Feb 15, 1991

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

Biochimica Et Biophysica Acta
J C LaceyC L Watkins

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.

Mentioned in this Paper

In Vivo NMR Spectroscopy
ACLY
One Step (dimethicone)
Amino Acids, I.V. solution additive
MT-TA gene
Triplet Codon-amino Acid Adaptor Activity
One-Step Dentin Bonding System
Transfer RNA
Protein Biosynthesis
N-acetylphenylalanine, (L)-isomer,3H-labeled

About this Paper

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