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Glycobiology Advance Access originally published online on May 28, 2008
Glycobiology 2008 18(8):587-592; doi:10.1093/glycob/cwn043
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© The Author 2008. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Temperature-dependent cooperativity in donor–acceptor substrate binding to the human blood group glycosyltransferases

Glen K Shoemaker2, Naoto Soya2, Monica M Palcic3 and John S Klassen1,2

2 Department of Chemistry, University of Alberta, Edmonton, Alberta, T6G 2G2, Canada
3 Carlsberg Laboratory, Gamle Carlsberg Vej 10, 2500 Valby, Denmark

1 To whom correspondence should be addressed: e-mail: john.klassen{at}ualberta.ca

Received on March 21, 2008; revised on May 15, 2008; accepted on May 16, 2008

Affinities of the human blood group glycosyltransferases, {alpha}-(1->3)-N-acetylgalactosaminyltransferase (GTA) and {alpha}-(1->3)-galactosyltransferase (GTB) for their common acceptor substrate {alpha}-L-Fucp-(1->2)-β-D-Galp-O(CH2)7CH3 (1), in the absence and presence of bound uridine 5'-diphosphate (UDP) and Mn2+ were determined using temperature-controlled electrospray ionization mass spectrometry. The presence of bound UDP and Mn2+ in the donor binding site has a marked influence on the thermodynamic parameters for the association of 1 with GTA and GTB. Both the enthalpy and entropy of association ({Delta}Ha, {Delta}Sa) decrease significantly. However, the free energy of association ({Delta}Ga) is unchanged at physiological temperature. The differences in the {Delta}Ha and {Delta}Sa values determined in the presence and absence of bound UDP are attributed to structural changes in the glycosyltransferases induced by the simultaneous binding of 1 and UDP.

Key words: Association constants / electrospray ionization mass spectrometry / human ABO(H) blood group glycosyltransferases / protein-oligosaccharide complexes / stoichiometry


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