{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yang X"],"funding":["National Institutes of Health","NIGMS NIH HHS","NIH HHS"],"pagination":["6004-6015"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11290465"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["22(29)"],"pubmed_abstract":["Glycosyltransferases are nature's key biocatalysts for the formation of glycosidic bonds. Discovery and characterization of new synthetically useful glycosyltransferases are critical for the development of efficient enzymatic and chemoenzymatic strategies for producing complex carbohydrates and glycoconjugates. Herein we report the identification of <i>Pasteurella multocida</i> PmNatB as a bifunctional single-catalytic-domain glycosyltransferase with both β1-3-galactosyltransferase and β1-3-<i>N</i>-acetylgalactosaminyltransferase activities. It is a novel glycosyltransferase for constructing structurally diverse GalNAcβ3Galα/βOR and Galβ3GalNAcα/βOR disaccharides in one-pot multienzyme systems with <i>in situ</i> generation of UDP-sugars."],"journal":["Organic & biomolecular chemistry"],"pubmed_title":["A bifunctional &lt;i&gt;Pasteurella multocida&lt;/i&gt; β1-3-galactosyl/&lt;i&gt;N&lt;/i&gt;-acetylgalactosaminyltransferase (PmNatB) for the highly efficient chemoenzymatic synthesis of disaccharides."],"pmcid":["PMC11290465"],"funding_grant_id":["S10OD025271","R44 GM139441","R42GM143998","R01 GM141324","R01GM141324","S10 OD025271","R42 GM143998"],"pubmed_authors":["Yang X","Mishra B","Chen X","Wei Y","Yu H"],"additional_accession":[]},"is_claimable":false,"name":"A bifunctional &lt;i&gt;Pasteurella multocida&lt;/i&gt; β1-3-galactosyl/&lt;i&gt;N&lt;/i&gt;-acetylgalactosaminyltransferase (PmNatB) for the highly efficient chemoenzymatic synthesis of disaccharides.","description":"Glycosyltransferases are nature's key biocatalysts for the formation of glycosidic bonds. Discovery and characterization of new synthetically useful glycosyltransferases are critical for the development of efficient enzymatic and chemoenzymatic strategies for producing complex carbohydrates and glycoconjugates. Herein we report the identification of <i>Pasteurella multocida</i> PmNatB as a bifunctional single-catalytic-domain glycosyltransferase with both β1-3-galactosyltransferase and β1-3-<i>N</i>-acetylgalactosaminyltransferase activities. It is a novel glycosyltransferase for constructing structurally diverse GalNAcβ3Galα/βOR and Galβ3GalNAcα/βOR disaccharides in one-pot multienzyme systems with <i>in situ</i> generation of UDP-sugars.","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-03-15T18:06:29.057Z","creation":"2025-08-13T03:04:42.613Z"},"accession":"S-EPMC11290465","cross_references":{"pubmed":["38993172"],"doi":["10.1039/d4ob00889h"]}}