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Complete switch from α-2,3- to α-2,6-regioselectivity in Pasteurella dagmatis β-D-galactoside sialyltransferase by
Katharina Schmölzer1, Tibor Czabany, Christiane Luley-Goedl
1Austrian Centre of Industrial Biotechnology, Petersgasse 14, 8010 Graz, Austria.
Abstract:
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.
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