Advertisement

The Pyruvate Dehydrogenase Complex of E. coli K-12 Structure and Synthesis

  • U. Henning
  • O. Vogel
  • W. Busch
  • J. E. Flatgaard
Part of the Colloquium der Gesellschaft für Biologische Chemie 13.–15. April 1972 in Mosbach/Baden book series (MOSBACH, volume 23)

Abstract

Since the pioneering experiments of Gunsalus and Hager [1] and of Koike, Reed, and Carroll [2, 3] α-ketoacid dehydrogenase complexes from a number of sources have been studied from many aspects. These enzymes catalyze an oxidative decarboxylation according to:
$$R - \mathop C\limits^{\mathop \parallel \limits^0 } - C{O_2}H + CoA + NAD + \to C{O_2} + R - \mathop C\limits^{\mathop \parallel \limits^0 } - S - CoA + NADH + H + $$
(1)
This overall reaction, proceeding with enzyme bound intermediates, requires three different enzyme components present in the complex : an α-ketoacid dehydrogenase (enzyme 1, E 1), a dihydrolipoamide transacetylase (E 2), and a dihydrolipoamide dehydrogenase (E 3). In the case of the pyruvate dehydrogenase complex they effect reaction (1) by the following sequence of reactions:
$$Pyruvate + TPP - E1 \to C{0_2} + {\text{Hydroxyethyl - TPP - E1}}$$
(2)
$${\text{Hydroxyethyl - TPP - E1 + Lipoyl - E2}} \to {\text{S - acetyl - dihydrolipoyl - E2 + TPP - E1}}$$
(3)
$${\text{S - Acetyl - dihydrolipoyl - E2 + CoA}} \to {\text{Acetyl - CoA}} + {\text{Dihydrolipoyl - E2}}$$
(4)
$${\text{Dihydrolipoyl - E2 + FAD - E3}} \to {\text{Lipoyl - E2 + reducedFAD - E3}}$$
(5)

Keywords

Polypeptide Chain Enzyme Complex Pyruvate Dehydrogenase Core Complex Lipoic Acid 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Gunsalus, I. C.: In: A symposium on the mechanism of enzyme action, p. 545 ( McElroy, W. D., Glass, B., Eds.). Baltimore: The Johns Hopkins Press 1954.Google Scholar
  2. 2.
    Koike, M., Reed, L. J., Carroll, W. R.: J. biol. Chem. 235, 1924 (1960).PubMedGoogle Scholar
  3. 3.
    Koike, M., Reed, L. J., Carroll, W. R.: J. biol. Chem. 238, 30 (1963).PubMedGoogle Scholar
  4. 4.
    Henning, U., Herz, C., Szolyvay, K.: Z. Vererbungsl. 95, 236 (1964).Google Scholar
  5. 5.
    Henning, U., Dietrich, J., Murray, K. N., Deppe, G.: In: Molecular genetics, p. 223 ( Schuster, H., Wittmann, G., Ed.). Berlin-Heidelberg-New York: Springer 1968.CrossRefGoogle Scholar
  6. 6.
    Dietrich, J., Henning, U.: Europ. J. Biochem. 14, 258 (1970).PubMedCrossRefGoogle Scholar
  7. 7.
    Flatgaarn, J. E., Hoehn, B., Henning, U.: Arch. Biochem. 143, 461 (1971).CrossRefGoogle Scholar
  8. 8.
    Vogel, O., Beikrich, H., Müller, H., Henning, U.: Europ. J. Biochem. 20, 169 (1971).PubMedCrossRefGoogle Scholar
  9. 9.
    Vogel, O., Henning, U.: Europ. J. Biochem. 18, 103 (1970).CrossRefGoogle Scholar
  10. 10.
    Williams, C. H.: J biol. Chem. 240, 4793 (1965).PubMedGoogle Scholar
  11. 11.
    Vogel, O., Höhn, B., Henning, U.: Europ. J. Biochem. (in press).Google Scholar
  12. 12.
    Vogel, O., Höhn, B., Henning, U.: Proc. nat. Acad. Sci. (Wash.) 69, 1615 (1972).CrossRefGoogle Scholar
  13. 13.
    Desnuelle, P.: In: The enzymes, 2nd Ed., Vol. 4, p. 93 ( Boyer, P., Lardy, H., Myrback, K., Eds.). New York: Acad. Press 1960.Google Scholar
  14. 14.
    Perham, R. N., Thomas, J. O.: FEBS Letters 15, 8 (1971).PubMedCrossRefGoogle Scholar
  15. 15.
    Busces, W., Henning, U.: In preparation.Google Scholar
  16. 16.
    Drapeau, G. R., Brammar, W. J., Yanofsky, C.: J. molec. Biol. 35, 357 (1968).PubMedCrossRefGoogle Scholar
  17. 17.
    Henning, U., Dennert, G., Hertel, R., Shipp, W. S.: Cold Spr. Harb. Symp. quant. Biol. 31, 227 (1966).CrossRefGoogle Scholar
  18. 18.
    Fernandes-Moran, H., Reed, L. J., Koike, M., Willms, C. R.:Science 145, 930 (1964).Google Scholar
  19. 19.
    Willms, C. R., Oliver, R. M., Henney, H. R., Mukherjee, B. B., Reed, L. J.: J. biol. Chem. 242, 889 (1967).PubMedGoogle Scholar
  20. 20.
    Reed, L. J., Oliver, R. M.: Brookhaven Symp. Biol. 21, 397 (1968).PubMedGoogle Scholar
  21. 21.
    Reed, L. J., Oliver, R. M.: In: Current topics in cellular regulation, p. 233 ( Horecker, B. L., Stadtman, E. R., Eds.). New York: Acad. Press 1969.Google Scholar
  22. 22.
    Rosenbaum, M.: Nature (Lond.) New Biology 230, 12 (1971).Google Scholar

Copyright information

© Springer-Verlag Berlin · Heidelberg 1972

Authors and Affiliations

  • U. Henning
    • 1
  • O. Vogel
    • 1
  • W. Busch
    • 1
  • J. E. Flatgaard
    • 1
  1. 1.Max-Planck-Institut für BiologieTübingenGermany

Personalised recommendations