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

  • Akira Seko
Reference work entry

Abstract

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).

Keywords

Ovarian Cancer Keratan Sulfate Backbone Structure Corneal Epithelial Cell Acceptor Substrate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Japan 2014

Authors and Affiliations

  1. 1.JST, ERATOWakoJapan

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