title: N-Acetyl-D- and L-esters of 5'-AMP hydrolyze at different rates.
abstract: Studies of the properties of aminoacyl derivatives of 5'-AMP are aimed at understanding the origin of the process of protein synthesis. Aminoacyl (2',3') esters of 5'-AMP can serve as models of the 3'-terminus of aminoacyl tRNA. We report here on the relative rates of hydrolysis of Ac-D- and L-Phe AMP esters as a function of pH. At all pHs above 3, the rate constant of hydrolysis of the Ac-L-Phe ester is 1.7 to 2.1 times that of Ac-D-Phe ester. The D-isomer seems partially protected from hydrolysis by a stronger association with the adenine ring of the 5'-AMP.
authors.affiliation: Department of Biochemistry, University of Alabama at Birmingham, USA.
authors.forename: N S
authors.initials: NS
authors.lastname: Wickramasinghe
authors.forename: J C
authors.initials: JC
authors.lastname: Lacey
mesh_terms: D000215:Acylation; D000249:Adenosine Monophosphate / Q000031:analogs & derivatives / Q000737:chemistry*; D000596:Amino Acids / Q000737:chemistry*; D000812:Anhydrides / Q000737:chemistry; D004952:Esters / Q000737:chemistry*; D019143:Evolution, Molecular; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007536:Isomerism; D010649:Phenylalanine / Q000737:chemistry*; D011506:Proteins / Q000138:chemical synthesis*
chemical_list: D000596:Amino Acids; D000812:Anhydrides; D004952:Esters; D011506:Proteins; D000249:Adenosine Monophosphate; D010649:Phenylalanine