The versatile enzyme Araf51 allowed efficient synthesis of rare pathogen-related β-D-galactofuranosyl-pyranoside disaccharides

Ilona Chlubniva (1, 2) , Blanka Kralova (1) , Hana Dvorakova (3) , Petr Hošek (1) , Vojtěch Spiwok (1) , Dominik Filipp (4) , Caroline Nugier-Chauvin (2) , Richard Daniellou (2) , Vincent Ferrières (2)

1 Department of Biochemistry and Microbiology
2 ISCR - Institut des Sciences Chimiques de Rennes
3 Laboratory of NMR spectroscopy
4 Laboratory of Immunobiology

The preparation of galactofuranosyl-containing disaccharidic parts of natural glycoconjugates was performed according to a chemo-enzymatic synthesis. Our goals were firstly to develop an alternative approach to standard chemical strategies by limiting the number of reaction and purification steps, and secondly to evaluate the scope of the Araf51 biocatalyst to transfer a galactofuranosyl moiety to a set of pyranosidic acceptors differing from each other by the series, the anomeric configuration as well as the conformation. The study of binding mode of the resulting disaccharides was also performed by molecular modeling and showed significant differences between (1→2)- and (1→6)-linked disaccharides.

Keywords: Carbohydrates; Biocatalysis

Domains: Chemical Sciences; Organic chemistry

Ilona Chlubniva, Blanka Kralova, Hana Dvorakova, Petr Hošek, Vojtěch Spiwok, et al.. The versatile enzyme Araf51 allowed efficient synthesis of rare pathogen-related β-D-galactofuranosyl-pyranoside disaccharides. Organic & Biomolecular Chemistry, 2014, 12 (19), pp.3080-3089. ⟨10.1039/C3OB42519C⟩. ⟨hal-00995753⟩