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- 中津 亨
- 京都大学化学研究所
書誌事項
- タイトル別名
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- Crystal Structure of Asparagine Synthetase-Evolutional Relationship to Class II Aminoacyl-tRNA Synthetase.
- アスパラギン ゴウセイ コウソ ノ ケッショウ コウゾウ 2ガタ アミノアシルーtRNA ゴウセイ コウソ ト ノ シンカ ジョウ ノ カンケイ
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The crystal structure of Eschelichia coli asparagine synthetase has been determined by X-ray diffraction analysis. The overall structure of the enzyme is remarkably similar to that of the catalytic domain of yeast aspartyl-tRNA synthetase despite low sequence similarity (11%) . These enzymes have a commom reaction mechanism that implies the formation of an aminoacyl-adenylate intermediate. The active site architecture and most of the catalytic residues are also conserved in both enzymes. These proteins have probably evolved from a common ancester even though their sequence similarities are small.
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 41 (2), 129-135, 1999
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
- 1390001204085763328
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- NII論文ID
- 10002591613
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- NII書誌ID
- AN00188364
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- ISSN
- 18845576
- 03694585
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- NDL書誌ID
- 4732019
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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
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- CiNii Articles
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- 使用不可