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Enzyme Nomenclature
Information on EC 1.14.13.131 - dimethyl-sulfide monooxygenase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.13.131
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RECOMMENDED NAME
GeneOntology No.
dimethyl-sulfide monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dimethyl sulfide + O2 + NADH + H+ = methanethiol + formaldehyde + NAD+ + H2O
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
dimethyl sulfide,NADH:oxygen oxidoreductase
The enzyme 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 enzyme from Hyphomicrobium is a two component system that includes an FMN-dependent reductase subunit and a monooxygenase subunit.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
large subunit DmoA; enzyme belongs to flavin-linked monooxygenases of the luciferase family
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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?
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
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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-1,4-dichloro-2-butene + O2 + NADH + H+
cis-1,4-dichloro-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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-
?
propylmethyl sulfide + O2 + NADH
? + NAD+ + H2O
about 35% of the activity with dimethyl sulfide
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-
?
trans-1,4-dichloro-2-butene + O2 + NADH + H+
trans-1,4-dichloro-2,3-butylene oxide + NAD+ + H2O
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-
-
-
?
trans-dichloroethylene + O2 + NADH + H+
trans-dichlorooxirane + NAD+ + H2O
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-
-
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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
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-
?
cis-1,2-dichloroethylene + O2 + NADH + H+
cis-1,2-dichlorooxirane + NAD+ + H2O
up to 100% substrate degradation
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-
?
trans-1,2-dichloroethylene + O2 + NADH + H+
2,3-dichlorooxirane + NAD+ + H2O
up to 32% substrate degradation
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-
?
trans-1,2-dichloroethylene + O2 + NADH + H+
2,3-dichlorooxirane + NAD+ + H2O
up to 32% substrate degradation
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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
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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
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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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8-anilinonaphthalenesulfonate
1 mM, almost complete inhibition
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable, more than 50% of the activity is lost when cell-free extracts are stored in ice for 2 h
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
environmental protection
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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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.131)
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