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Volume 272, Number 30, Issue of July 25, 1997 pp. 18580-18585
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Deletion of Two Exons from the Lymnaea stagnalis beta 1right-arrow 4-N-Acetylglucosaminyltransferase Gene Elevates the Kinetic Efficiency of the Encoded Enzyme for Both UDP-sugar Donor and Acceptor Substrates

(Received for publication, November 13, 1996, and in revised form, March 27, 1997)

Hans Bakker Dagger , Angelique Van Tetering Dagger , Marja Agterberg Dagger , August B. Smit § , Dirk H. Van den Eijnden Dagger and Irma Van Die Dagger

From the Departments of Dagger  Medical Chemistry and § Experimental Zoology, Vrije Universiteit, 1081 BT Amsterdam, The Netherlands

Lymnaea stagnalis UDP-GlcNAc:GlcNAcbeta -R beta 1right-arrow4-N-acetylglucosaminyltransferase (beta 4-GlcNAcT) is an enzyme with structural similarity to mammalian UDP-Gal:GlcNAcbeta -R beta 1right-arrow4-galactosyltransferase (beta 4-GalT). Here, we report that also the exon organization of the genes encoding these enzymes is very similar. The beta 4-GlcNAcT gene (12.5 kilobase pairs, spanning 10 exons) contains four exons, encompassing sequences that are absent in the beta 4-GalT gene. Two of these exons (exons 7 and 8) show a high sequence similarity to part of the preceding exon (exon 6), suggesting that they have originated by exon duplication. The exon in the beta 4-GalT gene, corresponding to beta 4-GlcNAcT exon 6, encodes a region that has been proposed to be involved in the binding of UDP-Gal. The question therefore arose, whether the repeating sequences encoded by exon 7 and 8 of the beta 4-GlcNAcT gene would determine the specificity of the enzyme for UDP-GlcNAc, or for the less preferred UDP-GalNAc. It was found that deletion of only the sequence encoded by exon 8 resulted in a completely inactive enzyme. By contrast, deletion of the amino acid residues encoded by exons 7 and 8 resulted in an enzyme with an elevated kinetic efficiency for both UDP-sugar donors, as well as for its acceptor substrates. These results suggest that at least part of the donor and acceptor binding domains of the beta 4-GlcNAcT are structurally linked and that the region encompassing the insertion contributes to acceptor recognition as well as to UDP-sugar binding and specificity.


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