Basic properties of the pyruvate dehydrogenase complex isolated from aurochs heart

• Autorzy: Czygier M. , Strumilo S.A.
• Języki publikacji: EN

Abstrakty

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 Michael is constant values for aurochs heart PDC are 22.4 ± 1.0,3.3 ± 0.1 and 24.4 ± 3.6 uM for pyruvate, CoA and NAD, accordingly. Acetyl-CoA is a competitive inhibitor with respect to CoA (Ki = 14.2 ± 0.4 uM), whereas NADH gives the same inhibition with respcct to NAD (Ki = 46.9 +10.0 uM). The Km for CoA and NAD of the aurochs heart PDC are lower than that of domestic animals PDC.

Słowa kluczowe

EN

basic property; pyruvate dehydrogenase complex; aurochs heart

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1994
• Tom: 41
• Numer: 4
• Opis fizyczny: p.453-457,fig.

Twórcy

autor

Czygier M.

• University of Warsaw, Branch in Bialystok, Swierkowa 20 B, 15-950 Bialystok, Poland

autor

Strumilo S.A.

Bibliografia

• 1. Hochachka, P.W. & Somcro, C.N. (1973) Strate­gies of biochemical adaptation. W.B. Saunders Company, Philadelphia, London, Toronto.
• 2. Somcro, G.N. & Hochachka, P.W. (1971) Bioche­mical adaptation to the environment. Amcr. Zoologist 11, 159-167.
• 3. Fortin, D., Coulon, J.F. & Roberge, A.C. (1993) Biochemical parameters and kinetic properties of dopamine-P-hydroxylase activity from cat and rat adrenals. Ccnnp. Biochem. Physiol. 104B, 567-576.
• 4. Ogawa, H., Comi, T. & Fujioka, M. (1993) Mammalian glycine N-methyltransferases — comparative kinetic and structural properties of the enzymes from human, rat, rabbit and pig liver. Camp. Biochem. Physiol. 106B, 601-612.
• 5. Linn, T.C., Pelley, J.W., Pettit, F.H., Hucho, F., Randall, D.D. & Reed, L.J. (1972) a-Keto acid dehydrogenase complexes. XV. Purification and properties of the component enzymes of the pyruvate dehydrogenase complexes from bovine kidney and heart. Arch. Biochem. Biophys. 148,327-342.
• 6. Barrera, C.R., Namihira, G., Hamilton, L., Munk, P., Eley, M.H., Linn, T.C. & Reed, L.j. (1972) a-Keto acid dehydrogenase complexes. XVI. Studies on the subunit structure of the pyruvate dehydrogenase complexes from bovine kidney and heart. Arch. Biochetn. Biophys. 148,345-358.
• 7. Hucho, F., Randall, D.D., Roche, T.E., Burgett, M.W., Pelley, J.M. & Reed, L.J. (1972) a-Kcto acid dehydrogenase complexes. XVII. Kinetic and regulatory properties of pyruvate dehydro­genase kinase and pyruvate dehydrogenase phosphatase from bovine kidney and heart. Arch. Biochem. Biophys. 151,328-340.
• 8. Strumilo, S.A. (1988) Hysteresis behaviour of the pyruvate dehydrogenase complex contain­ing endogenous thiamin pyrophosphate; in Tia- min pyrophosphate biochemistry (Schellenberger, A. & Schowen, R.L., eds.) pp. 83-91, CRC Press, Boca Raton, Florida.
• 9. Wieland, O.H. (1983) The mammalian pyruvate dehydrogenase complcx: structure and regula­tion. Rev. Physiol. Biochem. Pharmacol. 96, 123-170.
• 10. Yeaman, S.J. (1989) The 2-oxo acid dehydro­genase complex: recent advances. Biochem. /. 257,625-632.
• 11. Patel, M.S. & Roche, T.E. (1990) Molecular biology and biochemistry of pyruvate dehydro­genase complexes. FASEB J. 4,3224-3233.
• 12. Stanley, C.J. & Perham, R.N. (1980) Purification of 2-oxo acid dehydrogenase multienzyme complexes from ox heart — a new method. Biochem. J. 191,147*-154.
• 13. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227,680-485.
• 14. Keleti, T. (1986) Basic enzyme kinetics. Akademiai Kiado, Budapest.
• 15. Roche, T.E. & Cate, R.L. (1977) Purification of porcine liver pyruvate dehydrogenase complex and characterization of its catalytic and regula­tory properties. Arch. Biochem. Biophys. 183, 664-677.
• 16. Walsh, D.A., Cooper, R.H., Denton, R.M., Bridges, B.J. & Randle, P.J. (1976) The elementary reactions of the pig heart pyruvate dehydrogenase complex. A study of the inhibition by phosphorylation. Biochetn. J. 157, 41 -67.
• 17. Kiselevsky, Y.V., Ostrovtsova, S.A. & Strumilo, S.A. (1990) Interaction of the pyruvate dehydro­genase complex from human heart with tiamine pyrophosphate. Biomed. Biochim. Acta 49, 285-287.
• 18. Tsai, C.S., Burgett, M.W. & Reed, L.J. (1973) a-Keto acid dehydrogenase complexes. XX. A kinetic study of the pyruvate dehydrogenase complex from bovine kidney. J. Biol. Chem. 248, 8348-8352.
• 19. Siess, E.A., Wittmann, I. & Wieland, O.H. (1971) Interconversion and kinetic properties of pyru­vate dehydrogenase from brain. Hoppe-Seyler's Z. Physiol. Chem. 352,447-452.
• 20. Kiselevsky, Y.V., Ostrovtsova, S.A. & Strumilo, S.A. (1990) Kinetic characterization of the pyruvate and oxoglutarate dehydrogenase complexes from human heart. Acta Biochim. Polon. 37,135-139.
• 21. Strumilo, S., Kiselevsky, Y. & Ostrovtsova, S. (1991) Properties of the 2-oxo acid dehydro­genase complexes from human heart; in Bioche­mistry and Physiology of Thiamin Diphosphate Enzymes (Bisswanger, H. & Ullrich, J., eds.) pp. 200-208, Verlag-Chemie, Weinheim.