STEREOSELECTIVE FORMATION OF BIS(ALPHA-AMINOACYL) ESTERS OF 5'-AMP SUGGESTS A PRIMITIVE PEPTIDE SYNTHESIZING SYSTEM WITH A PREFERENCE FOR L-AMINO-ACIDS
STEREOSELECTIVE FORMATION OF BIS(ALPHA-AMINOACYL) ESTERS OF 5'-AMP SUGGESTS A PRIMITIVE PEPTIDE SYNTHESIZING SYSTEM WITH A PREFERENCE FOR L-AMINO-ACIDS
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DOI：
10.1016/0167-4838(91)90482-f
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发表时间：
1991-02-15
期刊：
影响因子：
--
通讯作者：
WATKINS, CL
中科院分区：
文献类型：
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作者：
LACEY, JC;THOMAS, RD;WATKINS, CL
在蛋白质的生物合成中，每个氨基酸从氨酰腺苷酸变成氨基酸酯，最后变成tRNA末端AMP残基的2'（3'）肽基酯。 因此，蛋白质合成的化学是氨酰和肽酰AMP的化学。 我们的数据揭示了5 '-AMP及其酯的性质，这些性质应该允许通过双（2'，3 '-氨基酰基）酯中间体优先催化合成L-氨基酸肽。 本文中的结果涉及所提出的方法中的一个步骤，并且显示预先存在的Ac-L-Phe单酯反应形成二酯的速度比预先存在的Ac-D-Phe单酯快约2.5倍。
In the biosynthesis of proteins, each amino acid passes from the aminoacyl adenylate to become an amino acid ester and finally a 2' (3') peptidyl ester of the AMP residue at the end of a tRNA. Consequently, the chemistry of protein synthesis is the chemistry of aminoacyl and peptidyl AMP. Our data has revealed properties of 5'-AMP and its esters which should allow the preferential catalytic synthesis of L-amino acid peptides via a bis(2', 3'-aminoacyl) ester intermediate. Results in this paper concern one step in the proposed process and show that preexisting Ac-L-Phe monoester reacts about 2.5-times faster to form diester than preexisting Ac-D-Phe monoester.