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Updated: Feb 11, 2026

Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues
Published on: February 17, 2017
α(1-3)-Galactosyltransferase Inhibition Based on a New Type of Disubstrate Analogue
Bernhard Waldscheck1, Markus Streiff2, Wolfgang Notz1
1Fachbereich Chemie, Universität Konstanz Fach M 725, 78457 Konstanz (Germany) Fax: (+49) 7531-883135.
Abstract:
How do retaining glycosyltransferases function? To answer this question, UDP-Gal and galactose were covalently linked to form disubstrate analogues 1, of which surprisingly 1β and not 1α inhibited α(1-3)-galactosyltransferases very well. An understanding of this inhibition is a key to the pharmacological prevention of hyperacute rejection in pig to primate xenotransplantation.
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