Computer Science
Scientific paper
Mar 1984
adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1984orli...15...45l&link_type=abstract
Origins of Life and Evolution of the Biosphere, Volume 15, Issue 1, pp.45-54
Computer Science
5
Scientific paper
We have used a novel spectrophotometric method to study the hydrolysis of N-acetylphenylalanyl adenylate anhydride (AcPhe-AMP) and phenylalanyl-adenylate anhydride (Phe-AMP) at low concentrations (10-5 M), 25 °C, constant buffer concentration (0.05 M), and as a function of pH. While Phe-AMP is susceptible principally to attack by OH-, with two different rates depending on whether the α-amino group of the amino acid is protonated or not, the AcPhe-AMP is susceptible to acid decomposition as well. At pH's 4 8, the Phe-AMP hydrolyzes faster than the AcPhe-AMP, but at pH less than 4 or pH greater than 8, the blocked form hydrolyzes faster. Both forms are also attacked by H2O, and at the same rate. Moreover, the hydrolysis of Phe-AMP is shown to be greatly catalyzed by carbonate, although the AcPhe-AMP is not subject to such catalysis. The rate laws for the various mechanisms and the activation energies for the hydrolyses at pH 7.1 are given.
Lacey C. Jr. J.
Mullins Dail W.
Senaratne Nalinie
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