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

Chem Commun (Camb). 2015 Feb 21;51(15):3083-6. doi: 10.1039/c4cc09772f.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Catalytic Domain
  • Pasteurella / enzymology
  • Sialyltransferases / chemistry*
  • beta-Galactoside alpha-2,3-Sialyltransferase


  • Bacterial Proteins
  • Sialyltransferases
  • beta-Galactoside alpha-2,3-Sialyltransferase