書誌事項
- タイトル別名
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- Functional and Structural Analyses of the Inactive Recombinant Enzymes from Hyperthermophilic Archaea Produced in <i>Escherichia coli</i>
- 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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<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>
収録刊行物
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- 日本結晶学会誌
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日本結晶学会誌 58 (5), 215-220, 2016
日本結晶学会
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詳細情報 詳細情報について
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- CRID
- 1390282679065865088
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- NII論文ID
- 130005267923
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- NII書誌ID
- AN00188364
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- ISSN
- 18845576
- 03694585
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- NDL書誌ID
- 027737182
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
- Crossref
- CiNii Articles
- KAKEN
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- 抄録ライセンスフラグ
- 使用不可
