Distribution and Substrate Specificity of Benzylpenicillin Acylase

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Distribution and substrate specificity of benzylpenicillin acylase.

Benzylpenicillin acylase, which hydrolyzes benzylpenicillin to 6-aminopenicillanic acid, was found to be widely distributed among members of the Schizomycetes, particularly in gram-negative bacteria, and in the genus Nocardia. The hydrolysis of a series of biosynthetic and semisynthetic penicillins by freeze-dried cells of a strain of Nocardia and of Proteus was studied. Benzylpenicillin was th...

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Residue Phe375 of cephalosporin acylase has been identified as one of the residues that is involved in substrate specificity. A complete mutational analysis was performed by substituting Phe375 with the 19 other amino acids and characterising all purified mutant enzymes. Several mutations cause a substrate specificity shift from the preferred substrate of the enzyme, glutaryl-7-ACA, towards the...

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[Study on substrate specificity of penicillin acylase of E. coli].

The hydrolysis of several phenylacetylamino compounds was studied using a purified preparation of E. coli penicillin acylase. The L-isomers of phenylacetyl amino acids were cleaved much faster than the D-isomers. The same observations was made for some phenylacetylamino beta-lactams. When the beta-lactam ring is incorporated in a penam or cephem ring system, the D-isomers were hydrolysed somewh...

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Mutations of penicillin acylase residue B71 extend substrate specificity by decreasing steric constraints for substrate binding.

Two mutant forms of penicillin acylase from Escherichia coli strains, selected using directed evolution for the ability to use glutaryl-L-leucine for growth [Forney, Wong and Ferber (1989) Appl. Environ. Microbiol. 55, 2550-2555], are changed within one codon, replacing the B-chain residue Phe(B71) with either Cys or Leu. Increases of up to a factor of ten in k (cat)/ K (m) values for substrate...

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Engineering the substrate specificity of a thermophilic penicillin acylase from thermus thermophilus.

A homologue of the Escherichia coli penicillin acylase is encoded in the genomes of several thermophiles, including in different Thermus thermophilus strains. Although the natural substrate of this enzyme is not known, this acylase shows a marked preference for penicillin K over penicillin G. Three-dimensional models were created in which the catalytic residues and the substrate binding pocket ...

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ژورنال

عنوان ژورنال: Applied Microbiology

سال: 1963

ISSN: 0003-6919

DOI: 10.1128/am.11.1.1-6.1963