由tRNAPhe相互作用诱导的酵母苯丙氨酰-tRNA合成酶催化位点的构象激活：缺乏这些残基的tRNAPhe结合时腺苷或CpCpA三核苷二磷酸氨基酰化的触发。
Conformational activation of the yeast phenylalanyl-tRNA synthetase catalytic site induced by tRNAPhe interaction: triggering of adenosine or CpCpA trinucleoside diphosphate aminoacylation upon binding of tRNAPhe lacking these residues.
作者信息
Renaud M, Bacha H, Remy P, Ebel J P
出版信息
Proc Natl Acad Sci U S A. 1981 Mar;78(3):1606-8. doi: 10.1073/pnas.78.3.1606.
Adenosine or CpCpA trinucleoside diphosphate can be aminoacylated by phenylalanyl-tRNA synthetase [L-phenylalanine:tRNAPhe ligase (AMP forming), EC 6.1.1.20] when the reaction takes place in the presence of tRNAPhe deprived of its 3' adenosine or pCpCpA terminus. This shows that, upon interaction with tRNA, a structural alteration of the enzyme's active site is achieved. This process may be a determining step in the specificity of the aminoacylation reaction.
当反应在缺失3'腺苷或对羟基苯甲酰胞苷胞苷腺苷（pCpCpA）末端的苯丙氨酰 - tRNA存在的情况下进行时，腺苷或对羟基苯甲酰胞苷胞苷腺苷三磷酸二核苷酸可被苯丙氨酰 - tRNA合成酶[L - 苯丙氨酸：tRNA苯丙氨酸连接酶（形成AMP），EC 6.1.1.20]氨酰化。这表明，与tRNA相互作用时，酶活性位点发生了结构改变。该过程可能是氨酰化反应特异性的决定性步骤。
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