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  • Title: Mucin synthesis. III. UDP-GlcNAc:Gal beta 1-3(GlcNAc beta 1-6)GalNAc-R (GlcNAc to Gal) beta 3-N-acetylglucosaminyltransferase, an enzyme in porcine gastric mucosa involved in the elongation of mucin-type oligosaccharides.
    Author: Brockhausen I, Williams D, Matta KL, Orr J, Schachter H.
    Journal: Can J Biochem Cell Biol; 1983 Dec; 61(12):1322-33. PubMed ID: 6231087.
    Abstract:
    Pig gastric mucosa microsomes have been shown to catalyze the following reaction: UDP-GlcNAc + Gal beta 1-3(GlcNAc beta 1-6)-GalNAc-alpha-R----GlcNAc beta 1-3Gal beta 1-3 (GlcNAc beta 1-6)GalNAc-alpha-R + UDP, where R is o-nitrophenyl or benzyl. The enzyme catalyzing this reaction has been named UDP-GlcNAc:Gal beta 1-3(GlcNAc beta 1-6)GalNAc-R (GlcNAc-R (GlcNAc to Gal) beta 3-N-acetylglucosaminyltransferase. The beta 3-GlcNAc-transferase does not act on Gal beta 1-3GalNAc-alpha-o-nitrophenyl. The beta 3-GlcNAc-transferase requires Mn2+ and Triton X-100 for optimal activity. The Vmax for the microsomal enzyme is 8.7 nmol/mg protein per hour and the Km values are 1.6, 0.9, and 1.2 mM for UDP-GlcNAc and the alpha-o-nitrophenyl and alpha-benzyl derivatives of Gal beta 1-3(GlcNAc beta 1-6)GalNAc, respectively. Pig gastric mucosa microsomes catalyze the transfer of GlcNAc to lactose to form GlcNAc beta 1-3Gal beta 1-4Glc, but fail to transfer GlcNAc to lactosyl ceramide, Gal beta 1-4GlcNAc, or Gal beta 1-4GlcNAc-beta-benzyl.
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