Advertisement

Activation of Pyruvate Oxidase and Interaction with Membrane Components

  • John G. Koland
  • Michael W. Mather
  • Robert B. Gennis
  • John S. White
  • Lowell P. Hager

Abstract

Pyruvate oxidase is one of several flavoprotein dehydrogenases that feed electrons into the E. coli respiratory chain. The enzyme catalyzes the oxidative decarboxylation of pyruvate to acetic acid and CO2 (Hager, 1957). Although usually a minor component in E. coli, it can be induced to higher levels in mutant strains and provides a pathway for pyruvate catabolism alternative to that of the pyruvate dehydrogenase complex. Pyruvate oxidase is a tetramer with identical subunits of 60,000 daltons (Williams and Hager, 1960; O’Brien et al., 1976). Each subunit has a tightly bound flav in adenine dinucleotide (FAD), and the addition of a second cofactor, thiamin pyrophosphate, is necessary to elicit catalytic activity. Enzymatic activity is easily monitored spectrophotometrically using ferricyanide as an artificial oxidant.

Keywords

Flavin Adenine Dinucleotide Hill Coefficient Turnover Number Midpoint Potential Nonanoic 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. Blake, R. (1977). Ph.D. dissertation, University of Illinois.Google Scholar
  2. Blake, R. Hager, L. P., and Gennis, R. B. (1978). J. Biol. Chem. 253, 1963–1971.Google Scholar
  3. Breslow, R. (1958). J. Am. Chem. Soc. 80, 3719–3726.CrossRefGoogle Scholar
  4. Cunningham, C. C., and Hager, L. P. (1971). J. Biol. Chem. 246, 1575–1582.Google Scholar
  5. Cunningham, C. C., and Hager, L. P. (1971). J. Biol. Chem. 246, 1583–1589.Google Scholar
  6. Cunningham, C. C., and Hager, L. P. (1975). J. Biol. Chem. 250, 7139–7146.Google Scholar
  7. Haddock, B. A., and Jones, C. W. (1977). Bacteriol. Rev. 41, 47–99.Google Scholar
  8. Hager, L. P. (1957). J. Biol. Chem. 229, 251–263.Google Scholar
  9. Hager, L. P., and Krampitz, L. O. (1963). Fed. Proc. 22, 536.Google Scholar
  10. Hendler, R. W., and Shrager, R. I. (1979). J. Biol. Chem. 254, 11288–11299.Google Scholar
  11. Houghton, R. L. (1979). Int. J. Biochem. 10, 205–208.CrossRefGoogle Scholar
  12. Krampitz, L. O. (1969). Annu. Rev. Biochem. 38, 213–239.CrossRefGoogle Scholar
  13. Massey, V., and Hemmerich, P. (1980). Biochem. Soc. Trans. 8, 246–257.Google Scholar
  14. O’Brien, T. A., and Gennis, R. B. (1980). J. Biol. Chem. 255, 3302–3307.Google Scholar
  15. O’Brien, T. A., Schrock, H. L., Russell, P., Blake, R., and Gennis, R. B. (1976). Biochim. Biophys. Acta 452, 13–29.Google Scholar
  16. O’Brien, T. A., Blake, R., and Gennis, R. B. (1977). Biochemistry 16, 3105–3109.CrossRefGoogle Scholar
  17. Palmer, G., and Massey, V. (1968). In Biological Oxidations (T. P. Singer, ed.), pp. 263–300, Interscience, New York.Google Scholar
  18. Pudek, M. R., and Bragg, P. D. (1976). Arch. Biochem. Biophys. 174, 546–552.CrossRefGoogle Scholar
  19. Raj. T., Russell, P., Flygare, W. H., and Gennis, R. B. (1977). Biochem. Biophys. Acta 481, 42–49.Google Scholar
  20. Reid, G. A., and Ingledew, W. J. (1979). Biochem. J. 182, 465–472.Google Scholar
  21. Russell, P. (1979). Ph.D. dissertation, University of Illinois.Google Scholar
  22. Russell, P., Hager, L. P., and Gennis, R. B. (1977). J. Biol. Chem. 252, 7877–7882.Google Scholar
  23. Russell, P., Schrock, H. L., and Gennis, R. B. (1977). J. Biol. Chem. 252, 7883–7887.Google Scholar
  24. Schrock, H. L., and Gennis, R. B. (1977). J. Biol. Chem. 252, 5990–5995.Google Scholar
  25. Schrock, H. L., and Gennis, R. B. (1980). Biochim. Biophys. Acta 614, 215–220.Google Scholar
  26. Williams, F. R., and Hager, L. P. (1960). Biochim. Biophys. Acta 38, 566–567.CrossRefGoogle Scholar
  27. Williams, F. R., and Hager, L. P. (1966). Arch. Biochem. Biophys. 116, 168–176.CrossRefGoogle Scholar
  28. Yamato, I., Anraku, Y., and Hirosawa, K. (1975). J. Biochem. (Tokyo) 77, 705–718.Google Scholar

Copyright information

© Plenum Press, New York 1982

Authors and Affiliations

  • John G. Koland
    • 1
  • Michael W. Mather
    • 1
  • Robert B. Gennis
    • 1
  • John S. White
    • 2
  • Lowell P. Hager
    • 2
  1. 1.Department of Chemistry, School of Chemical SciencesUniversity of IllinoisUrbanaUSA
  2. 2.Department of Biochemistry, School of Chemical SciencesUniversity of IllinoisUrbanaUSA

Personalised recommendations