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Updated: Jun 27, 2026

Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta
Published on: December 5, 2019
Potent ligands for prokaryotic UDP-galactopyranose mutase that exploit an enzyme subsite
Emily C Dykhuizen1, Laura L Kiessling
1Department of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
Abstract:
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.
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