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Accumulation of acyl-enzyme intermediates during turnover of penicillins by the class A beta-lactamase of Staphylococcus aureus PC1.
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Substrate-specific inactivation of staphylococcal penicillinase.
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Reversible inhibition of penicillinase by quinacillin: evaluation of mechanisms involving two conformational states of the enzyme.
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The reversible deactivation of beta-lactamase from Staphylococcus aureus by quinacillin and cephaloridine and its modification by antibodies.
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CENTA as a chromogenic substrate for studying beta-lactamases.
Antimicrob Agents Chemother. 2001 Jun;45(6):1868-71. doi: 10.1128/AAC.45.6.1868-1871.2001.
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Reversible deactivation of beta-lactamase by quinacillin. Extent of the conformational change in the isolated transitory complex.
Biochem J. 1986 Aug 1;237(3):723-30. doi: 10.1042/bj2370723.
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Identification of the site of covalent attachment of nafcillin, a reversible suicide inhibitor of beta-lactamase.
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Substrate-induced deactivation of penicillinases. Studies of beta-lactamase I by hydrogen exchange.
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Transition state structures of a dipeptide related to the mode of action of beta-lactam antibiotics.
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The inhibition of staphylococcal beta-lactamase by clavulanic acid.
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