| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5280074 | Tetrahedron Letters | 2007 | 4 Pages |
Abstract
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. Acyclic alditol-aminophosphonates in the d-galactose and d-lyxose series were designed as mimics of high energy intermediates of the UGM catalyzed isomerization. Interestingly, the d-lyxitol-aminophosphonate displayed better inhibition properties than the d-galactitol-aminophosphonate.
Graphical abstractAcyclic alditol-aminophosphonates 1 and 2 were designed as mimics of high energy intermediates of the UGM catalyzed isomerization. Interestingly, the d-lyxitol-aminophosphonate 2 displayed better inhibition properties than 1.Download full-size image
Related Topics
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Authors
Weidong Pan, Christophe Ansiaux, Stéphane P. Vincent,