UDP-N-acetyl-D-Glucosamine is a natural nucleotide sugar that is used by glycosyltransferases to transfer N-acetyl-D-glucosamine residues to substrates.1It is an important component of antibiotic biosynthesis pathways in fungi and lipopolysaccharide production in bacteria.2,3 1.Roseman, S.Reflections on glycobiologyJ. Biol. Chem.276(45)41527-41542(2001) 2.Kudo, F., and Eguchi, T.Biosynthetic genes for aminoglycoside antibioticsJ. Antibiot. (Tokyo)62(9)471-481(2009) 3.Mulrooney, E.F., Poon, K.K., McNally, D.J., et al.Biosynthesis of UDP-N-acetyl-L-fucosamine, a precursor to the biosynthesis of lipopolysaccharide in Pseudomonas aeruginosa serotype O11J. Biol. Chem.280(20)19535-19542(2005)
N,N'-Diacetylchitobiose, a dimer of β(1,4) linked N-acetyl-D glucosamine, is derived from the hydrolysis of chitin. This compound serves as an alternative carbon source for E. coli.
AB05831, also known as 2-Acetamido-1,2-dideoxynojirimycin, is a highly potent and specific inhibitor of beta-hexosaminidase. N-Acetyl-3-hexosaminidase (HEX) is a member of lysosomal hydrolases, which catalyzes hydrolysis of terminal, non-reducing N-acetyl-|3-D-glucosamine (GlcNAc) andN-acetyl-(3-D-galactosamine (GalNAc) residues in glycoproteins, gan-gliosides, and glycosaminoglycans (GAGs). HEX, released by chondrocytes into the extracellular compartment, promotes cartilage matrix degradation. Osteoarthritis patients have increased HEX activity in synovial fluid.