Published in
Royal Society of Chemistry, Chemical Communications, 15(51), p. 3083-3086, 2015
DOI: 10.1039/c4cc09772f
Links
Tools
Complete switch from $α$-2,3- to $α$-2,6-regioselectivity in Pasteurella dagmatis $β$- d -galactoside sialyltransferase by active-site redesign
Journal article published in 2015 by
Katharina Schmölzer,
Tibor Czabany,
Christiane Luley-Goedl,
Tea Pavkov-Keller,
Doris Ribitsch,
Helmut Schwab,
Karl Gruber 
,
Hansjörg Weber,
Bernd Nidetzky
,
Hansjörg Weber,
Bernd Nidetzky
This paper is available in a repository.
Full text: Download
Published version:
archiving forbidden
Data provided by 
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.