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Information on EC 1.14.13.131 - 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, DMS oxygenase,
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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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1,1-dichloro-1-propene + O2 + NADH + H+
? + NAD+ + H2O
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high rate of oxidation
no detection of oxidation products, but detection of chloride ions released stoichiometrically in the process of oxidation
-
?
1,1-dichloroethylene + O2 + NADH + H+
? + NAD+ + H2O
1,3-dichloro-1-propene + O2 + NADH + H+
? + NAD+ + H2O
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high rate of oxidation
no detection of oxidation products, but detection of chloride ions released stoichiometrically in the process of oxidation
-
?
1-butene + O2 + NADH + H+
1,2-butylene oxide + NAD+ + H2O
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-
-
-
?
2,3-dichloro-1-propene + O2 + NADH + H+
? + NAD+ + H2O
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high rate of oxidation
no detection of oxidation products, but detection of chloride ions released stoichiometrically in the process of oxidation
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?
3,4-dichloro-1-butene + O2 + NADH + H+
3,4-dichloro-1,2-butylene oxide + NAD+ + H2O
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diastereomeric product
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?
cis-1,2-dichloroethylene + O2 + NADH + H+
cis-1,2-dichlorooxirane + NAD+ + H2O
cis-1,4-dichloro-2-butene + O2 + NADH + H+
cis-1,4-dichloro-2,3-butylene oxide + NAD+ + H2O
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-
-
-
?
cis-2,3-butene + O2 + NADH + H+
2,3-butylene oxide + NAD+ + H2O
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-
-
-
?
cis-dichloroethylene + O2 + NADH + H+
cis-dichlorooxirane + NAD+ + H2O
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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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-
?
isobutene + O2 + NADH + H+
isobutylene oxide + NAD+ + H2O
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-
-
-
?
propene + O2 + NADH + H+
propylene oxide + NAD+ + H2O
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-
-
-
?
propylmethyl sulfide + O2 + NADH
? + NAD+ + H2O
about 35% of the activity with dimethyl sulfide
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-
?
trans-1,2-dichloroethylene + O2 + NADH + H+
2,3-dichlorooxirane + NAD+ + H2O
trans-1,4-dichloro-2-butene + O2 + NADH + H+
trans-1,4-dichloro-2,3-butylene oxide + NAD+ + H2O
-
-
-
-
?
trans-dichloroethylene + O2 + NADH + H+
trans-dichlorooxirane + NAD+ + H2O
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-
-
-
?
trichloroethylene + O2 + NADH + H+
? + NAD+ + H2O
additional information
?
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1,1-dichloroethylene + O2 + NADH + H+
? + NAD+ + H2O
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-
-
-
?
1,1-dichloroethylene + O2 + NADH + H+
? + NAD+ + H2O
up to 33% substrate degradation
1,1-dichloroethylene is partially converted to corresponding dihydroxy-dichloroehtylene, and approximately 50% of the resultant dihydroxy-dichloroethylene are dechlorinated
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?
1,1-dichloroethylene + O2 + NADH + H+
? + NAD+ + H2O
up to 33% substrate degradation
1,1-dichloroethylene is partially converted to corresponding dihydroxy-dichloroehtylene, and approximately 50% of the resultant dihydroxy-dichloroethylene are dechlorinated
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?
cis-1,2-dichloroethylene + O2 + NADH + H+
cis-1,2-dichlorooxirane + NAD+ + H2O
up to 100% substrate degradation
-
-
?
cis-1,2-dichloroethylene + O2 + NADH + H+
cis-1,2-dichlorooxirane + NAD+ + H2O
up to 100% substrate degradation
-
-
?
trans-1,2-dichloroethylene + O2 + NADH + H+
2,3-dichlorooxirane + NAD+ + H2O
up to 32% substrate degradation
-
-
?
trans-1,2-dichloroethylene + O2 + NADH + H+
2,3-dichlorooxirane + NAD+ + H2O
up to 32% substrate degradation
-
-
?
trichloroethylene + O2 + NADH + H+
? + NAD+ + H2O
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-
-
-
?
trichloroethylene + O2 + NADH + H+
? + NAD+ + H2O
Acinetobacter sp. 20B grown on dimethyl sulfide degrades up to 50% of 75 mg trichloroethylene/l, respectively
-
-
?
trichloroethylene + O2 + NADH + H+
? + NAD+ + H2O
Acinetobacter sp. 20B grown on dimethyl sulfide degrades up to 50% of 75 mg trichloroethylene/l, respectively
-
-
?
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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component dsoA
UniProt
brenda
component dsoA
UniProt
brenda
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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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expression of DMS monooxygenase genes dsoABCDEF in Escherichia coli
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environmental protection
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Acinetobacter sp. 20B grown on dimethyl sulfide degrades up to 25% of 1.5 mg trichloroethylene/l, respectively. Escherichia coli harboring the DMS monooxygenase genes from strain 20B alone, or in combination with the cumene dioxygenase genes from Pseudomonas fluorescens IP01, degrades up to 50% and 88% of 75 mg TCE/l, respectively. The growth rates of the E. coli recombinants remain nearly unaffected by TCE at least up to 150 mg/l
environmental protection
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Acinetobacter sp. 20B grown on dimethyl sulfide degrades up to 25% of 1.5 mg trichloroethylene/l, respectively. Escherichia coli harboring the DMS monooxygenase genes from strain 20B alone, or in combination with the cumene dioxygenase genes from Pseudomonas fluorescens IP01, degrades up to 50% and 88% of 75 mg TCE/l, respectively. The growth rates of the E. coli recombinants remain nearly unaffected by TCE at least up to 150 mg/l
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Takami, W.; Horinouchi, M.; Nojiri, H.; Yamane, H.; Omori, T.
Evaluation of trichloroethylene degradation by E. coli transformed with dimethyl sulfide monooxygenase genes and/or cumene dioxygenase genes
Biotechnol. Lett.
21
259-264
1999
Acinetobacter sp. (O32428), Acinetobacter sp. 20B (O32428)
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brenda
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
Takami, W.; Yoshida, T.; Nojiri, H.; Yamane, H.; Omori, T.
Oxidation of chlorinated olefins by Escherichia coli transformed with dimethyl sulfide monooxygenase genes or cumene dioxygenase genes
J. Gen. Appl. Microbiol.
45
69-75
1999
Acinetobacter sp. (O32428)
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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