Substrate specificity of penicillin acylase of E. coli.

Abstract

The hydrolysis of several phenylacetylamino compounds was studied using a purified preparation of Escherichia coli penicillin acylase. The L-isomers of phenylacetyl amino acids were cleaved much faster than the D-isomers. The same observation was made for some phenylacetylamino .beta.-lactams. When the .beta.-lactam ring was incorporated in a penam or cephem ring system, the D-isomers were hydrolyzed somewhat faster than the L-isomers. Benzylpenicillins with a hydroxy- or an amino-group in .alpha.-position of the side chain were hydrolyzed in the normal and the 6-epi-series.