Alkaline Hydrolysis of N-acetylolycine

A faster reaction of the cation is expected for the compounds with a free amino group in the acyl moiety. Such an increase was observed for Ala-Ala-pnitroan~lide b.ut not with Ala-p-nitroanilide. Fischer · et al. concluded that a larger inc-rease in k1 with the latter compound was compensated by a reductionin k2/ki. so that the observed k1k2/(k~1 + k2) term remains the same. This assumption of a low k2/k-1-value militates earlier papers of Eriksson a. Mere s a a r [2}. For methylamino acid anilides the latter observed 23 orders of magnitude greater k1k2/(k1 +k2) terms for the cations, which were largely due to strongly enhanced ~/k-1-values. . .·· It thus appeared that a study of the hydrolysis of anilides of peptides and amino acids by another approach is appropriate. We now report _ _on . the Q-values of the rate constants for the indiviqual steps obtained for the hydrolysis of acetyl glycine p-nitro and p-acetyl-anilides (AGNA and .AGAA, respectively). Twoother substrates, the p-cyano·and p-ethoxycarbonyl-derivati ves, were found to be unstable in highly alkaline solution. _ Results and Discussion. The rate profiles for AGNA and AGAA are shown on Fig. 1. .At high pH the slopE; of log ko.bs tends towards zero because of