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Inactivation of yeast glucose-6-P dehydrogenase by aspirin

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Summary

Glucose-6-P dehydrogenase is irreversibly inactivated by treatment with Na salts of aspirin. Kinetic data show that 1 molecule of aspirin reacts with each active unit when the enzyme is inactivated. The rate of inactivation is enhanced with increasing pH but is reduced in the presence of glucose-6-P or NADP+. Na salicylate fails to inactivate the enzyme.

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Authors and Affiliations

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

    P. F. Han, G. Y. Han, H. C. McBay & J. Johnson Jr

  2. Department of Chemistry, Morehouse College, 30314, Atlanta, Georgia, USA

    P. F. Han, G. Y. Han, H. C. McBay & J. Johnson Jr

Authors
  1. P. F. Han
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  2. G. Y. Han
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  3. H. C. McBay
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  4. J. Johnson Jr
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Additional information

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

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Han, P.F., Han, G.Y., McBay, H.C. et al. Inactivation of yeast glucose-6-P dehydrogenase by aspirin. Experientia 36, 1149–1150 (1980). https://doi.org/10.1007/BF01976092

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