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It was demonstrated that phenylmethanesulfonyl fluoride-a very potent inhibitor of penicillin amidase from Escherichia coli-binds covalently to the enzyme in molar ratio 1:1. The chloride, the azide and the N-hydroxysuccinimide ester of phenylmethanesulfonic acid are also very strong inactivators of the amidase. Weaker inhibition was noted with para-substituted phenylmethanesulfonyl chlorides and with phenylethanesulfonyl and alkylsulfonyl chlorides. The inactivated amidase could be reactivated by incubation either with 6-amino-penicillanic acid or with proteins from E. coli extract. Benzyl isocyanate is also a potent covalent inhibitor of the amidase but inactivated amidase could be not reactivated in this way. It was demonstrated that representatives of all inactivator types bind to one active site of the amidase. Interdependence between inactivation rate and stability of some sulfonyl inhibitors was observed. No inhibition was noted the amide, the hydrazide and the methyl ester of phenylmethanesulfonic acid.

Phenylalkylsulfonyl Derivatives as Covalent Inhibitors of Penicillin Amidase