Crystal Structure of Asparagine Synthetase-Evolutional Relationship to Class II Aminoacyl-tRNA Synthetase.

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  • アスパラギン合成酵素の結晶構造　ＩＩ型アミノアシルーｔＲＮＡ合成酵素との進化上の関係
  • 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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Abstract

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.

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