PMID: 4901824Dec 1, 1969Paper

Deacylation of acylamino compounds other than penicillins by the cell-bound penicillin acylase of Escherichia coli

The Biochemical Journal
M Cole

Abstract

1. The action of the penicillin acylase enzyme of Escherichia coli N.C.I.B. 8743 on non-penicillin substrates suggests that the enzyme is an amidohydrolase. 2. The rates of hydrolysis for a small group of penicillins closely parallel those for a corresponding series of N-acylglycines. 3. For a series of E. coli strains, ability to cause rapid hydrolysis of phenylacetylglycine is correlated with ability to hydrolyse benzylpenicillin. 4. Amides and N-acylglycines are hydrolysed to the corresponding acids. The phenylacetyl group is hydrolysed most readily. Benzamide and beta-phenylpropionamide are not substrates. In a series of aliphatic acylglycines only valeryl- and hexanoyl-glycine are substrates. 5. Acylated l- but not d-alpha-amino acids are hydrolysed. d-alpha-Hydroxyphenylacetamide is a better substrate than the l compound.

Citations

Nov 29, 2014·Critical Reviews in Biotechnology·Vellore Sunder AvinashCheravakkattu Gopalan Suresh
Jul 19, 2013·Biotechnology Advances·Michal GrulichPavel Kyslík
Oct 1, 1980·Archives of Microbiology·D PfeiferR Plapp
Jan 1, 1973·Zeitschrift für allgemeine Mikrobiologie·E J Vandamme, J P Voets
Jan 1, 1975·Folia Microbiologica·V Vojtísek, J Slezák
Jan 1, 1991·Folia Microbiologica·Z A MahmoodS M Zoha
Oct 1, 1989·Applied and Environmental Microbiology·L J ForneyD M Ferber

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