UDP-GlcNAc: BetaGal Beta-1,3-N-Acetylglucosaminyltransferase 7 (B3GNT7)

  • Akira Seko
Reference work entry


UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 7 (B3GNT7, β3GnT7, EC, 2.4.1.- ) is one of the members of large β1,3-GlcNAc/Gal/GalNAc-transferase family (Narimatsu 2006). Like as many other glycosyltransferases, this enzyme is a type II membrane-bound protein, orienting its catalytic domain into the lumenal side of the Golgi apparatus. B3GNT7 preferentially acts on sulfated type 2 glycans as described below, indicating that B3GNT7 is responsible for the elongation of backbone structure of keratan sulfate: (1) 6-O-sulfation of nonreducing terminal GlcNAc residues by CHST6, (2) β-galactosylation at the 4-OH of SO3 →6GlcNAc by B4GALT4, (3) β-N-acetylglucosaminylation of the 3-OH of Gal residue by B3GNT7, (4) repeating (1)–(3), and (5) 6-O-sulfation of Gal residues by CHST1 (Fig. 31.1).


Ovarian Cancer Keratan Sulfate Backbone Structure Corneal Epithelial Cell Acceptor Substrate 
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Copyright information

© Springer Japan 2014

Authors and Affiliations

  1. 1.JST, ERATOWakoJapan

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