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Complete switch from α-2,3- to α-2,6-regioselectivity in Pasteurella dagmatis β-d-galactoside sialyltransferase by active-site redesign

Chemical Communications, ISSN: 1364-548X, Vol: 51, Issue: 15, Page: 3083-3086
2015
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Article Description

Structure-guided active-site redesign of a family GT-80 β-d-galactoside sialyltransferase (from Pasteurella dagmatis) to change enzyme regioselectivity from α-2,3 in the wild type to α-2,6 in a P7H-M117A double mutant is reported. Biochemical data for sialylation of lactose together with protein crystal structures demonstrate highly precise enzyme engineering.

Bibliographic Details

Schmölzer, Katharina; Czabany, Tibor; Luley-Goedl, Christiane; Pavkov-Keller, Tea; Ribitsch, Doris; Schwab, Helmut; Gruber, Karl; Weber, Hansjörg; Nidetzky, Bernd

Royal Society of Chemistry (RSC)

Materials Science; Chemical Engineering; Chemistry

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