Insights into the Mechanism ofEscherichia coliMethionine Aminopeptidase from the Structural Analysis of Reaction Products and Phosphorus-Based Transition-State Analogues†,‡

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<div>Conjugation of the transitionstate-cation analogue DANA to polymeric scaffolds led to highly potent inhibitors of bacterial sialidases. Each clustered DANA on the polymers saw its inhibitory potency for S. pneumoniae or B. thetaiotaomicron sialidases improved by more than four orders of magnitude. This extends the multivalent concept to this important class of enzymes.</div><div><br></div>


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