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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