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.

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. Research Abstract Details 

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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. Abstract Text:

Mamoru Nishimoto,Haruhide Mori,Tsuneharu Moteki,Yukiko Takamura,Gaku Iwai,Yu Miyaguchi,Masayuki Okuyama,Jintanart Wongchawalit,Rudee Surarit,Jisnuson Svasti,Atsuo Kimura,Seiya Chiba,

cDNAs encoding three alpha-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.

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. Publishing Authors By Initials

M Nishimoto,H Mori,T Moteki,Y Takamura,G Iwai,Y Miyaguchi,M Okuyama,J Wongchawalit,R Surarit,J Svasti,A Kimura,S Chiba,

For similar enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: glucosidases: alpha-glucosidases research abstracts see: enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: glucosidases: alpha-glucosidases research

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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. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Bioscience, biotechnology, and biochemistry

VOLUME: 71

Page Numbers: 1703-16

Journal Abbreviation: Biosci. Biotechnol. Biochem.

ISSN: 0916-8451

DAY: 7

MONTH: 07

YEAR: 2007

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. Information

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LANGUAGE: eng

NlmUniqueID: 9205717

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. Keywords Mesh Terms:

KEYWORDS: alpha-Glucosidases

MESH TERMS: genetics

Chemical & Substance for Abstract: 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. Information

Substance Name: alpha-Glucosidases

Registry Number: EC 3.2.1.20

Grant and Affiliation Information for 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.

AFFILIATION: Division of Applied Bioscience, Research Faculty of Agriculture, Hokkaido University, Sapporo, Japan.

Country: Japan

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MEDLINETA: Biosci Biotechnol Biochem

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