Structural highlights
FunctionOGA_BACTN Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. Publication Abstract from PubMedThe chemoenzymatic synthesis of oligosaccharides presents a highly attractive methodology with significant potential for diverse applications, particularly through using various glycosidases. In this study, the O-glycan core 6 disaccharide moiety, GlcNAcbeta1-6GalNAc, was successfully synthesized via enzymatic glycosylation using an N-acetyl-beta-D-glucosaminidase from Bacteroides thetaiotaomicron (BtOGA), a member of glycoside hydrolase family 84 (GH84), alongside an N-acetyl-D-glucosamine oxazoline derivative (GlcNAc-oxa) as the glycosyl donor. Furthermore, an investigation into glycosyl acceptor recognition in BtOGA-catalyzed enzymatic glycosylation indicated that the presence of an aromatic group at the anomeric position and an axial hydroxy group at the 4-position of the saccharide moiety is crucial for effective recognition of BtOGA as a glycosyl acceptor. The protecting-group-free chemoenzymatic synthesis of the core 6 disaccharide moiety was achieved by integrating the direct synthesis of GlcNAc-oxa thorough Shoda activation method using a water-soluble dehydration condensing agent in an aqueous medium, followed by BtOGA-catalyzed enzymatic glycosylation. beta1,6-Selective Enzymatic N-Acetylglucosamination Catalyzed by the Family GH84 N-Acetyl-beta-D-glucosaminidase from Bacteroides thetaiotaomicron and its Glycosyl Acceptor Specificity.,Okuno R, Nakada S, Tonomura K, Aso Y, Takeshita D, Ohnuma T, Tanaka T Chem Asian J. 2025 Apr 8:e202500142. doi: 10.1002/asia.202500142. PMID:40195893[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
This page was last modified 05:33, 23 April 2025.