PubMed:36634517 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/36634517","sourcedb":"PubMed","sourceid":"36634517","source_url":"https://www.ncbi.nlm.nih.gov/pubmed/36634517","text":"The first report of enzymatic transglycosylation catalyzed by family GH84 N-acetyl-β-d-glucosaminidase using a sugar oxazoline derivative as a glycosyl donor.\nO-Glycosylated N-acetyl-β-d-glucosamine-selective N-acetyl-β-d-glucosaminidase (O-GlcNAcase), belonging to glycoside hydrolase family 84 (GH84), is known as a retaining glycosidase with the possibility of enzymatic transglycosylation. However, no enzymatic transglycosylation catalyzed by GH84 O-GlcNAcase has been reported. Here, enzymatic transglycosylation catalyzed by GH84 O-GlcNAcase was first reported. The enzymatic transglycosylation catalyzed by the GH84 O-GlcNAcase from Bacteroides thetaiotaomicron (BtGH84 O-GlcNAcase) was attained using 1,2-oxazoline derivative of N-acetyl-d-glucosamine (GlcNAc oxazoline) as a glycosyl donor substrate. The β-linked N-acetyl-d-glucosamine (GlcNAc) derivative was enzymatically synthesized using N-(2-hydroxyethyl)acrylamide as an acceptor substrate. Interestingly, the β1,6-linked disaccharide derivative of GlcNAc was also obtained in the case of using the GlcNAc derivative with a triazole-linked acrylamide group as an acceptor substrate. Additionally, a one-pot chemo-enzymatic transglycosylation starting from unprotected GlcNAc through GlcNAc oxazoline successfully showed through the combination with the direct synthesis of GlcNAc oxazoline in water and the enzymatic transglycosylation.","tracks":[{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":641,"end":669},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"818"},{"subj":"T1","pred":"source","obj":"NCBITAXON"}]}],"config":{"attribute types":[{"pred":"source","value type":"selection","values":[{"id":"NCBITAXON","color":"#98ec93","default":true}]}]}}