| EC |
1.8.5.3 |
| Accepted name: |
respiratory dimethylsulfoxide reductase |
| Reaction: |
dimethylsulfide + menaquinone + H2O = dimethylsulfoxide + menaquinol |
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For diagram of dimethyl sulfide catabolism, click here |
| Other name(s): |
dmsABC (gene names); DMSO reductase (ambiguous); dimethylsulfoxide reductase (ambiguous) |
| Systematic name: |
dimethyl sulfide:menaquinone oxidoreductase |
| Comments: |
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: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Daruwala, R. and Meganathan, R. Dimethyl sulfoxide reductase is not required for trimethylamine N-oxide reduction in Escherichia coli. FEMS Microbiol. Lett. 67 (1991) 255–259. [PMID: 1769531] |
| 2. |
Miguel, L. and Meganthan, R. Electron donors and the quinone involved in dimethyl sulfoxide reduction in Escherichia coli. Curr. Microbiol. 22 (1991) 109–115. |
| 3. |
Simala-Grant, J.L. and Weiner, J.H. Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase. Microbiology 142 (1996) 3231–3239. [DOI] [PMID: 8969520] |
| 4. |
Rothery, R.A., Trieber, C.A. and Weiner, J.H. Interactions between the molybdenum cofactor and iron-sulfur clusters of Escherichia coli dimethylsulfoxide reductase. J. Biol. Chem. 274 (1999) 13002–13009. [DOI] [PMID: 10224050] |
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| [EC 1.8.5.3 created 2011, modified 2019] |
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