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Functional and Structural Characterization of α-(1→2) Branching Sucrase Derived from DSR-E Glucansucrase

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Brison, Yoann | Pijning, Tjaard | Malbert, Yannick | Fabre, Émeline | Mourey, Lionel | Morel, Sandrine | Potocki-Veronese, Gabrielle | Monsan, Pierre | Tranier, Samuel | Remaud-Siméon, Magali | Dijkstra, Bauke, W

Edité par CCSD ; American Society for Biochemistry and Molecular Biology -

International audience. Background: The transglucosidase GBD-CD2 shows a unique ␣-(132) branching specificity among GH70 family members when catalyzing dextran glucosylation from sucrose. Results: The truncated form ⌬N 123-GBD-CD2 was biochemically studied and structurally characterized at 1.90 Å resolution. Conclusion: Dextran recognition and regiospecificity clearly involves a residue in subsite ϩ1. Significance: This is the first three-dimensional structure of a GH70 enzyme that reveals determinants of ␣-(132) linkage specificity.

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