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Glycobiology Advance Access published online on May 28, 2008
Glycobiology, 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

Communications

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, CANADA T6G 2G2
3 Carlsberg Laboratory, Gamle Carlsberg Vej 10, 2500 Valby, Denmark

1 Author to whom correspondence should be addressed: Prof. John Klassen, E-mail: john.klassen{at}ualberta.ca

Received on March 21, 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 association of 1 to 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 GTs induced by the simultaneous binding of 1 and UDP.

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


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N. Soya, G. K Shoemaker, M. M Palcic, and J. S Klassen
Comparative study of substrate and product binding to the human ABO(H) blood group glycosyltransferases
Glycobiology, November 1, 2009; 19(11): 1224 - 1234.
[Abstract] [Full Text] [PDF]


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