The allosteric properties of rat liver fructose-1,6-bisphosphatase

D. W. Meek, H. G. Nimmo

    Research output: Contribution to journalArticle

    11 Citations (Scopus)

    Abstract

    Inhibition of rat liver fructose-1,6-bisphosphatase by AMP was uncompetitive with respect to fructose 1,6-bisphosphate in the absence of fructose 2,6-bisphosphate, but non-competitive in its presence. AMP was unable to bind to the enzyme except in the presence of one of the fructose bisphosphates; the binding stoicheiometry was 2 molecules/tetramer. Increasing concentrations of Mg2+ increased the Hill coefficient h and the apparent Ki for AMP, whereas fructose 2,6-bisphosphate had the opposite effect. Increasing concentrations of both AMP and fructose 2,6-bisphosphate decreased h and increased the apparent Ka for Mg2+. AMP slightly decreased, and Mg2+ slightly increased, the apparent Ki for fructose 2,6-bisphosphate, but each had only small effects on h. These results are interpreted in terms of a new three-state model for the allosteric properties of the enzyme, in which fructose 2,6-bisphosphate can bind both to the catalytic site and to an allosteric site and AMP can bind to the enzyme only when the catalytic site is occupied.
    Original languageEnglish
    Pages (from-to)131-138
    Number of pages8
    JournalBiochemical Journal
    Volume222
    Issue number1
    Publication statusPublished - 15 Aug 1984

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    Fructose-Bisphosphatase
    Adenosine Monophosphate
    Liver
    Rats
    Catalytic Domain
    Enzymes
    Allosteric Site
    Fructose
    fructose 2,6-diphosphate
    Molecules

    Cite this

    Meek, D. W., & Nimmo, H. G. (1984). The allosteric properties of rat liver fructose-1,6-bisphosphatase. Biochemical Journal, 222(1), 131-138.
    Meek, D. W. ; Nimmo, H. G. / The allosteric properties of rat liver fructose-1,6-bisphosphatase. In: Biochemical Journal. 1984 ; Vol. 222, No. 1. pp. 131-138.
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    abstract = "Inhibition of rat liver fructose-1,6-bisphosphatase by AMP was uncompetitive with respect to fructose 1,6-bisphosphate in the absence of fructose 2,6-bisphosphate, but non-competitive in its presence. AMP was unable to bind to the enzyme except in the presence of one of the fructose bisphosphates; the binding stoicheiometry was 2 molecules/tetramer. Increasing concentrations of Mg2+ increased the Hill coefficient h and the apparent Ki for AMP, whereas fructose 2,6-bisphosphate had the opposite effect. Increasing concentrations of both AMP and fructose 2,6-bisphosphate decreased h and increased the apparent Ka for Mg2+. AMP slightly decreased, and Mg2+ slightly increased, the apparent Ki for fructose 2,6-bisphosphate, but each had only small effects on h. These results are interpreted in terms of a new three-state model for the allosteric properties of the enzyme, in which fructose 2,6-bisphosphate can bind both to the catalytic site and to an allosteric site and AMP can bind to the enzyme only when the catalytic site is occupied.",
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    Meek, DW & Nimmo, HG 1984, 'The allosteric properties of rat liver fructose-1,6-bisphosphatase', Biochemical Journal, vol. 222, no. 1, pp. 131-138.

    The allosteric properties of rat liver fructose-1,6-bisphosphatase. / Meek, D. W.; Nimmo, H. G.

    In: Biochemical Journal, Vol. 222, No. 1, 15.08.1984, p. 131-138.

    Research output: Contribution to journalArticle

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    AU - Nimmo, H. G.

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    AB - Inhibition of rat liver fructose-1,6-bisphosphatase by AMP was uncompetitive with respect to fructose 1,6-bisphosphate in the absence of fructose 2,6-bisphosphate, but non-competitive in its presence. AMP was unable to bind to the enzyme except in the presence of one of the fructose bisphosphates; the binding stoicheiometry was 2 molecules/tetramer. Increasing concentrations of Mg2+ increased the Hill coefficient h and the apparent Ki for AMP, whereas fructose 2,6-bisphosphate had the opposite effect. Increasing concentrations of both AMP and fructose 2,6-bisphosphate decreased h and increased the apparent Ka for Mg2+. AMP slightly decreased, and Mg2+ slightly increased, the apparent Ki for fructose 2,6-bisphosphate, but each had only small effects on h. These results are interpreted in terms of a new three-state model for the allosteric properties of the enzyme, in which fructose 2,6-bisphosphate can bind both to the catalytic site and to an allosteric site and AMP can bind to the enzyme only when the catalytic site is occupied.

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