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Volume 272, Number 36, Issue of September 5, 1997 pp. 22721-22727
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Purification and Characterization of UDP-N-Acetylglucosamine: 1,3-D-Mannoside 1,4-N-Acetylglucosaminyltransferase (N-Acetylglucosaminyltransferase-IV) from Bovine Small Intestine

(Received for publication, March 14, 1997, and in revised form, June 24, 1997)

Suguru Oguri , Mari Toba Minowa , Yoshito Ihara ^¶ , Naoyuki Taniguchi ^¶ , Hiroshi Ikenaga and Makoto Takeuchi

From the  Central Laboratories for Key Technology, KIRIN Brewery Co., Ltd., 1-13-5 Fukuura, Kanazawa-ku, Yokohama 236, Japan and the ^¶ Department of Biochemistry, Osaka University Medical School, 2-2 Yamadaoka, Suita, Osaka 565, Japan

A new 1,4-N-acetylglucosaminyltransferase (GnT) which involves in branch formation of Asn-linked complex-type sugar chains has been purified 224,000-fold from bovine small intestine. This enzyme requires divalent cations, such as Mn²⁺, and catalyzes the transfer of GlcNAc from UDP-GlcNAc to biantennary oligosaccharide and produces triantennary oligosaccharide with the 1-4-linked GlcNAc residue on the Man1-3 arm. The purified enzyme shows a single band of M_r 58,000 and behaves as a monomer. The substrate specificity demonstrated that the 1-2-linked GlcNAc residue on the Man1-3 arm (GnT-I product) is essential for the enzyme activity. 1-4-Galactosylaion to this essential 1-2-linked GlcNAc residue or N-acetylglucosaminylation to the -linked Man residue (bisecting GlcNAc, GnT-III product) blocks the enzyme action, while 1-6-N-acetylglucosaminylation to the Man1-6 arm (GnT-V product) increases the transfer. Based on these findings, we conclude that the purified enzyme is UDP-N-acetylglucosamine:-3-D-mannoside -1,4-N-acetylglucosaminyltransferase IV (GnT-IV), that has been a missing link on biosynthesis of complex-type sugar chains.

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