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