The interaction of fructose 2,6-bisphosphate with an allosteric site of rat liver fructose 1,6-bisphosphatase

D. W. Meek, H. G. Nimmo

    Research output: Contribution to journalArticle

    24 Citations (Scopus)

    Abstract

    Rat liver fructose 1,6-bisphosphatase can be protected against partial inactivation by N-ethylmaleimide by low concentrations of fructose 2,6-bisphosphate or high concentrations of fructose 1,6-bisphosphate. The partially inactivated enzyme has a much reduced sensitivity to high substrate inhibition and has lost the sigmoid component of the inhibition by fructose 2,6-bisphosphate; this compound is a simple linear competitive inhibitor of the modified enzyme. The results suggest that fructose 2,6-bisphosphate can bind to the enzyme at two distinct sites, the catalytic site and an allosteric site. High levels of fructose 1,6-bisphosphate probably inhibit by binding to the allosteric site.
    Original languageEnglish
    Pages (from-to)105-109
    Number of pages5
    JournalFEBS Letters
    Volume160
    Issue number1-2
    DOIs
    Publication statusPublished - 22 Aug 1983

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