マンソン住血吸虫症媒介中間宿主貝<i>Biomphalaria glabrata</i> cDNA由来フォスファーゲンキナーゼの分子生物学的研究

DOI Web Site 参考文献43件
  • AGATSUMA Takeshi
    Department of Environmental Health Science, Kochi Medical School, Kochi University
  • FUKUNAGA Sae
    Department of Environmental Health Science, Kochi Medical School, Kochi University
  • JARILLA Blanca R.
    Department of Environmental Health Science, Kochi Medical School, Kochi University
  • NAGATAKI Mitsuru
    Department of Environmental Health Science, Kochi Medical School, Kochi University
  • TOKUHIRO Shinji
    Department of Environmental Health Science, Kochi Medical School, Kochi University
  • XIAO Jing-Ying
    Department of Environmental Health Science, Kochi Medical School, Kochi University
  • DEVI Kangjam R.
    Department of Environmental Health Science, Kochi Medical School, Kochi University
  • NOMURA Haruka
    Department of Environmental Health Science, Kochi Medical School, Kochi University
  • SHIMADA Masaaki
    Department of Eco-epidemiology, Institute of Tropical Medicine, Nagasaki University
  • UDA Kouji
    Laboratory of Biochemistry, Faculty of Science, Kochi University
  • SUZUKI Tomohiko
    Laboratory of Biochemistry, Faculty of Science, Kochi University

書誌事項

タイトル別名
  • Molecular characterization of a cDNA-derived phosphagen kinase from <i>Biomphalaria glabrata</i>, the intermediate host of <i>Schistosoma mansoni</i>
  • Molecular characterization of a cDNA derived phosphagen kinase from Biomphalaria glabrata the intermediate host of Schistosoma mansoni

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抄録

The present study contains the first description of phosphagen kinase (PK) from the intermediate snail host, Biomphalaria glabrata. We determined the cDNA sequence of PK from the snail B. glabrata, a vector of Schistosoma mansoni, and then cloned the cDNA into a pMAL plasmid and expressed it in Escherichia coli as a fusion protein with maltose-binding protein (MBP). The recombinant protein, consisting of 353 amino acids, has a calculated molecular mass of 39,376 Da and an estimated isoelectric point (pI) of 6.12. B. glabrata PK showed significant activity with the substrate L-arginine, indicating AK, and has the following kinetic constants determined for the forward reaction: KmArg=0.26 mM, KdArg=0.28 mM, kcat=20.3 s-1 and Vmax=30.4 μmol Pi/min/mg protein. Comparison of kcat/KmArg values with other AKs indicates that B. glabrata AK has a high catalytic efficiency (78.12 s-1 mM-1), although it exhibited weak synergism during substrate binding (KdArg/KmArg=1.08). In view of the significance of AK in temporal energy buffering, this enzyme may be a novel molluscicide target to control B. glabrata and consequently control the transmission of schistosomiasis.

収録刊行物

  • 衛生動物

    衛生動物 62 (1), 1-11, 2011

    日本衛生動物学会

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