1.8.5.3: respiratory dimethylsulfoxide reductase
This is an abbreviated version!
For detailed information about respiratory dimethylsulfoxide reductase, go to the full flat file.
Word Map on EC 1.8.5.3
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1.8.5.3
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rhodobacter
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sphaeroides
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molybdoenzyme
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molybdopterin
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capsulatus
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dithiolene
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pyranopterins
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narghi
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tord
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bismolybdopterin
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mo-containing
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high-g
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menaquinol
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wiv
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frdabcd
- 1.8.5.3
- rhodobacter
- sphaeroides
-
molybdoenzyme
- molybdopterin
- capsulatus
-
dithiolene
-
pyranopterins
- narghi
- tord
-
bismolybdopterin
-
mo-containing
-
high-g
- menaquinol
- wiv
- frdabcd
Reaction
Synonyms
dimethyl sulfoxid reductase, dimethyl sulfoxide reductase, dimethyl sulfoxide/trimethylamine N-oxide reductase, dimethyl sulfoxie reductase, dimethylsulfoxide reductase, dms, DmsA, DmsABC, DmsABC sulfoxide reductase, DmsC, DMSO reductase, DMSOR, dorA, More, respiratory dimethyl sulfoxide reductase
ECTree
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Inhibitors
Inhibitors on EC 1.8.5.3 - respiratory dimethylsulfoxide reductase
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2-n-heptyl-4-hydroxyquinoline N-oxide
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residues Pro80, Ser81, Cys102, and Tyr104 of electron transfer subunit DmsB are located at the DmsB-DmsC interface and are critical for the binding of the MQH2 inhibitor analogue 2-n-heptyl-4-hydroxyquinoline N-oxide
2-n-heptyl-4-hydroxyquinoline-N-oxide
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menaquinol analogue. 2-n-Heptyl-4-hydroxyquinoline-N-oxide fluorescence is quenched when 2-n-heptyl-4-hydroxyquinoline-N-oxide binds to the holoenzyme DmsABC. The binding stoichiometry is about 1:1. There is one high-affinity 2-n-heptyl-4-hydroxyquinoline-N-oxide binding site per DmsABC molecule located in the DmsC subunit. The interaction follows a two-step equilibrium model, a fast bimolecular step followed by a slow unimolecular step. The quenching of 2-n-heptyl-4-hydroxyquinoline-N-oxide fluorescence occurs in the bimolecular step