Calmodulin antagonists inhibit the mitochondrial pyruvate dehydrogenase complex.
1987
Abstract Calmodulin antagonists, including phenothiazine, sulfonamide, butyrophenone, and imidazolium derivatives, were in vitro inhibitors of pea mitochondrial pyruvate dehydrogenase complex activity. Inhibition was observed both during direct assay of the partially purified complex and during assay of pyruvate oxidation by isolated, intact mitochondria. When tested against the purified complex, the sulfonamide compound N-(6-aminohexyl)-5-chloro-1-naphthalene sulfonamide (W-7) was a competitive inhibitor with respect to coenzyme A and an uncompetitive inhibitor with respect to NAD and pyruvate. Inhibition of a process as crucial as mitochondrial respiration should serve to emphasize the care necessary in interpretation of whole-organism calmodulin antagonist studies.
Keywords:
- Mitochondrial pyruvate dehydrogenase complex
- Pyruvate dehydrogenase phosphatase
- Oxoglutarate dehydrogenase complex
- Pyruvate decarboxylation
- Pyruvate dehydrogenase kinase
- Pyruvate dehydrogenase complex
- Biochemistry
- Molecular biology
- Dihydrolipoyl transacetylase
- Branched-chain alpha-keto acid dehydrogenase complex
- Biology
- Correction
- Source
- Cite
- Save
- Machine Reading By IdeaReader
14
References
29
Citations
NaN
KQI