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Glycobiology Advance Access originally published online on January 12, 2004
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Glycobiology vol 14 no 4 pp. 347-356, 2004
Glycobiology vol. 14 no. 4 © Oxford University Press 2004; all rights reserved.

Structure/function study of Lewis {alpha}3- and {alpha}3/4-fucosyltransferases: the {alpha}1,4 fucosylation requires an aromatic residue in the acceptor-binding domain

Fabrice Dupuy1, Agnès Germot, Raymond Julien and Abderrahman Maftah

Unité de Génétique Moléculaire Animale, UMR 1061 Université-INRA, GDR-CNRS 2590, Institut des Sciences de la Vie et de la Santé, Faculté des Sciences et Techniques, 87060 Limoges, France

Received on October 27, 2003; revised on December 30, 2003; accepted on December 30, 2003

All vertebrate {alpha}3- and {alpha}3/4-FUTs possess the characteristic acceptor-binding motif VxxHH(W/R)(D/E). FUT6 and FUTb enzymes, harboring R in the acceptor-binding motif, transfer fucose in {alpha}1,3 linkage, whereas FUT3 and FUT5 enzymes with W at the candidate position can also transfer fucose in {alpha}1,4 linkage—FUT3 being more efficient than FUT5. To determine the involvement of the W/R residue in acceptor recognition, we produced 34 variants of human FUT3, FUT5, FUT6, and ox FUTb Lewis enzymes. Among the FUT3 variants where W111 was replaced by the other amino acids, only enzymes with an aromatic residue at the candidate position kept about 50% of {alpha}1,4 activity and showed no changes in Km values for GDP-Fuc donor and H-type 1 acceptor substrates. All other substitutions produced enzymes with less than 20% of the {alpha}1,4 activity. Thus the ability of {alpha}3/4-FUTs to recognize type 1 substrates involves the aromatic character of W in the acceptor-binding domain. The {alpha}1,3 activity of FUT6 and FUTb significantly decreased when their R residue was substituted by basic or charged residues. Moreover, FUT3 and FUT5 variants with W->R substitution had a better affinity for H-type 2 substrate and higher {alpha}1,3 activities. Therefore the optimal fucose addition in {alpha}1,3 linkage requires the R residue in the acceptor-binding motif of Lewis FUTs.

1 To whom correspondence should be addressed; e-mail: fabrice.dupuy{at}unilim.fr


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