously depleted of cations. None of the divalent cations, added alone or in combination, fully restores activity
additional information
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divalent cation required, no residual monooxygenase activity in preparations previously depleted of cations. None of the divalent cations, added alone or in combination, fully restores activity
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8-anilinonaphthalenesulfonate
1 mM, almost complete inhibition
Cd2+
1 mM, about 15% residual activity
Hg2+
1 mM, about 5% residual activity
Pb2+
1 mM, about 10% residual activity
umbelliferone
1 mM, almost complete inhibition
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0.0172
Dimethyl sulfide
pH 7.4, 30°C
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5.45
Dimethyl sulfide
pH 7.4, 30°C
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brenda
large subunit DmoA; enzyme belongs to flavin-linked monooxygenases of the luciferase family
UniProt
brenda
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physiological function
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pathway of dimethyl sulfoxide metabolism involves an initial reduction to dimethyl sulfide, which is subsequently oxidized by the NADH-dependent mono-oxygenase to formaldehyde and methanethiol. Further oxidation of methanethiol is by a hydrogen peroxide-producing oxidase, again resulting in the production of formaldehyde
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19000
1 * 53000 + 1 * 19000, SDS-PAGE. DmoA, 53-kDa FMNH2-dependent monooxygenase, and DmoB, 19-kDa NAD(P)H-dependent flavin oxidoreductase subunit
53000
1 * 53000 + 1 * 19000, SDS-PAGE. DmoA, 53-kDa FMNH2-dependent monooxygenase, and DmoB, 19-kDa NAD(P)H-dependent flavin oxidoreductase subunit
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dimer
1 * 53000 + 1 * 19000, SDS-PAGE. DmoA, 53-kDa FMNH2-dependent monooxygenase, and DmoB, 19-kDa NAD(P)H-dependent flavin oxidoreductase subunit
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unstable, more than 50% of the activity is lost when cell-free extracts are stored in ice for 2 h
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Boden, R.; Borodina, E.; Wood, A.; Kelly, D.; Murrell, J.; Schäfer, H.
Purification and characterization of dimethylsulfide monooxygenase from Hyphomicrobium sulfonivorans
J. Bacteriol.
193
1250-1258
2011
Hyphomicrobium sulfonivorans (E9JFX9), Hyphomicrobium sulfonivorans
brenda
De Bont, J.; Van Dijken, J.; Harder, W.
Dimethyl sulphoxide and dimethyl sulphide as a carbon, sulphur and energy source for growth of Hyphomicrobium S
J. Gen. Microbiol.
127
315-323
1981
Hyphomicrobium sp.
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brenda
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1.14.13.131 dissimilatory dimethyl sulfide monooxygenase
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