title: Stereoselective, nonenzymatic, intramolecular transfer of amino acids.
abstract: Biological systems synthesize proteins with an almost exclusive use of L-amino acids and virtually none of the D isomer. There has been no satisfactory explanation for the origin of this use of the L isomer. Research presented here shows that at pH 5, transfer of phenylalanine from the adenylate anhydride to ester occurs and is 95-97% efficient for the L isomer and only about 50% efficient for the D isomer. The origin of the use of the L isomer, given D-ribose nucleotides, may be based in part on this stereoselectivity.
authors.affiliation: Department of Biochemistry, University of Alabama, Birmingham 35294.
authors.forename: N S
authors.initials: NS
authors.lastname: Wickramasinghe
authors.forename: M P
authors.initials: MP
authors.lastname: Staves
authors.forename: J C
authors.initials: JC
authors.lastname: Lacey
mesh_terms: D000249:Adenosine Monophosphate / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry; D000596:Amino Acids / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D007202:Indicators and Reagents; D007700:Kinetics; D008958:Models, Molecular; D008968:Molecular Conformation; D010649:Phenylalanine; D013237:Stereoisomerism
chemical_list: D000596:Amino Acids; D007202:Indicators and Reagents; C042022:phenylalanyl-AMP anhydride; D000249:Adenosine Monophosphate; D010649:Phenylalanine