DISTRIBUTION AND SUBSTRATE SPECIFICITY OF BENZYLPENICILLIN ACYLASE

  • 1 January 1963
    • journal article
    • research article
    • Vol. 11  (1) , 1-+
Abstract
Benzylpenicillin acylase hydrolyzes benzylpenicillin to 6-aminopenicillanic acid and is widely distributed among 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 was 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.