Substrate specificity of penicillin acylase of E. coli.
- 1 January 1978
- journal article
- research article
- Published by Japan Antibiotics Research Association in The Journal of Antibiotics
- Vol. 31 (8) , 783-788
- https://doi.org/10.7164/antibiotics.31.783
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.This publication has 5 references indexed in Scilit:
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- Preparation and isomerization of 5-epibenzylpenicillinsThe Journal of Organic Chemistry, 1976
- Enzymatic Deacylation of S 35 -BenzylpenicillinJournal of Bacteriology, 1965
- DISTRIBUTION AND SUBSTRATE SPECIFICITY OF BENZYLPENICILLIN ACYLASE1963
- SPECIFICITY OF AMINO ACID ACYLASESJournal of Biological Chemistry, 1952