Synthesis and analysis of substrate analogues for UDP-galactopyranose mutase: implication for an oxocarbenium ion intermediate in the catalytic mechanism.
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ABSTRACT:
SUBMITTER: Itoh K
PROVIDER: S-EPMC2515276 | biostudies-literature | 2007 Mar
REPOSITORIES: biostudies-literature
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Synthesis and analysis of substrate analogues for UDP-galactopyranose mutase: implication for an oxocarbenium ion intermediate in the catalytic mechanism.
Itoh Kenji K Huang Zhishu Z Liu Hung-wen HW
Organic letters 20070201 5
[reaction: see text] UDP-D-galactofuranose (2), which is essential for both cell growth and virulence in many pathogenic microorganisms, is converted from UDP-D-galactopyranose (UDP-Galp, 1) by the flavin adenine dinucleotide (FAD)-dependent enzyme UDP-galactopyranose mutase (UGM). Here, we report the synthesis of UDP-GalOH (13) and show it as an inhibitor for UGM with a binding affinity similar to that of 1. These results are more consistent with a mechanism involving an oxocarbenium ion interm ...[more]
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