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 expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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SYSTEMATIC NAME
IUBMB Comments
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.
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
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
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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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure to 2.28 A resolution and comparison with those of its homologues long-chain alkane monooxygenase LadA and dibenzothiophene sulfone monooxygenase BdsA. Their overall structures are similar, all share a conserved TIM-barrel fold which is composed of eight alpha-helices and eight beta-strands, and all have five additional insertions. The substrate-binding pocket of DmoA is smaller compared with those of LadA and BdsA
upon expression in Escherichia coli, DmoA and DmoB subunits are able to generate product, albeit at a lower turnover than the natively expressed enzyme. No static protein-protein interactions are observed under the conditions tested between the two subunits
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