Changes in some properties of the aurochs heart pyruvate dehydrogenase complex induced by its partial phosphorylation.
Comparative studies on the properties of the dephosphorylated and partially phosphorylated (to 35% activity reduction) pyruvate dehydrogenase complex (PDC) from aurochs heart muscle have been made. Data have been obtained indicating that the partial phosphorylation of PDC abolishes the kinetic attributes of a positive cooperativity of the pyruvate binding sites (nH = 1.5) featuring at low substrate concentrations. In addition, the partially phosphorylated PDC is inactivated slower at 50 degrees C.
Czygier
M B
MB
Institute of Biology, University of Warsaw Branch, Biafystok, Poland.
Strumilo
S A
SA
D000818:Animals; D001665:Binding Sites; D016164:Bison / Q000378:metabolism*; D004795:Enzyme Stability; D007700:Kinetics; D009206:Myocardium / Q000201:enzymology*; D010766:Phosphorylation; D011768:Pyruvate Dehydrogenase Complex / Q000378:metabolism*; D013835:Thiamine Pyrophosphate / Q000378:metabolism*
D011768:Pyruvate Dehydrogenase Complex; D013835:Thiamine Pyrophosphate