Publication: 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
Issued Date
2007-09-10
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13476947
09168451
09168451
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2-s2.0-34548400313
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Mahidol University
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SCOPUS
Bibliographic Citation
Bioscience, Biotechnology and Biochemistry. Vol.71, No.7 (2007), 1703-1716
Suggested Citation
Mamoru Nishimoto, Haruhide Mori, Tsuneharu Moteki, Yukiko Takamura, Gaku Iwai, Yu Miyaguchi, Masayuki Okuyama, Jintanart Wongchawalit, Rudee Surarit, Jisnuson Svasti, Atsuo Kimura, Seiya Chiba 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. Bioscience, Biotechnology and Biochemistry. Vol.71, No.7 (2007), 1703-1716. doi:10.1271/bbb.70125 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/24120
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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
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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.