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Appl Environ Microbiol. 1963 January; 11(1): 1-6

Distribution and Substrate Specificity of Benzylpenicillin Acylase¹

Fermentation Research Department, Chas. Pfizer & Co., Inc., Groton, Connecticut

ABSTRACT

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 the preferred substrate; all departures from the benzylpenicillin side-chain structure led to reduction of substrate activity (the greater the departure, the greater the reduction in activity). Penicillin amides and methyl esters were also hydrolyzed, as were suitable N-acyl derivatives of 7-aminocephalosporanic acid. Occurrence of an enzyme activity which hydrolyzes benzylpenicillinamide to benzylpenicillin was detected in certain strains of yeasts.

¹ Presented in part at the 137th National Meeting (St. Louis, Mo.), March 27-30, 1961, and the 140th National Meeting (Chicago, Ill.) September 4-8, 1961, of the American Chemical Society.