title: Synthesis and analysis of substrate analogues for UDP-galactopyranose mutase: implication for an oxocarbenium ion intermediate in the catalytic mechanism.
abstract: [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 intermediate in UGM catalysis.
authors.affiliation: Division of Medicinal Chemistry, College of Pharmacy and Department of Chemistry and Biochemistry, University of Texas at Austin, Austin, Texas 78712, USA.
authors.forename: Kenji
authors.initials: K
authors.lastname: Itoh
authors.forename: Zhishu
authors.initials: Z
authors.lastname: Huang
authors.forename: Hung-wen
authors.initials: HW
authors.lastname: Liu
mesh_terms: D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D019751:Intramolecular Transferases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D007477:Ions / Q000737:chemistry*; D015394:Molecular Structure; D013379:Substrate Specificity
chemical_list: D007477:Ions; D019751:Intramolecular Transferases; C098051:UDP-galactopyranose mutase