Transglucosidases as efficient tools for oligosaccharide and glucoconjugate synthesis.
Transglucosidases are highly promising enzymatic tools for glucodiversification. Instead of involving nucleotide-activated sugars as d-glucosyl donor, they use the energy of simple osidic linkages to synthesize carbohydrate derivatives. The remarkable promiscuity of these enzymes regarding the acceptor substrate offers great opportunities for novel synthetic reactions. Glucansucrases that use sucrose as donor substrate are of particular interest and have been widely utilized to produce diverse structurally controlled molecules. Besides site-directed mutagenesis, recent developments in the combined use of computational protein design and molecular engineering have led to major achievements to create novel enzymes, in particular for the chemo-enzymatic synthesis of antigenic oligosaccharides. These promising results pave the way to the future development of tailored catalysts for the synthesis of glucoconjugates of pharmaceutical and nutritional interest.
Monsan
Pierre
P
Université de Toulouse, INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077 Toulouse, France. pierre.monsan@insatoulouse.fr
Remaud-Siméon
Magali
M
André
Isabelle
I
D001709:Biotechnology / Q000379:methods; D006027:Glycosides / Q000378:metabolism*; D016695:Glycosyltransferases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D007218:Industrial Microbiology / Q000379:methods; D016297:Mutagenesis, Site-Directed; D050505:Mutant Proteins / Q000235:genetics / Q000378:metabolism; D009844:Oligosaccharides / Q000378:metabolism*; D015202:Protein Engineering; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism
D006027:Glycosides; D050505:Mutant Proteins; D009844:Oligosaccharides; D011994:Recombinant Proteins; D016695:Glycosyltransferases