1887

Abstract

Summary: Experiments have been carried out on the kinetics of induced synthesis of lysine decarboxylase in washed suspensions of The enzyme is produced when glucose and lysine are present simultaneously. Lysine analogues tested as inducers were inactive. In anaerobic synthesis the rate of formation of new enzyme is directly proportional to the degree of saturation of the enzyme by its substrate; in aerobic synthesis a maximal rate is found even when the enzyme is almost totally unsaturated. The pH curve for enzyme synthesis corresponds closely with that for enzyme activity. Adapted cells undergo de-adaptation when incubated with glucose in the absence of lysine; this is due to the effect of cadaverine on the co-enzyme. The bearing of these results on current theories of enzyme induction is discussed.

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/content/journal/micro/10.1099/00221287-11-3-426
1954-12-01
2024-04-24
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References

  1. Cohen P.P. 1940; Transamination with purified enzyme preparations (transaminase). J. biol. Chem. 136:565
    [Google Scholar]
  2. Dixon M. 1953; The determination of enzyme inhibitor constants. Biochem. J. 55:171
    [Google Scholar]
  3. Galat A. 1947; An improved synthesis of DL-lysine. J. Amer. Chem. Soc. 69:86
    [Google Scholar]
  4. Gale E.F. 1940; The production of amines by bacteria. 1. The decarboxylation of amino-acids by strains of Bact. Coli. . Biochem. J. 34:392
    [Google Scholar]
  5. Gale E.F. 1947; The assimilation of amino-acids by bacteria. 1. The passage of certain amino-acids across the cell wall and their concentration in the internal environment of Streptococcus Faecalis. . J.Gen. Microbiol. 1:53
    [Google Scholar]
  6. Gaudry R. 1948; The synthesis of sl-α-amino-ɛ-hydroxycaproic acid and a new synthesis of dl-lysine. Canad. J. Res. B 26:387
    [Google Scholar]
  7. Mclaren A.D., Knight C.A. 1951; Preparation and microbiological activity of an homolog of lysine. J. Amer. Chem. Soc. 73:4478
    [Google Scholar]
  8. Mandelstam J. 1952; Studies in biochemical adaptation. The ‘mass action’ theory of enzyme adaptation. Biochem. J. 51:674
    [Google Scholar]
  9. Mandelstam J., Yudkin J. 1952; Studies in biochemical adaptation. Some aspects of galactozymase production by yeast in relation to the ‘mass action’ theory of enzyme adaptation. Biochem. J. 51:686
    [Google Scholar]
  10. Monod J., Cohn M. 1952; La biosynthse induite des enzymes (adaptation enzymatique). Advanc. Enzymol. 13:67
    [Google Scholar]
  11. Monod J., Cohen-Bazire G., Cohn M. 1951; Sur la biosynth�se de la βgalactosidase (lactase) chez Esch. Coli. La specificité de l’induction. Biochim. Biophys.Acta 7:585
    [Google Scholar]
  12. Neuberger A., Sanger F. 1943; Availability of acetyl derivatives of lysine for growth. Biochem. J. 37:515
    [Google Scholar]
  13. Oesterlin M. 1932; Über die Darstellung von Aminbasen aus Carbons�uren mittels Stickstoffwasserstoffsäure. Z. Angew. Chem. 45:536
    [Google Scholar]
  14. Pollock M.R. 1950; Penicillinase adaptation in B. Cereus: adaptive enzyme formation in the absence of free substrate. Brit. J. Exp. Path. 31:739
    [Google Scholar]
  15. Rodwell A.W. 1953; Factors affecting the activation of the ornithine decarboxylase of a strain of Lactobacillus. . J. Gen. Microbiol. 8:238
    [Google Scholar]
  16. Sanger F. 1946; The free amino group of gramicidin S. Biochem. J. 40:261
    [Google Scholar]
  17. Yudkin J. 1938; Enzyme variation in micro-organisms. Biol. Rev. 13:93
    [Google Scholar]
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