Deacylation of acylamino compounds other than penicillins by the cell-bound penicillin acylase of Escherichia coli.
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.
D000577:Amides / Q000378:metabolism; D000581:Amidohydrolases / Q000378:metabolism*; D000596:Amino Acids / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D005998:Glycine / Q000378:metabolism; D006626:Hippurates / Q000378:metabolism; D010648:Phenylacetates / Q000378:metabolism; D013237:Stereoisomerism
D000577:Amides; D000596:Amino Acids; D006626:Hippurates; D010648:Phenylacetates; D000581:Amidohydrolases; D005998:Glycine