Mesh : Pasteurella multocida / enzymology Disaccharides / chemistry chemical synthesis biosynthesis N-Acetylgalactosaminyltransferases / metabolism chemistry Galactosyltransferases / metabolism

来  源:   DOI:10.1039/d4ob00889h   PDF(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 Pasteurella multocida PmNatB as a bifunctional single-catalytic-domain glycosyltransferase with both β1-3-galactosyltransferase and β1-3-N-acetylgalactosaminyltransferase activities. It is a novel glycosyltransferase for constructing structurally diverse GalNAcβ3Galα/βOR and Galβ3GalNAcα/βOR disaccharides in one-pot multienzyme systems with in situ generation of UDP-sugars.
摘要:
糖基转移酶是自然界形成糖苷键的关键生物催化剂。新的合成有用的糖基转移酶的发现和表征对于开发用于生产复杂碳水化合物和糖缀合物的有效酶促和化学酶促策略至关重要。在此,我们报告了多杀性巴氏杆菌PmNatB作为具有β1-3-半乳糖基转移酶和β1-3-N-乙酰半乳糖胺转移酶活性的双功能单催化结构域糖基转移酶的鉴定。它是一种新型的糖基转移酶,用于在一锅法多酶系统中构建结构多样的GalNAcβ3Galα/βOR和Galβ3GalNAcα/βOR二糖,并原位生成UDP糖。
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