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首页> 外文期刊>Angewandte Chemie >Structural Basis for the Recognition of para-Benzoyl-L-phenylalanine by Evolved Aminoacyl-tRNA Synthetases
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Structural Basis for the Recognition of para-Benzoyl-L-phenylalanine by Evolved Aminoacyl-tRNA Synthetases

机译:进化的氨酰基-tRNA合成酶识别对苯甲酰基-L-苯丙氨酸的结构基础

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摘要

A wide array of amino acids with novel chemical and biological properties have been genetically encoded in both prokaryotic and eukaryotic organisms,which include the efficient photo-cross-linker para-benzoyl-L-phenylalanine(pBpa,Figure 1).Orthogonal tRNA/aminoacyl-tRNA syn-thetase(aaRS)pairs that selectively recognize pBpa have been evolved from both Methanococcus jannaschii(Mj)and Escherichia coli(Ec)tyrosyl-tRNA synthetases(TyrRS)in bacteria and yeast,respectively.
机译:在原核生物和真核生物中都已经遗传编码了许多具有新颖化学和生物学特性的氨基酸,包括有效的光交联剂对苯甲酰基-L-苯丙氨酸(pBpa,图1)。正交tRNA /氨基酰基选择性识别pBpa的-tRNA合酶(aaRS)对分别从细菌和酵母中的詹氏甲烷球菌(Mj)和大肠杆菌(Ec)酪氨酰-tRNA合成酶(TyrRS)进化而来。

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