Reversibility of the ampicillin- and nitrite-induced inactivation of β-lactamase I

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Abstract
.beta.-Lactamase I [EC 3.5.2.5] was isolated from Bacillus cereus 569/H. Treatment with ampicillin in the presence of NaNO2 at pH 4 or 5 resulted in the inactivation of the enzyme presumably by modification of a carboxyl group in the active site. This inactivation was rapidly reversible at neutral pH, and the available evidence points to the participation of a 2nd carboxyl group which is involved in the reactivation process.