Abstract
Synthesis of penicillinamidohydrolase (penicillin acylase, EC 3.5.1.11) inEscherichia coli is subjected to the absolute catabolite repression by glucose and partial repression by acetate. Both types of catabolite repression of synthesis of the enzyme inEscherichia coli are substantially influenced by cyclic 3,′5′-adenosinemonophosphate (cAMP). Growth diauxie in a mixed medium containing glucose and phenylaoetic acid serving as carbon and energy sources is overcome by cAMP. cAMP does not influence the basal rate of the enzyme synthesis (without the inducer). Derepression of synthesis of penicillinamidohydrolasa by cAMP in a medium with glucose and inducer (phenylacetic acid) is associated with utilization of the inducer, due probably to derepression of other enzymes responsible for degradation of phenylacetic acid. Lactate can serve as a “catabolically neutral” source of carbon suitable for the maximum production of penicillinamidohydrolase. The gratuitous induction of the enzyme synthesis in a medium with lactate as the carbon and energy source and with phenylacetic acid is not influenced by cAMP; however, cAMP overcomes completely the absolute catabolite repression of the enzyme synthesis by glucose.
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References
Anderson R. L., Wood W. A.: Carbohydrate metabolism in microorganisms.Annu. Rev. Microbiol. 23, 539 (1969).
Arditti R. R., Scaife J. G., Beckwith J. R.: The nature of mutants in thelac-promoter region.J. Mol. Biol. 38, 421 (1968).
De Crombrugghe B., Perlman R. L., Varmus H. E., Pastan I.: Regulation of inducible enzyme synthesis inEscherichia coli by cyclic adenosine 3′,5′-monophosphate.J. Biol. Chem. 244, 5828 (1969).
Golub E. I., Garayev M. M., Romanova N. B.: Mutants ofEscherichia coli with suppressed glucose transport-producers of penicillin acylase.Antibiotiki 18, 882 (1973).
Jost J. P., Rickenberg H. V.:Cyclic AMP. Annu. Rev. Biochem. 40, 741 (1971).
Kaufmann W., Bauer K.: The production of penicillin amidase byEscherichia coli ATCC 9637.J. Gen. Microbiol. 35 (Soc. Gen. Microbiol. Proc. IV), p. iv (1964).
Levitov M. M., Klapovskaya K. I., Kleyner G. I.: Induced biosynthesis of acylase inEscherichia coli.Mikrobiologiya 36, 912 (1967).
Magasanik B.: Catabolite repression.Cold Spr. Harb. Symp. Quant. Biol. 26, 249 (1961).
McFall E.: Role of adenosine 3′,5′-cyclic monophosphate and its specific binding protein in the regulation of D-serine deaminase synthesis.J. Bacterial. 113, 781 (1973).
Moses V., Sharp P. B.: Adenosine 3′,5′-cyclic monophosphate and catabolite repression inEscherichia coli.Biochem. J. 118, 481 (1970).
Paigen K., Beverly W.: Catabolite repression and other control mechanisms in carbohydrate utilisation, p. 251, in A. H. Rosse and J. F. Wilkinson (Eds.):Advances in Microbial Physiology, vol. 4. Academic Press, London—New York 1970.
Pan S. C., Perlman D.: Determination of phenylacetic acid and phenylacetamides in samples from penicillin fermentation.Anal. Chem. 26, 1432 (1954).
Pastan I.: Current directions in research on cyclic AMP, p. 65, in C. B. Anfisen, R. F. Goldberger and A. N. Schechter (Eds.):Current Topics in Biochemistry. Academic Press, New York—London 1972.
Perlman R. L., Pastan I.: Cyclic 3′,5′-AMP: stimulation of beta-galactosidase and tryptophanase induction inEscherichia coli.Biochim. Biophys. Res. Commun. 30, 656 (1968a).
Perlman R. L., Pastan I.: Regulation of beta-galactosidase synthesis inEscherichia coli by cyclic adenosine 3′,5′-monophosphate.J. Biol. Chem. 243, 5420 (1968b).
Perlman R. L., De Crombrugghe B., Pastan I.: Cyclic AMP regulates catabolite and transient repression inEscherichia coli.Nature 233, 810(1969).
Rickenberg H. V., Hsie A. W., Janecek J.: The CR mutation and catabolite repression inEscherichia coli.Biochem. Biophys. Res. Commun. 31, 603 (1968).
Silverstone A. E., Magasanik B., Reznikoff W. S., Miller J. H., Beckwith J. R.: Catabolite sensitive site of thelac-operon.Nature 221, 1012 (1969).
Simon M., Stboman D., Apirion D.: Reversion of catabolite repression by cyclic-AMP. Its presence is necessary during initiation of newlac-m-RNA molecules.Bacteriol. Proc. Amer. Soc. Microbiol. P192 (1971).
Szentirmai A.: Production of penicillin acylase.Appl. Microbiol. 12, 185 (1964).
Tyler B., Magasanik B.: Molecular basis of transient repression of beta-galactosidase inEscherichia coli.J. Bacteriol. 97, 550 (1969).
Tyler B., Magasanik B.: Physiological basis of transient repression of catabolite enzymes inEscherichia coli.J. Bacteriol. 102, 411 (1970).
Varmus H. E., Perlman R. L., Pastan I.: Regulation oflac-messenger ribonucleic acid synthesis by cyclic adenosine 3′,5′-monophosphate and glucose.J. Biol. Chem. 245, 2259 (1970).
Vajtísek V., Slezák J., Culík K.: Method of obtaining microbial mutants producing penicillin acylase, especially fromEscherichia coli. Czechosl. Patent No. 1622–74 (1973).
Vojtísek V., Slezák J.: Penicillinamidohydrolase inEscherichia coli. I. Substrate specificity.Folia Microbiol. 20, 224 (1975).
Vojtísek V., Slezák J.: Penicillinamidohydrolase inEscherichia coli, II. Synthesis of the enzyme, kinetics and specificity of its induction and the effect of O2.Folia Microbiol. 20, 289 (1975).
Zubay G., Schwartz D., Beckwith J.: Mechanism of activation of catabolite sensitive genes: a positive control system.Proc. Natl. Acad. Sci. USA 66, 104 (1970).
Yudkin M. D.: Effect of point mutation in the lac promoter on transient and severe catabolite repression of thelac-operon ofEscherichia coli.Biochem. J. 123, 579 (1971).
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Vojtíek, V., Slezák, J. Penicillinamidohydrolase inEscherichia coli . Folia Microbiol 20, 298–306 (1975). https://doi.org/10.1007/BF02878111
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DOI: https://doi.org/10.1007/BF02878111