An investigation of the kinase activity of aurochs heart pyruvate dehydrogenase complex.
The purified aurochs heart pyruvate dehydrogenase complex (PDC) saturated to approximation 60% with endogenous thiamine pyrophosphate (TPP), was slowly and incompletely inactivated by its kinase in the presence of ATP. Exogenous TPP or ADP, but not pyruvate, strongly inhibited the kinase activity. The kinetic properties of the aurochs heart PDC kinase suggested the occurrence of two active sites each with different affinities for ATP (K'm - 1.7 microM, K''m = 48 microM).
Czygier
M
M
Department of Biochemistry, University of Warsaw, Bialystok, Poland.
Strumilo
S
S
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D016164:Bison; D007700:Kinetics; D009206:Myocardium / Q000201:enzymology*; D010770:Phosphotransferases / Q000378:metabolism*; D011768:Pyruvate Dehydrogenase Complex / Q000378:metabolism*
D011768:Pyruvate Dehydrogenase Complex; D000255:Adenosine Triphosphate; D010770:Phosphotransferases