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  • Title: Fructose 1,6-bisphosphatase: the role of lysosomal enzymes in the modification of catalytic and structural properties.
    Author: Pontremoli S, Melloni E, Balestrero F, Franzi AT, De Flora A, Horecker BL.
    Journal: Proc Natl Acad Sci U S A; 1973 Feb; 70(2):303-5. PubMed ID: 4346880.
    Abstract:
    Seasonal variations in the properties of rabbit-liver fructose 1,6-bisphosphatase have now been linked to corresponding changes in the levels of proteolytic activity in the liver extracts. Incubation of native fructose 1,6-bisphosphatase with purified liver lysosomes causes a 3-fold increase in catalytic activity at pH 9.2, with a smaller, and variable, decrease in activity tested at pH 7.5. These changes in catalytic properties are accompanied by the appearance of a smaller subunit, as was previously reported for the enzyme treated with subtilisin. AMP, a negative modulator of fructose bisphosphatase activity, protects against this action of lysosomes. This proteolytic modification of fructose bisphosphatase by lysosomal enzymes may play a role in the modulation of gluconeogenesis.
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