Human alpha1, 3 fucosyltransferases (FTs) are biologically important enzymes that catalyze the final step in the synthesis of ligands for adhesion molecules and important antigens. In spite of their important functions, very little biochemical information exists on these proteins beyond a predicted amino acid sequence and the identification of a limited set of naturally occurring mutants. The goal of the proposed research is to obtain information on the biochemistry of this class of enzymes, with the ultimate aim of identifying amino acids within these proteins that are involved in acceptor (e.g. oligosaccharides) and nucleotide sugar donor substrate binding, and catalysis. Experiments will focus on identifying amino acids that are involved in the binding of the nucleotide sugar donor substrate. In addition, an analysis of the disulfide bonding pattern of the FTs will be done by mass spectrometric analysis. The information obtained from the combination of molecular biology, biochemistry and protein analysis will provide detailed information on this family of glycosyltransferases and this information will generate a model that can be utilized to design future studies of these important proteins.
Human alpha1,3 fucosyltransferases are biologically important proteins that calalyze the final step in the synthesis of binding partners for adhesion molecules and important antigens. The goal of the proposed research is to obtain information on the biochemistry of this class of proteins, with the ultimate aim of identifying units of these proteins that are involved in reactant binding and catalysis. Experiments will also focus on an analysis of critical linkages within the protein to define how the protein is folded into its active shape.
