Literature summary 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 .

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.14.13.245	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 and Products (Substrate)

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

General Information

EC Number	General Information	Comment	Organism
1.14.13.245	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.

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Release 2023.1 (January 2023)