Endo-α-Mannosidase-Catalyzed Transglycosylation
| Autor: | Yoichi Takeda, Shogo Iwamoto, Akira Seko, Kiichiro Totani, Yayoi Yoshimura, Ichiro Matsuo, Yukishige Ito, Yuta Kasahara |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Mannosidase Glycosylation Stereochemistry Molecular Conformation Oligosaccharides alpha-Mannosidase 01 natural sciences Biochemistry Substrate Specificity 03 medical and health sciences chemistry.chemical_compound symbols.namesake Humans Glycoside hydrolase Glycosyl Molecular Biology 010405 organic chemistry Organic Chemistry Glycosyl acceptor Glycosynthase Golgi apparatus 0104 chemical sciences 030104 developmental biology chemistry symbols Biocatalysis Molecular Medicine |
| Zdroj: | Chembiochem : a European journal of chemical biology. 18(14) |
| ISSN: | 1439-7633 |
| Popis: | In order for facilitating the synthesis of oligosaccharides, transglycosylation reactions mediated by glycoside hydrolases have been studied in various contexts. In this study, we examined the transglycosylating activity of a Golgi endo-α-mannosidase. We prepared various glycosyl donors and acceptors, and recombinant human Golgi endo-α-mannosidase and its various mutants were expressed. The enzyme was able to mediate transglycosylation from α-glycosyl-fluorides. Systematic screening of various point mutants revealed that the E407D mutant had excellent transglycosylation activity and extremely low hydrolytic activity. Substrate specificity analysis revealed that minimum motif required for glycosyl acceptor is Manα1- 2Man. The synthetic utility of the enzyme was demonstrated by generation of a high-mannose-type undecasaccharide (Glc1 Man9 GlcNAc2 ). |
| Databáze: | OpenAIRE |
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