EC 184.108.40.206 - Respiratory dimethylsulfoxide reductase
IntEnz Enzyme Nomenclature
dimethylsulfoxide reductase [ambiguous]
28494 [IUBMB]a menaquinonea menaquinonePOLYMER:9537Formula: C11H8O2(C5H8)n
Charge: (0)(0)ndimethyl sulfidedimethyl sulfideName origin: UniProt - CHECKED (C)Formula: C2H6S
Charge: 0ChEBI compound status: CHECKED (C)H2OH2OName origin: UniProt - CHECKED (C)Formula: H2O
Charge: 0ChEBI compound status: CHECKED (C)=a menaquinola menaquinolPOLYMER:9539Formula: C11H10O2(C5H8)n
The enzyme participates in bacterial electron transfer pathways in which dimethylsulfoxide (DMSO) is the terminal electron acceptor. It is composed of three subunits - DmsA contains a bis(guanylyl molybdopterin) cofactor and a [4Fe-4S] cluster, DmsB is an iron-sulfur protein, and DmsC is a transmembrane protein that anchors the enzyme and accepts electrons from the quinol pool. The electrons are passed through DmsB to DmsA and on to DMSO. The enzyme can also reduce pyridine-N-oxide and trimethylamine N-oxide to the corresponding amines with lower activity.
Links to other databases
Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase.Microbiology 142 : 3231-3239 (1996). [PMID: 8969520]
Dimethyl sulfoxide reductase is not required for trimethylamine N-oxide reduction in Escherichia coli.FEMS Microbiol. Lett. 67 : 255-259 (1991). [PMID: 1769531]
Electron-donors and the quinone involved in dimethyl-sulfoxide reduction in Escherichia coli.Curr. Microbiol. 22 : 109-115 (1991).
Interactions between the molybdenum cofactor and iron-sulfur clusters of Escherichia coli dimethylsulfoxide reductase.J. Biol. Chem. 274 : 13002-13009 (1999). [PMID: 10224050]
[EC 220.127.116.11 created 2011]