Trends in Glycoscience and Glycotechnology
Online ISSN : 1883-2113
Print ISSN : 0915-7352
ISSN-L : 0915-7352
The Roles of the N-terminal α-helical and C-terminal Src Homology 3 Domains in the Enzymatic Functions of FUT8
Hideyuki IharaYoshitaka Ikeda
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2021 Volume 33 Issue 193 Pages E69-E73


The core α1,6-fucose structure, a major structure in asparagine-linked oligosaccharides, has a variety of biological and physiological characteristics. In eukaryotes, the core α1,6-fucose structure is biosynthesized by the α1,6-fucosyltransferase, FUT8. FUT8 is composed of a catalytic domain and two additional domains, an N-terminal α-helical (coiled-coil) and a C-terminal Src homology 3 (SH3) domain. The most recent structural and biochemical studies clearly show that these domains have precise functions. In this minireview, we summarize our current knowledge of the roles of the α-helical (coiled-coil) and SH3 domains in FUT8 functions, with a particular focus on the dimer formation that is essential for the activity, substrate recognition and other characteristics of this enzyme.

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© 2021 FCCA (Forum: Carbohydrates Coming of Age)
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