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Irreversible inactivation of yeast glucose-6-P dehydrogenase by penicillin G

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Summary

Yeast glucose-6-P dehydrogenase is irreversibly inactivated by penicillin G. Kinetic data show that 1 molecule of penicillin G reacts with each active unit when the enzyme is inactivated The rate of inactivation increases greatly with increasing pH. This irreversible inactivation by penicillin G is largely prevented by pyridoxal-P, a reversible inactivator of this enzyme. Prior treatment of penicillin G with penicillinase totally abolishes its ability to inactivate the enzyme.

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Authors and Affiliations

  1. Department of Chemistry, Atlanta University, 30314, Atlanta, Georgia, USA

    P. F. Han, Y. H. Marian, H. W. Matthews & J. Johnson

  2. School of Pharmacy, Mercer University, 30312, Atlanta, Georgia, USA

    P. F. Han, Y. H. Marian, H. W. Matthews & J. Johnson

Authors
  1. P. F. Han
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  2. Y. H. Marian
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  3. H. W. Matthews
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  4. J. Johnson
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Additional information

This work was supported by grant RR-8006 from the General Research Branch, Division of Research Resouces, NIH (USA).

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Han, P.F., Marian, Y.H., Matthews, H.W. et al. Irreversible inactivation of yeast glucose-6-P dehydrogenase by penicillin G. Experientia 37, 687–689 (1981). https://doi.org/10.1007/BF01967923

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