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Abstract
The interaction of penicillinase (penicillin amidohydrolase, EC 3.5.2.6) with substrates and with their analogs produces a conformational change in the active site of the enzyme, which is manifested in changed reactivity towards iodine and p-chloromercuribenzoate (p-hydroxymercuribenzoate) and in modified stability to heat, photo-oxidation, -and proteolysis. The analogs studied were (a) derivatives of 6-aminopenicillanic acid, which differ from the substrates in the structure of the side-chain, and (b) derivatives of 7-aminocephalosporanic acid, which differ in the structure of the nucleus.
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