A bifunctional Pasteurella multocida ß1-3-galactosyl/N-acetylgalactosaminyltransferase (PmNatB) for the highly efficient chemoenzymatic synthesis of disaccharides.

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 ß1-3-galactosyltransferase and ß1-3-N-acetylgalactosaminyltransferase activities. It is a novel glycosyltransferase for constructing structurally diverse GalNAcß3Galα/ßOR and Galß3GalNAcα/ßOR disaccharides in one-pot multienzyme systems with in situ generation of UDP-sugars.