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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |