Springer Nature is making Coronavirus research free. View research | View latest news | Sign up for updates

Enzyme induction and repression in anabolic and catabolic pathways

  • 182 Accesses

  • 13 Citations


Microorganisms have evolved enzymes which catalyze a large number of reactions in the sequences to form essential cellular constituents and liberate energy and carbon for cellular processes. Regulation of the use of energy and of the monomeric cellular precursors to the synthesis of those enzymes required under changing environmental conditions depends on the one hand on the level of end products of a reaction sequence and on the other upon the presence of the first, or early members of a reaction sequence. These cases in turn represent product repression and substrate, or substrate like, induction of enzyme formation. Though the repression system has generally been considered to operate in anabolic and the induction system in catabolic processes, the experiments presented demonstrate a role for both types of control in formation of biosynthetic and peripheral pathway enzymes. The induction of biosynthetic enzymes is shown in Pseudomonas putida, and organism with three clusters of genes for the tryptophan pathway. The repression of degradative enzymes is shown in an extended pathway of peripheral oxidation of terpenoid compounds. The enzymes for steps following conversion of neutral to non-essential acidic products are repressed as well as enzymes beyond convergence with isobutyrate formation and conversion to the succinyl and propionyl intermediates.

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


  1. Bertland, A. U. II, S. Johnson, and I. C. Gunsalus: Induced enzymes in terpene metabolism: An FMN-coupled DPNH oxidase in pseudomonads. Bact. Proc. 1963, 105.

  2. Bertland, A. U. II: Camphor metabolism in a saprophytic pseudomonad: Genetic aspects, induced enzyme formation and isolation of bacteriophage. Ph. D. Thesis, University of Illinois 1965.

  3. Bradshaw, W. H., H. E. Conrad, E. J. Corey, I. C. Gunsalus, and D. Lednicer: Microbiological degradation of (+)-camphor. J. Amer. chem. Soc. 81, 5507–5508 (1959).

  4. Chakrabarty, A. M., J. F. Niblack, and I. C. Gunsalus: A phage-initiated polysaccharide depolymerase in Pseudomonas putida. Virology 32, 532–534 (1967).

  5. Conrad, H. E., R. Dubus, M. J. Namtvedt, and I. C. Gunsalus: Mixed function oxidation II. Separation and properties of the enzyme catalyzing camphor lactonization. J. biol. Chem. 240, 495–503 (1965).

  6. Crawford, I. P., and I. C. Gunsalus: Inducibility of tryptophan synthetase in Pseudomonas putida. Proc. nat. Acad. Sci. (Wash.) 56, 717–724 (1966).

  7. Cushman, D. W.: Methylene hydroxylase monoxygenases: Components and properties of 2-bornane 5-exo-hydroxylase. Ph. D. Thesis. University of Illinois 1967.

  8. Gornall, A. G., C. J. Bardawill, and M. M. David: Determination of serum protein by means of the biuret reaction. J. biol. Chem. 177, 751–766 (1949).

  9. Gunsalus, I. C., H. E. Conrad, and P. W. Trudgill: Generation of active oxygen for mixed-function oxidation. In: T. Kink, H. S. Mason, and S. Morrison (Ed.): Oxidase and related redox systems. New York: J. Wiley 1965.

  10. Hegeman, G. D.: Synthesis of the enzymes of the mandelate pathway by Pseudomonas putida. I. Synthesis of enzymes of wild type. J. Bact. 91, 1140–1154 (1966).

  11. Jacob, F., and J. Monod: Genetic regulatory mechanism in the synthesis of Proteins. J. molec. Biol. 3, 318–356 (1961).

  12. Jacobson, L. A.: Enzyme induction and repression in the catabolism of (+)-camphor by Pseudomonas putida. Ph. D. Thesis, University of Illinois 1967.

  13. —, R. C. Bartholomaus, and I. C. Gunsalus: Biochem. biophys. Res. Commun. 24, 955–960 (1966).

  14. Maas, W., and E. McFall: Genetic aspects of metabolic control. Ann. Rev. Microbiol. 18, 95–110 (1964).

  15. Ornston, L. N.: The conversion of catechol and protocatechuate of β-ketoadipate by Pseudomonas putida, IV. Regulation. J. biol. Chem. 241, 3800–3810 (1966).

  16. Pardee, A. B., and L. Prestidge: The initial kinetics of enzyme induction. Biochim. biophys. Acta (Amst.) 49, 77–88 (1961).

  17. Schmidt, G. L.: Control and convergence in the valine-isobutyrate oxidative pathway, Honors B.S. Thesis, University of Illinois 1967.

  18. Stanier, R. Y., G. D. Hegeman, and L. N. Ornston: The mechanism of so-called “sequential induction” in Pseudomonas fluorescens. In: Colloq. Int. Centre Nat. Rech. Sci., pp. 227–236. Marseilles 1965.

  19. Stevenson, I. L., and J. Mandelstam: Induction and multi-sensitive end-product repression in two converging pathways degrading aromatic substance in Pseudomonas fluorescens. Biochem. J. 96, 354–362 (1965).

  20. Yanofsky, C.: The tryptophan synthetase system. Bact. Rev. 24, 221–245 (1960).

Download references

Author information

Additional information

Dedicated to C. B. van Niel on the occasion of his 70th birthday. Supported in part by grant G24037 from the National Science Foundation.

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Gunsalus, I.C., Bertland, A.U. & Jacobson, L.A. Enzyme induction and repression in anabolic and catabolic pathways. Archiv. Mikrobiol. 59, 113–122 (1967).

Download citation


  • Enzyme
  • Terpenoid
  • Pseudomonas Putida
  • Biosynthetic Enzyme
  • Catabolic Pathway