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.

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

     1 Oxidoreductases

         1.8 Acting on a sulfur group of donors

             1.8.5 With a quinone or similar compound as acceptor

                1.8.5.3 respiratory dimethylsulfoxide reductase

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Results	in table
2580	AA Sequence
7	Cloned(Commentary)
28	Cofactor
6	Crystallization (Commentary)
7	Expression
46	General Information
2	Inhibitors
70	kcat/KM [mM/s]
71	KM Value [mM]
11	Localization
19	Metals/Ions
1	Molecular Weight [Da]
19	Natural Substrates/ Products (Substrates)
55	Organism
5	Pathway
8	PDB ID
4	pH Optimum
1	pH Range
1	Posttranslational Modification
74	Protein Variants
2	Purification (Commentary)
5	Reaction
54	Reference
2	Source Tissue
10	Specific Activity [micromol/min/mg]
116	Substrates and Products (Substrate)
4	Subunits
61	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
1	Temperature Stability [°C]
80	Turnover Number [1/s]

Inhibitors

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Inhibitors on EC 1.8.5.3 - respiratory dimethylsulfoxide reductase

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

2-n-heptyl-4-hydroxyquinoline N-oxide

Escherichia coli

-

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

711196

2-n-heptyl-4-hydroxyquinoline-N-oxide

Escherichia coli

-

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

712339