Complete switch from α-2, 3- to α-2, 6-regioselectivity in Pasteurella dagmatis β-d-galactoside sialyltransferase by active-site redesign. Issue 15 (26th January 2015)

• Record Type: Journal Article
• Authors: Schmölzer, Katharina; Czabany, Tibor; Luley-Goedl, Christiane; Pavkov-Keller, Tea; Ribitsch, Doris; Schwab, Helmut; Gruber, Karl; Weber, Hansjörg; Nidetzky, Bernd
• Is Part Of: Chemical communications. Volume 51:Issue 15(2015)
• Page Start: 3083
• Page End: 3086
• Publication Date: 2015-01-26
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c4cc09772f
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : Incorporation of Pro7His and Met117Ala substitutions resulted in a completely regioselective and highly efficient α-2, 6-sialyltransferase. 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.