Format

Send to

Choose Destination
Org Lett. 2009 Jan 1;11(1):193-6. doi: 10.1021/ol802094p.

Potent ligands for prokaryotic UDP-galactopyranose mutase that exploit an enzyme subsite.

Author information

1
Department 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.

PMID:
19067595
PMCID:
PMC3010353
DOI:
10.1021/ol802094p
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for American Chemical Society Icon for PubMed Central
Loading ...
Support Center