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Literature summary for 1.14.13.245 extracted from

  • Horinouchi, M.; Yoshida, T.; Nojiri, H.; Yamane, H.; Omori, T.
    Polypeptide requirement of multicomponent monooxygenase DsoABCDEF for dimethyl sulfide oxidizing activity (1999), Biosci. Biotechnol. Biochem., 63, 1765-1771 .
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Acinetobacter sp. O32428 and O32429 and O32430 and O32431 and O32432 and O32433 O32428 i.e. subunit DsoA, O32429 i.e. subunit DsoB, O32430 i.e. subunit DsoC, O32431 i.e. subunit DsoD, O32432 i.e. subunit DsoE, O32433 i.e. subunit DsoF
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dimethyl sulfide + NADH + H+ + O2
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Acinetobacter sp. dimethyl sulfoxide + NAD+ + H2O
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General Information

General Information Comment Organism
physiological function subunits DsoB, C, D, E, and F are needed for DMS-oxidizing activity in polypeptide requirement experiments, while subunit DsoA is not necessary for it. Complementation of the deletion mutants lacking DsoC or F with the corresponding Dmp polypeptides supports the DMS-oxidizing activity, while complementation of the deletion mutants lacking any of the oxygenase subunits (DsoB, D, or E) with the corresponding Dmp polypeptides reduces or nullifies the activity Acinetobacter sp.