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Literature summary for 4.2.1.157 extracted from

  • Kim, J.; Pierik, A.; Buckel, W.
    A complex of 2-hydroxyisocaproyl-Coenzyme A dehydratase and its activator from clostridium difficile stabilized by aluminium tetrafluoride-adenosine diphosphate (2010), Chemphyschem, 11, 1307-1312.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
[4Fe-4S]-center
-
Clostridioides difficile

Inhibitors

Inhibitors Comment Organism Structure
AlF4- AlF4 in combination with ADP traps the interaction of the activator protein with the dehydratase by forming a stable complex containing 1.0 mol homodimeric activator, 1.0 mol heterodimeric dehydratase and 1.2 mol ADP. The formation proceeds much slower than the activation but in an almost irreversible manner. The isolated complex is devoid of any activity Clostridioides difficile

Metals/Ions

Metals/Ions Comment Organism Structure
Iron the complex of the heterodimeric dehydratase and the homodimeric activator complex contains per mol 8.5 mol Fe corresponding to the sum of 5.0 mol Fe/mol dehydratase and 3.7 mol Fe/mol activator Clostridioides difficile

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
148000
-
1:1 protein complex of the heterodimeric dehydratase (89 kDa) and the homodimeric activator (60 kDa), stable only in the presence of AlF4-, gel filtration Clostridioides difficile

Organism

Organism UniProt Comment Textmining
Clostridioides difficile
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-
-