Lacey J C, Thomas R D, Staves M P, Watkins C L
Department of Biochemistry, University of Alabama, Birmingham.
Biochim Biophys Acta. 1991 Feb 15;1076(3):395-400. doi: 10.1016/0167-4838(91)90482-f.
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.
在蛋白质生物合成过程中，每个氨基酸从氨酰腺苷酸转变为氨基酸酯，最终成为位于转运核糖核酸（tRNA）末端的AMP残基的2'（3'）肽基酯。因此，蛋白质合成的化学过程就是氨酰基和肽基AMP的化学过程。我们的数据揭示了5'-AMP及其酯的特性，这些特性应能通过双（2'，3'-氨酰基）酯中间体优先催化合成L-氨基酸肽。本文的研究结果涉及所提出过程中的一个步骤，结果表明，预先存在的Ac-L-苯丙氨酸单酯形成二酯的反应速度比预先存在的Ac-D-苯丙氨酸单酯快约2.5倍。
