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α (1‐3)‐Galactosyltransferase Inhibition Based on a New Type of Disubstrate Analogue
Author(s) -
Waldscheck Bernhard,
Streiff Markus,
Notz Wolfgang,
Kinzy Willy,
Schmidt Richard R.
Publication year - 2001
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20011105)40:21<4007::aid-anie4007>3.0.co;2-f
Subject(s) - xenotransplantation , galactosyltransferase , glycosyltransferase , galactose , function (biology) , chemistry , computational biology , microbiology and biotechnology , biochemistry , biology , medicine , gene , transplantation , enzyme
How do retaining glycosyltransferases function? To answer this question, UDP‐Gal and galactose were covalently linked to form disubstrate analogues 1 , of which surprisingly 1 β and not 1 α 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.