title: Basic properties of the pyruvate dehydrogenase complex isolated from aurochs heart.
abstract: The purified aurochs (Bison bonasus, European bison) heart pyruvate dehydrogenase complex (PDC) has a set of subunits typical of mammalian PDC. PDC from aurochs heart contains firmly bound tiamine pyrophosphate in the amount providing over 50% of the maximal activity of the complex. The apparent value for activation energy of PDC is 60 kJ/mol. The Michaelis constant values for aurochs heart PDC are 22.4 +/- 1.0, 3.3 +/- 0.1 and 24.4 +/- 3.6 microM for pyruvate, CoA and NAD, accordingly. Acetyl-CoA is a competitive inhibitor with respect to CoA (Ki = 14.2 +/- 0.4 microM), whereas NADH gives the same inhibition with respect to NAD (Ki = 46.9 +/- 10.0 microM). The Km for CoA and NAD of the aurochs heart PDC are lower than that of domestic animals PDC.
authors.affiliation: Department of Biochemistry, University of Warsaw, Białystok, Poland.
authors.forename: M
authors.initials: M
authors.lastname: Czygier
authors.forename: S A
authors.initials: SA
authors.lastname: Strumiło
mesh_terms: D000818:Animals; D016164:Bison; D007700:Kinetics; D009206:Myocardium / Q000201:enzymology*; D011768:Pyruvate Dehydrogenase Complex / Q000737:chemistry* / Q000302:isolation & purification*
chemical_list: D011768:Pyruvate Dehydrogenase Complex