3554-91-4Relevant articles and documents
Structural analysis of a family 101 glycoside hydrolase in complex with carbohydrates reveals insights into its mechanism
Gregg, Katie J.,Suits, Michael D. L.,Deng, Lehua,Vocadlo, David J.,Boraston, Alisdair B.
, p. 25657 - 25669 (2015/10/28)
O-Linked glycosylation is one of the most abundant posttranslational modifications of proteins. Within the secretory pathway of higher eukaryotes, the core of these glycans is frequently an N-acetylgalactosamine residue that is α-linked to serine or threo
Novel phosphoramidate prodrugs of N-acetyl-(d)-glucosamine with antidegenerative activity on bovine and human cartilage explants
Serpi, Michaela,Bibbo, Rita,Rat, Stephanie,Roberts, Helen,Hughes, Claire,Caterson, Bruce,Alcaraz, María José,Gibert, Anna Torrent,Verson, Carlos Raul Alaez,McGuigan, Christopher
supporting information; experimental part, p. 4629 - 4639 (2012/07/01)
(d)-Glucosamine and other nutritional supplements have emerged as safe alternative therapies for osteoarthritis (OA), a chronic and degenerative articular joint disease. In our preceding paper, a series of novel O-6 phosphate N-acetyl (d)-glucosamine prod
Optimization of UDP-N-acetylmuramic acid synthesis
Humljan, Jan,Starcevic,Car,Stefanic Anderluh,Kocjan,Jenko,Urleb
, p. 102 - 106 (2008/09/21)
UDP-N-acetylmuramic acid (UDP-MurNAc) is a substrate of MurC, an important enzyme in the intracellular pathway of bacterial peptidoglycan biosynthesis. Various approaches towards preparation of UDP-Mur/VAc have been published but these synthetic preparations were shown to include many problematic steps. An optimization study with the focus on muramyl phosphate and UMP-morpholidate coupling was performed, resulting in a synthetic procedure enabling robust and easily reproducible production on a multi-gram scale.