Role of Proteinases and Their Inhibitors in the Regulation of Yeast Metabolism

  • Helmut Holzer


Further experiments on the tryptophan synthase proteolyzing system of yeast are presented. This report describes the isolation of two proteinases, their identification with the proteinases A and B of Hata et al ., (1967a), the isolation and characterization of macromolecular inhibitors of these enzymes, their substrate specificity with respect to other yeast enzymes, and the role and control of the overall system under different growth conditions. Furthermore, it has been shown that tryptophan synthase inactivating proteinase II is identical to the chitin synthase activating enzyme, while the inhibitor of the tryptophan synthase proteolyzing enzymes is identical to the inhibitor of the chitin synthase activating proteinase described by Cabib and Ulane (1973). Possible mechanisms allowing for the specific proteolytic modification of certain enzymes in response to physiological demands are discussed.


Substrate Enzyme Limited Proteolysis Amino Acid Ester Disc Electrophoresis Yeast Metabolism 
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  1. Aibara, S., Hayashi, R., and Hata, T., (1971), Agric. BioZ. Chem., 35, 658.CrossRefGoogle Scholar
  2. Cabib, E., and Farkas, V., (1971), Proc. Nat. Acad. Sci. USA., 68, 2052.CrossRefGoogle Scholar
  3. Cabib, E., and Keller, F. A., (1971), J. Biol. Chem., 246, 167.Google Scholar
  4. Cabib, E.,.and Ulane, R., (1973), Biochem. Biophys. Res. Commun., 50, 186.CrossRefGoogle Scholar
  5. Doi, E., Hayashi, R., and Hata, T., (1967), Agric. Biol. Chem., 31, 160.CrossRefGoogle Scholar
  6. Ferguson, A. R., Katsunuma, T., Betz, H., and Holzer, H., (1973), Eur. J. Biochem.32,444.Google Scholar
  7. Hasilik,A,and Holzer,H.(1973),Biochem.Biophys.Res. Commun,in the press.Google Scholar
  8. Hata, T.,Hayashi,R.,and Doi, E.,(1967a),Agric. Biol. Chem., 31,150.Google Scholar
  9. Hata, T.,Hayashi,R.,and Doi, E.,(1967b),Agric. Biol. Chem., 31,357.Google Scholar
  10. Juni, E. and Heym, G. A.,(1968a), Arch. Biochem.Biophys.,127,79.Google Scholar
  11. Juni, E. and Heym, G. A.,(1968b), Arch. Biochem.Biophys.,127,89.Google Scholar
  12. Katsunuma, T., Schött,E.H.,Elsässer, S., and Holzer, H., (1972), Eur. J. Biochem., 27, 520.CrossRefGoogle Scholar
  13. Katunuma, N., Kito, K., and Kominami, E., (1971a), Biochem. Biophys. Res. Commun., 45, 76.CrossRefGoogle Scholar
  14. Katunuma, N., Kominami, E., and Kominami, S., (1971b), Biochem. Biophys. Res. Commun., 45, 70.CrossRefGoogle Scholar
  15. Lenney, J. F., and Dalbec, J. M., (1967), Arch. Biochem. Biophys., 120, 42.Google Scholar
  16. Lenney, J. F., and Dalbec, J. M., (1969), Arch. Biochem. Biophys., 129, 407.CrossRefGoogle Scholar
  17. Manney, T. R., (1968), J. Bacteriol., 96, 403.Google Scholar
  18. Schött, H. E., (1973), Doctoral Dissertation, University of Freiburg (German).Google Scholar
  19. Schött, H. E., and Holzer, H., (1973), Eur. J. Biochem.,submitted.Google Scholar

Copyright information

© Springer-Verlag Berlin · Heidelberg 1974

Authors and Affiliations

  • Helmut Holzer
    • 1
  1. 1.Abteilung für Enzymchemie des Instituts für Biochemie der Gesellschaft für Strahlen- und UmweltforschungBiochemisches Institut der Universität FreiburgFreiburg i. BrW. Germany

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