Stereoselective formation of bis(alpha-aminoacyl) esters of 5'-AMP suggests a primitive peptide synthesizing system with a preference for L-amino acids.
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.
Lacey
J C
JC
Department of Biochemistry, University of Alabama, Birmingham.
Thomas
R D
RD
Staves
M P
MP
Watkins
C L
CL
D000249:Adenosine Monophosphate / Q000031:analogs & derivatives* / Q000138:chemical synthesis; D004952:Esters; D007202:Indicators and Reagents; D007536:Isomerism; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides / Q000138:chemical synthesis*; D010649:Phenylalanine / Q000031:analogs & derivatives*
D004952:Esters; D007202:Indicators and Reagents; D010455:Peptides; D000249:Adenosine Monophosphate; D010649:Phenylalanine; C048994:N-acetylphenylalanyl-adenosine monophosphate-anhydride; C044228:N-acetylphenylalanine