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Catabolite inactivation of fructose 1,6-bisphosphatase inKluyveromyces fragilis

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Abstract

Catabolite inactivation of fructose 1,6-bisphosphatase inKluyveromyces fragilis was found to occur as a one-step process with a half-life of approximately 90 min in contrast to the two-step process previously reported forSaccharomyces cerevisiae. No rapid initial 50% loss of activity immediately after a glucose-induced catabolite inactivation was found; nevertheless, fructose 1,6-bisphosphatase was rapidly phosphorylated within 5 min of glucose addition. This result supports the hypothesis that protein phosphorylation serves as a signal for the specific degradation of fructose 1,6-bisphosphatase during catabolite inactivation.

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  1. Yukiyasu Toyoda

    Present address: Department of Clinical Biochemistry, Faculty of Pharmacy, Meijo University, 1230 York Avenue, 468, Nagoya, Japan

Authors and Affiliations

  1. Rockefeller University, 1230 York Avenue, 10021, New York, New York, USA

    Yukiyasu Toyoda &  José Sy

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  1. Yukiyasu Toyoda
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  2. José Sy
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Toyoda, Y., Sy, J. Catabolite inactivation of fructose 1,6-bisphosphatase inKluyveromyces fragilis . Current Microbiology 12, 241–244 (1985). https://doi.org/10.1007/BF01573338

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