Literature summary extracted from
Kim, J.; Lu, Y.; Buckel, W.
ATP- and redox-induced conformational changes in the activator of the radical enzyme 2-hydroxyisocaproyl-CoA dehydratase (2007), C. R. Chimie, 10, 742-747.
No PubMed abstract available
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
4.2.1.157 |
additional information |
a [4Fe-4S] cluster-containing protein activates 2-hydroxyisocaproyl-CoA dehydratase by an ATP-driven electron transfer. Reduction of the activator protein and binding of ATP induce conformational changes necessary to transfer the electron to the dehydratase. Interaction of both proteins promotes ATP hydrolysis |
Clostridioides difficile |
|
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
4.2.1.157 |
bathophenanthroline |
a [4Fe-4S] cluster-containing protein activates 2-hydroxyisocaproyl-CoA dehydratase by an ATP-driven electron transfer. Iron chelation by bathophenanthroline removes the reduced [4Fe-4S] cluster from the activator protein in an ATP-dependent manner. With ADP, no chelation is observed. Chelation of the oxidised [4Fe-4S] cluster occurs faster with ADP than with ATP |
Clostridioides difficile |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.2.1.157 |
Clostridioides difficile |
- |
- |
- |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
4.2.1.157 |
[4Fe-4S]-center |
a [4Fe-4S] cluster-containing protein activates 2-hydroxyisocaproyl-CoA dehydratase by an ATP-driven electron transfer. Iron chelation by bathophenanthroline removes the reduced [4Fe-4S] cluster from the activator protein in an ATP-dependent manner. With ADP, no chelation is observed. Chelation of the oxidised [4Fe-4S] cluster occurs faster with ADP than with ATP |
Clostridioides difficile |
|