Complete switch from α-2,3- to α-2,6-regioselectivity in Pasteurella dagmatis β-<scp>d</scp>-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.