Abstract
In the absence of chelating agents, the sensitivity of rabbit liver fructose 1,6-bisphosphatase to inhibition by AMP is increased by approximately 10-fold, apparently related to the presence of bound Zn 2+. At pH 7.5, 10 μM AMP causes virtually complete inhibition and nearly full activity is restored by the addition of chelating agents such as EDTA or histidine. These properties provide a mechanism for the induction of Fru-P 2ase activity under gluconeogenic conditions.
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