Characterization of a Novel Polypeptide N-Acetylgalactosaminyltransferase (dGalNAc-T3) from Drosophila(Biochemistry/Molecular Biology)
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概要
- 論文の詳細を見る
Polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferases) catalyze the initial reaction of mucin-type O-glycosylation. Here, we report the first biochemical characterization of one of the Drosophila GalNAc-transferases, dGalNAc-T3. This enzyme retains conserved motifs essential for the catalytic activity, but is a novel isozyme in that it has several inserted sequences in its lectin-like domain. Northern hybridization analysis of this isozyme identified a 2.5-kb mRNA in Drosophila larva. Biochemical characterization was carried out using the recombinant soluble dGalNAc-T3 expressed in COS7 cells. dGalNAc-T3, which required Mn^<2+> for the activity, had a pH optimum ranging from pH 7.5 to 8.5, and glycosylated most effectively at 29-33℃. Its K_m for UDP-GalNAc was 10.7 μM, which is as low as that of mammalian isozymes. dGalNAc-T3 glycosylated the peptides containing a sequence of XTPXP or TTAAP most efficiently. The enzyme was irreversibly inhibited by p-chloromercuriphenylsulphonic acid, indicating the presence of essential Cys residues for the activity.
- 公益社団法人日本薬学会の論文
- 2004-10-01
著者
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Nakamura Norifumi
President's Office Yoshitomi Pharmaceutical Industries Ltd.
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Nakamura Norihiro
Department Of Biological Sciences Graduate School Of Science Osaka University
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Katano Kenji
Department Of Biotechnology Faculty Of Engineering Kyoto Sangyo University
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NAKAMURA Naosuke
Department of Biotechnology, Faculty of Engineering, Kyoto Sangyo University
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TOBA Shinya
Department of Biotechnology, Faculty of Engineering, Kyoto Sangyo University
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KUROSAKA Akira
Department of Biotechnology, Faculty of Engineering, Kyoto Sangyo University
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Toba Shinya
Department Of Biotechnology Faculty Of Engineering Kyoto Sangyo University
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Kurosaka Akira
Department Of Biotechnology Faculty Of Engineering Kyoto Sangyo University
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