Issue 15, 2015
From the journal:

Chemical Communications

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

Katharina Schmölzer,a   Tibor Czabany,b   Christiane Luley-Goedl,a   Tea Pavkov-Keller,a   Doris Ribitsch,a   Helmut Schwab,c   Karl Gruber,d   Hansjörg Webere  and  Bernd Nidetzky*ab  

* Corresponding authors

a Austrian Centre of Industrial Biotechnology, Petersgasse 14, 8010 Graz, Austria

b Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, Petersgasse 12/1, 8010 Graz, Austria
E-mail: bernd.nidetzky@tugraz.at
Fax: +43 316 8738434
Tel: +43 316 8738400

c Institute of Molecular Biotechnology, Graz University of Technology, NAWI Graz, Petersgasse 14, 8010 Graz, Austria

d Institute of Molecular Biosciences, University of Graz, NAWI Graz, Humboldtstrasse 50/3, 8010 Graz, Austria

e Institute of Organic Chemistry, Graz University of Technology, NAWI Graz, Stremayrgasse 9, 8010 Graz, Austria

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.

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

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Article information

DOI
https://doi.org/10.1039/C4CC09772F
Article type
Communication
Submitted
06 Dec 2014
Accepted
24 Dec 2014
First published
07 Jan 2015

Chem. Commun., 2015,51, 3083-3086

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

K. Schmölzer, T. Czabany, C. Luley-Goedl, T. Pavkov-Keller, D. Ribitsch, H. Schwab, K. Gruber, H. Weber and B. Nidetzky, Chem. Commun., 2015, 51, 3083 DOI: 10.1039/C4CC09772F

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