The rate determining step of N-acylamino acid hydrolysis catalyzed by Acylase-I (aminoacylase) and the polar effects in the reaction have been studied. It has been shown that Km (app) = KS consequently kcat = k2. The polar substituent effects were established for compounds substituted both in the N-acyl moiety and in the aminoacid side-chain. The role of polar effect manifests itself also in the case of halogen substituted acyl derivatives in the α- and β-position. It has been concluded that a nucleophilic attack occurs on the carbonyl carbon of the acylamino group in the rate determining step of the reaction.
|Number of pages||9|
|Journal||Biochemical and biophysical research communications|
|Publication status||Published - Sep 3 1971|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology