Functional and Structural Analyses of the Inactive Recombinant Enzymes from Hyperthermophilic Archaea Produced in <i>Escherichia coli</i>

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  • GODA Shuichiro
    Department of Advanced Engineering, Graduate School of Engineering, Nagasaki University
  • SAKURABA Haruhiko
    Department of Applied Biological Science, Faculty of Agriculture, Kagawa University
  • OHSHIMA Toshihisa
    Department of Biomedical Engineering, Faculty of Engineering, Osaka Institute of Technology

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Other Title
  • 大腸菌体内で不活性型として生産される超好熱アーキア由来リコンビナント酵素の機能・構造解析
  • ダイチョウ キンタイ ナイ デ フカッセイガタ ト シテ セイサン サレル チョウコウネツ アーキア ユライ リコンビナント コウソ ノ キノウ ・ コウゾウ カイセキ

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Abstract

<p>Several enzymes containing glutamate dehydrogenase from hyperthermophiles have been reported to be expressed as inactive forms in a mesophile Escherichia coli. We have recently found that the recombinant Pyrobaculum islandicum glutamate dehydrogenase（Pis-GDH）expressed in E. coli hardly exhibits the activity, and that the heat treatment dramatically activated the inactive enzyme to the activity level comparable to that of the native enzyme. This review focuses mainly on the structural changes of the Pis-GDH in heat activation measured by small-angle X-ray scattering, differential scanning calorimetry, circular dichroism, and fluorescence spectrum in the presence of 8-anilinonaphthalene-1-sulfonate. In addition, we describe the hyperthermophilic homoserine dehydrogenase showing unique coenzyme preference as other type of the inactive recombinant enzyme. This may be informative for the better production of active recombinant enzymes from hyperthermophiles.</p>

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