Journal
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
Volume 16, Issue 5, Pages 1123-1125Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2005.11.106
Keywords
enzymes; mechanism; tuberculosis; conformation; galactofuranose
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UDP-galactopyranose mutase (UGM) catalyzes the isomerization of UDP-galactopyranose (UDP-Galp) into UDP-galactofuranose (UDP-Galf), an essential step of the mycobacterial cell wall biosynthesis. The first mechanistic assumption proposed in the literature was the involvement of 1,4-anhydrogalactose 1 as intermediate of this ring contraction. To confirm or rule out this hypothesis, we synthesized 1 and engaged it in reactions with UGM. The expected formations of UDP-Galf and UDP-Galp were never observed, thus showing that 1 is not, in fact, a low energy intermediate of this enzymatic contraction. (C) 2005 Elsevier Ltd. All rights reserved.
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