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• W2043624103 abstract "Human fructose-1,6-bisphosphatase (FBPase, EC 3.1.3.11) is a key gluconeogenic enzyme, responsible for the hydrolysis of fructose-1,6-bisphosphate to fructose-6-phosphate, and thus presents an opportunity for the development of novel therapeutics focused on lowering the hepatic glucose production in type 2 diabetics. In its active form FBPase exists as a homotetramer and is allosterically regulated by AMP. In an HTS campaign aromatic sulfonylureas have been identified as FBPase inhibitors mimicking AMP. By bridging two adjacent allosteric binding sites using two aromatic sulfonylureas as anchor units and covalently linking them, it was possible to obtain dual binding AMP site inhibitors that exhibit a strong inhibitory effect." @default.
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• W2043624103 date "2008-08-01" @default.
• W2043624103 modified "2023-09-24" @default.
• W2043624103 title "Allosteric FBPase inhibitors gain 105 times in potency when simultaneously binding two neighboring AMP sites" @default.
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• W2043624103 doi "https://doi.org/10.1016/j.bmcl.2008.06.103" @default.
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