Potent ligands for prokaryotic UDP-galactopyranose mutase that exploit an enzyme subsite.
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ABSTRACT:
SUBMITTER: Dykhuizen EC
PROVIDER: S-EPMC3010353 | biostudies-literature | 2009 Jan
REPOSITORIES: biostudies-literature
Publications
Potent ligands for prokaryotic UDP-galactopyranose mutase that exploit an enzyme subsite.
Dykhuizen Emily C EC Kiessling Laura L LL
Organic letters 20090101 1
UDP-galactopyranose mutase (UGM or Glf), which catalyzes the interconversion of UDP-galactopyranose and UDP-galactofuranose, is implicated in the viability and virulence of multiple pathogenic microorganisms. Here we report the synthesis of high-affinity ligands for UGM homologues from Klebsiella pneumoniae and Mycobacterium tuberculosis. The potency of these compounds stems from their ability to access both the substrate binding pocket and an adjacent site. ...[more]
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