Stereoselective formation of bis(alpha-aminoacyl) esters of 5'-AMP suggests a primitive peptide synthesizing system with a preference for L-amino acids

Abstract

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.