Skip to main content
Log in

Regulation of the formation of protease inBacillus megaterium

I. The influence of amino acids on the enzyme formation

  • Published:
Folia Microbiologica Aims and scope Submit manuscript

Abstract

Protease is synthesized by the cultures growing in a glucose-containing mineral medium. However, it is formed even during incubation of the washed cells in a nitrogen free medium. The enzyme synthesis is decreased substantially by the addition of the individual amino acids or their mixture. Threonine, isoleucine, leucine and valine are the most inhibitory. Arginine, cysteine, glycine, lysine and tryptophan in concentrations of 103 m do not inhibit the production of protease. The growth of the culture is also somewhat inhibited by threonine and isoleucine, the repression of protease being, however, much higher. Concentrations of 103 m inhibit its synthesis by 80–90%. However, the enzyme activity is not influenced. The inhibition is caused byl,-isomers. Repression of the enzyme synthesis after the addition of threonine into the medium is much greater in a growing culture than in a culture starving in a nitrogen-free medium. However the level of free threonine in the pool is roughly the same in both growing and non-growing cultures. A mixture of 13 amino acids, which themselves are little inhibitory, suppresses the synthesis of protease much more than threonine or isoleucine. The inhibitory effect of the individual amino acids on the enzyme formation is apparently additive.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Armstrong, F. B., Wagner, R. P.:Repression of the valine — isoleucine pathway in Salmonella. Proc. nat. Acad. Sci.,49: 628, 1963.

    Article  PubMed  CAS  Google Scholar 

  • Bernlohr, R. W.:Postlogarithmic phase metabolism of sporulating microorganisms. I. Protease of Bacillus licheniformis. J. biol. Chem.239: 538, 1964.

    PubMed  CAS  Google Scholar 

  • Chaloupka, J.:Proteolytic enzymes of actinomyces Streptomyces griseus II. The influence of the nature and concentration of nitrogen on the secretion of protease. Čs. mikrobiol.1: 32, 1956.

    CAS  Google Scholar 

  • Chaloupka, J., Křečková, P.:Protease repression in Bacillus megaterium KM. Biochem. Biophys. Res. Commun.8: 120, 1962.

    Article  PubMed  CAS  Google Scholar 

  • Chaloupka, J., Křečková, P., Říhová, L.:Repression of protease in Bacillus megaterium by single aminoacid. Biochem. Biophys. Res. Commun.12: 380, 1963.

    Article  PubMed  CAS  Google Scholar 

  • Chaloupka, J., Liebster, J.:A proteolytic system in growing and non-growing cells of Escherichia coli, Fol. microbiol.4: 167, 1959.

    Article  CAS  Google Scholar 

  • Chaloupka, J., Liebster, J., Janeček, J.:The use of labeled substrates for the study of intracellular proteinases. Peaceful Uses of Atomic Energy. Proc. 2nd Int. conference, V. 25, p. 140, Geneva 1958.

  • Jacob, F., Monod, J.:Genetic regulatory mechanisms in the synthesis of proteins. J. mol. Biol.3: 318, 1961.

    Article  PubMed  CAS  Google Scholar 

  • Lowry, H. O., Rosenbrough, N. J., Farr, A. L., Randall, R. J.:Protein measurement with the folin phenol reagent. J. biol. Chem.193: 265, 1951.

    PubMed  CAS  Google Scholar 

  • Magasanik, B.:Catabolite repression. Cold Spring Harbor Symp. Quant. Biol.26: 249, 1961.

    PubMed  CAS  Google Scholar 

  • Mandelstam, J.:Induction and repression of β-galactosidase in non-growing Escherichia coli. Biochem. J.79: 489, 1961.

    PubMed  CAS  Google Scholar 

  • Mc Quillen, K.:Bacterial protoplasts: growth and division of protoplasts of Bacillus megaterium. Biochim. biophys. Acta,18: 485, 1955.

    Article  Google Scholar 

  • Merkel, J. R., Traganza, E. D., Mukherjee, B. B., Griffin, T. B., Prescott, J. M.:Proteolytic activity and general characteristics of a marine bacterium, Aeromonas proteolytica Sp. N. 1. J. Bacteriol.87: 1227, 1964.

    PubMed  CAS  Google Scholar 

  • Moore, S., Stein, W. H.:Procedures of the Chromatographic determination of amino acids on four per cent crosslinked sulfonated polystyrene resins. J. biol. Chem.211: 893, 1954.

    PubMed  CAS  Google Scholar 

  • Neumark, R., Citri, N.:Repression of protease formation in Bacillus cereus. Biochim. biophys. Acta,59: 749; 1962.

    Article  PubMed  CAS  Google Scholar 

  • Park, J. F., Hancock, R.:A fractionation procedure for the studies of the synthesis of cell wall mucopeptide and of other polymers in cells of Staphylococcus aureus. J. gen. Microbiol.,22: 249, 1960.

    PubMed  CAS  Google Scholar 

  • Rabin, R., Zimmerman, L. N.:Proteinase biosynthesis by Streptococcus liquefaciens. I. The effect of carbon and nitrogen sources, pH and inhibitors. Can. J. Microbiol.2: 747, 1956.

    Article  CAS  Google Scholar 

  • Tsuru, D.:Inhibitory effect by glycine on the production of amylase and proteinase by Bacillus subtilis. I. Effect of glycine and glycine derivatives on the enzyme production by the washed cells. Agr. Biol. Chem.26: 288, 1962.

    CAS  Google Scholar 

  • Vinter, V.:Sporulation of bacilli. II. Proteolytic enzymes in the process of sporulation of Bacillus megaterium. Čs. mikrobiol.1: 63, 1956a.

    CAS  Google Scholar 

  • Vinter, V.:Sporulation of bacilli III. Consumption of calcium by the cells and decrease in proteolytic activity of the medium during sporulation in Bacillus megaterium. Čs. mikrobiol.1: 145, 1956b.

    CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Chaloupka, J., Křečková, P. Regulation of the formation of protease inBacillus megaterium . Folia Microbiol 11, 82–88 (1966). https://doi.org/10.1007/BF02878835

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02878835

Keywords

Navigation