Further evidence for direct interaction of pyruvate dehydrogenase multienzyme complex with citric acid cycle based on nonlinearity of hill plots in presence of C2 and C4 substrate analogues.
1. Mammalian pyruvate dehydrogenase multienzyme complex (PDC) is measured with two different optical assays: (i) formation of p-nitro-acetanilid with arylamine-acetyltransferase and (ii) NAD reduction. 2. It is found that in contrast to the NAD assay system (ii) the coupled system (i) exhibits cooperativity with a Hill coefficient n = 3 over the whole range of substrate concentration. 3. The cooperative behaviour can be modified by presence of dichloroacetate (n = 2) and acetoin (n = 1----3). From additional measurements of PDC activity with toluene permeabilized mitochondria of fed and starved rats it is concluded that PDC activity in vivo is modified by changes in enzyme enzyme aggregation and interaction beside the known phosphorylation dephosphorylation mechanism.
Institut für Physiologische Chemie II, Universität Düsseldorf, B.R.D.
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D000818:Animals; D001665:Binding Sites; D002952:Citric Acid Cycle / Q000502:physiology*; D007700:Kinetics; D008297:Male; D008930:Mitochondria, Liver / Q000201:enzymology / Q000378:metabolism; D011768:Pyruvate Dehydrogenase Complex / Q000378:metabolism*; D011773:Pyruvates / Q000378:metabolism; D051381:Rats; D012044:Regression Analysis; D013379:Substrate Specificity; D013552:Swine; D014050:Toluene / Q000494:pharmacology
D011768:Pyruvate Dehydrogenase Complex; D011773:Pyruvates; D014050:Toluene