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Literature summary for 1.8.5.3 extracted from
- Interaction of 2-n-heptyl-4-hydroxyquinoline-N-oxide with dimethyl sulfoxide reductase of Escherichia coli (1998), J. Biol. Chem., 273, 20758-20763.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H65R | mutation in subunit DmsC. Mutant blocks binding of the menaquinol analogue 2-n-heptyl-4-hydroxyquinoline-N-oxide to the protein | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 2-n-heptyl-4-hydroxyquinoline-N-oxide | 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 | Escherichia coli |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
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