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Literature summary for 4.2.1.157 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
Search for more literature for 4.2.1.157

Activating Compound

Activating Compound Comment Organism Structure
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

Inhibitors Comment Organism Structure
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

Organism UniProt Comment Textmining
Clostridioides difficile
-
-
-

Cofactor

Cofactor Comment Organism Structure
[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