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Angew Chem Int Ed Engl. 2001 Nov 05;40(21):4007-4011. doi: 10.1002/1521-3773(20011105)40:21<4007::AID-ANIE4007>3.0.CO;2-F.

α(1-3)-Galactosyltransferase Inhibition Based on a New Type of Disubstrate Analogue.

Angewandte Chemie (International ed. in English)

Bernhard Waldscheck, Markus Streiff, Wolfgang Notz, Willy Kinzy, Richard R Schmidt

Affiliations

  1. Fachbereich Chemie, Universität Konstanz Fach M?725, 78457 Konstanz (Germany) Fax: (+49)?7531-883135.
  2. Novartis Pharma AG Transplantation Research, WSJ 386.643 4002 Basel (Switzerland).

PMID: 29712256 DOI: 10.1002/1521-3773(20011105)40:21<4007::AID-ANIE4007>3.0.CO;2-F

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.

© 2001 WILEY-VCH Verlag GmbH, Weinheim, Fed. Rep. of Germany.

Keywords: C-glycosides ; C-ketosides ; disubstrate analogues ; inhibitors ; transferases

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