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A 1-acetamido derivative of 6-epi-valienamine: an inhibitor of a diverse group of beta-N-acetylglucosaminidases

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JournalOrganic and Biomolecular Chemistry
DatePublished - 2007
Issue number18
Volume5
Number of pages7
Pages (from-to)3013-3019
Original languageEnglish

Abstract

The synthesis of an analogue of 6-epi-valienamine bearing an acetamido group and its characterisation as an inhibitor of beta-N-acetylglucosaminidases are described. The compound is a good inhibitor of both human O-GlcNAcase and human beta-hexosaminidase, as well as two bacterial beta-N-acetylglucosaminidases. A 3-D structure of the complex of Bacteroides thetaiotaomicron BtGH84 with the inhibitor shows the unsaturated ring is surprisingly distorted away from its favoured solution phase conformation and reveals potential for improved inhibitor potency.

    Research areas

  • SUBSTRATE-ASSISTED CATALYSIS, O-GLCNACASE, D-GLUCOSAMINIDASE, GLYCOSIDE HYDROLASE, MECHANISM, HEXOSAMINIDASE, GLUCOSIDASE, ANALOGS, CRYSTALLOGRAPHY, PURIFICATION

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