Investigation on the mechanism of acylase-I-catalyzed acylamino acid hydrolysis

L. Ötvös, E. Moravcsik, Gy Mády

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15 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1056-1064
Number of pages9
JournalBiochemical and biophysical research communications
Volume44
Issue number5
DOIs
Publication statusPublished - Sep 3 1971

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ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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