Thermus thermophilus無機ピロリン酸加水分解酵素の三量体間界面改変による耐熱化 Thermostabilization by the Improvement of Intertrimeric Residues in Thermus thermophilus Inorganic Pyrophosphatase

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著者

    • 田中 浩史 Tanaka Hiroshi
    • Laboratory of Biochemistry, Department of Mathematical and Natural Sciences, Faculty of Integrated Arts and Sciences, The University of Tokushima
    • 前田 歩 Maeda Ayumi
    • Laboratory of Biochemistry, Department of Mathematical and Natural Sciences, Faculty of Integrated Arts and Sciences, The University of Tokushima
    • 京極 仁美 Kyogoku Hitomi
    • Laboratory of Biochemistry, Department of Mathematical and Natural Sciences, Faculty of Integrated Arts and Sciences, The University of Tokushima
    • 香西 美甫 Kouzai Miho
    • Laboratory of Biochemistry, Department of Mathematical and Natural Sciences, Faculty of Integrated Arts and Sciences, The University of Tokushima
    • 佐藤 高則 Satoh Takanori
    • Laboratory of Biochemistry, Department of Mathematical and Natural Sciences, Faculty of Integrated Arts and Sciences, The University of Tokushima

抄録

Inorganic pyrophosphatase (EC. 3.6.1.1) from Thermus thermophilus (Tth PPase)is a thermostablehomohexamer of 174 amino acids,and its intertrimer interface is formed mainly by the symmetric α-helix Abetween subunits. Amino acids and their interactions composing intertrimer interface are different in hexamericFamily I PPases,and then it was deduced that Tth PPase showed high thermostability because of stabilizing thisinterface by interactions of these residues. In this study,we focused on Thr138 and Ala141 residues in intertrimerinterface of Tth PPase to confirm the relationship between intertrimeric residues and thermostability, and thenimproved their combination to His and Asp/Glu (HD or HE variant).As results,the HD variant showed the highest thermostability of enzyme activity,fluorescence spectra, andquaternary structure in the wild type Tth PPase and all variants. Especially,about 38% of hexamer and almost40% of enzyme activity were observed in HD variant after heating even at 85℃. Therefore,we suggested thatthe conversion to a set of ionic His138 and Asp141 at intertrimer interface had increased the thermostability ofTth PPase,and then suppressed its thermal aggregation.

収録刊行物

  • 徳島大学総合科学部自然科学研究

    徳島大学総合科学部自然科学研究 22, 85-96, 2008-12

    徳島大学

各種コード

  • NII論文ID(NAID)
    110008694550
  • NII書誌ID(NCID)
    AN10065859
  • 本文言語コード
    ENG
  • 資料種別
    Departmental Bulletin Paper
  • 雑誌種別
    大学紀要
  • ISSN
    09146385
  • NDL 記事登録ID
    10784501
  • NDL 雑誌分類
    ZM1(科学技術--科学技術一般)
  • NDL 請求記号
    Z14-1395
  • データ提供元
    NDL  NII-ELS  IR 
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