title: Complete switch from α-2,3- to α-2,6-regioselectivity in Pasteurella dagmatis β-D-galactoside sialyltransferase by active-site redesign.
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.
authors.affiliation: Austrian Centre of Industrial Biotechnology, Petersgasse 14, 8010 Graz, Austria.
authors.forename: Katharina
authors.initials: K
authors.lastname: Schmölzer
authors.forename: Tibor
authors.initials: T
authors.lastname: Czabany
authors.forename: Christiane
authors.initials: C
authors.lastname: Luley-Goedl
authors.forename: Tea
authors.initials: T
authors.lastname: Pavkov-Keller
authors.forename: Doris
authors.initials: D
authors.lastname: Ribitsch
authors.forename: Helmut
authors.initials: H
authors.lastname: Schwab
authors.forename: Karl
authors.initials: K
authors.lastname: Gruber
authors.forename: Hansjörg
authors.initials: H
authors.lastname: Weber
authors.forename: Bernd
authors.initials: B
authors.lastname: Nidetzky
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D020134:Catalytic Domain; D010325:Pasteurella / Q000201:enzymology; D012799:Sialyltransferases / Q000737:chemistry*; D000094663:beta-Galactoside alpha-2,3-Sialyltransferase
chemical_list: D001426:Bacterial Proteins; D012799:Sialyltransferases; D000094663:beta-Galactoside alpha-2,3-Sialyltransferase