AI Article Synopsis
- The study focuses on creating and testing selective inhibitors for class II fructose bisphosphate aldolases, which depend on zinc.
- The most effective inhibitor identified is a simplified version of fructose bisphosphate that effectively binds to the enzyme’s active site due to its metal-chelating properties.
- Additionally, this compound demonstrates effectiveness against both Helicobacter pylori and Mycobacterium tuberculosis, which are significant bacteria in human health.
Article Abstract
We report the synthesis and biochemical evaluation of selective inhibitors of class II (zinc-dependent) fructose bisphosphate aldolases. The most active compound is a simplified analogue of fructose bisphosphate, bearing a well-positioned metal chelating group. It is a powerful and highly selective competitive inhibitor of isolated class II aldolases. We report crystallographic studies of this inhibitor bound in the active site of the Helicobacter pylori enzyme. The compound also shows activity against Mycobacterium tuberculosis isolates.
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| http://dx.doi.org/10.1002/chem.200800857 | DOI Listing |
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