Molecular Cloning of cDNAs and Genes for Three .ALPHA.-Glucosidases from European Honeybees, Apis mellifera L., and Heterologous Production of Recombinant Enzymes in Pichia pastoris

• NISHIMOTO Mamoru

  Division of Applied Bioscience, Research Faculty of Agriculture, Hokkaido University

• MORI Haruhide

  Division of Applied Bioscience, Research Faculty of Agriculture, Hokkaido University

• MOTEKI Tsuneharu

  Division of Applied Bioscience, Research Faculty of Agriculture, Hokkaido University

• TAKAMURA Yukiko

  Division of Applied Bioscience, Research Faculty of Agriculture, Hokkaido University

• IWAI Gaku

  Division of Applied Bioscience, Research Faculty of Agriculture, Hokkaido University

• MIYAGUCHI Yu

  Division of Applied Bioscience, Research Faculty of Agriculture, Hokkaido University

• OKUYAMA Masayuki

  Division of Applied Bioscience, Research Faculty of Agriculture, Hokkaido University

• WONGCHAWALIT Jintanart

  Division of Applied Bioscience, Research Faculty of Agriculture, Hokkaido University

• SURARIT Rudee

  Faculty of Dentistry, Mahidol University

• SVASTI Jisnuson

  Faculty of Science, Mahidol University

• KIMURA Atsuo

  Division of Applied Bioscience, Research Faculty of Agriculture, Hokkaido University

• CHIBA Seiya

  Division of Applied Bioscience, Research Faculty of Agriculture, Hokkaido University

Bibliographic Information

Other Title

• Molecular cloning of cDNAs and genes for three α-glucosidases from European honeybees, Apis mellifera L., and heterologous production of recombinant enzymes in Pichia pastoris
• Molecular cloning of cDNA s and genes for three a glucosidases from European honeybees Apis mellifera L and heterologous production of recombinant enzymes in Pichia pastoris
• Molecular Cloning of cDNAs and Genes for Three α-Glucosidases from European Honeybees,<i>Apis mellifera</i>L., and Heterologous Production of Recombinant Enzymes in<i>Pichia pastoris</i>

Abstract

cDNAs encoding three α-glucosidases (HBGases I, II, and III) from European honeybees, Apis mellifera, were cloned and sequenced, two of which were expressed in Pichia pastoris. The cDNAs for HBGases I, II, and III were 1,986, 1,910, and 1,915 bp in length, and included ORFs of 1,767, 1,743, and 1,704 bp encoding polypeptides comprised of 588, 580, and 567 amino acid residues, respectively. The deduced proteins of HBGases I, II, and III contained 18, 14, and 8 putative N-linked glycosylation sites, respectively, but at least 2 sites in HBGase II were unmodified by N-linked oligosaccharide. In spite of remarkable differences in the substrate specificities of the three HBGases, high homologies (38–44% identity) were found in the deduced amino acid sequences. In addition, three genomic DNAs, of 13,325, 2,759, and 27,643 bp, encoding HBGases I, II, and III, respectively, were isolated from honeybees, and the sequences were analyzed. The gene of HBGase I was found to be composed of 8 exons and 7 introns. The gene of HBGase II was not divided by intron. The gene of HBGase III was confirmed to be made up of 9 exons and 8 introns, and to be located in the region upstream the gene of HBGase I.

Journal

• Bioscience, Biotechnology, and Biochemistry

  Bioscience, Biotechnology, and Biochemistry 71 (7), 1703-1716, 2007

  Japan Society for Bioscience, Biotechnology, and Agrochemistry

Keywords

• honeybee α-glucosidase
• <I>Apis mellifera</I>
• cloning of α-glucosidase
• <I>Pichia pastoris</I>

Details

• CRID: 1390001206480464256
• NII Article ID: 10027516699
• NII Book ID: AA10824164
• DOI: 10.1271/bbb.70125
• ISSN: 13476947
• ISSN: 09168451
• HANDLE: 2115/30119
• NDL BIB ID: 8840102
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I8840102
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.70125
• Text Lang: en
• Data Source:
  • JaLC
  • IRDB
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed