Journal
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
Volume 19, Issue 3, Pages 814-816Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2008.12.014
Keywords
Enzymes; Mechanism; Tuberculosis; Fluorine; Carbohydrate; Conformation; Galactofuranose
Categories
Funding
- F.N.R.S.
- FRFC [2.4.625.08.F]
- University of Namur
- Centre National de la Recherche Scientifique (CNRS)
- Research National Agency [ANR JCJC06_140075]
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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. UDP-(6-deoxy-6-fluoro)-D-galactofuranose 1 was tested as substrate of UGM. Turnover could be observed by HPLC. The k(cat) (7.4 s (1)) and the K-m (24 mM) of 1 were thus measured and compared with those of UDP- Galf and other fluorinated analogs. The presence of the fluorine atom at the 6-position had a moderate effect on the rate of the reaction but a huge one on the interactions between the enzyme and its substrate. This result demonstrated that key interactions occur at the vicinity of the 6-position of UDPgalactose in the Michaelis complex. (C) 2009 Elsevier Ltd. All rights reserved.
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