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.
Original language | English |
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Pages (from-to) | 4353-4356 |
Number of pages | 4 |
Journal | Tetrahedron Letters |
Volume | 48 |
Issue number | 25 |
DOIs | |
Publication status | Published - 18 Jun 2007 |