Reversibility of the ampicillin-and nitrite-induced inactivation of beta-lactamase I.
beta-Lactamase I was isolated from Bacillus cereus 569/H. Treatment with ampicillin in the presence of sodium nitrite at pH 4 or 5 resulted in the inactivation of the enzyme presumably by modification of a carboxyl group in the active site. However, this inactivation was rapidly, reversible at neutral pH and the available evidence points to the participation of a second carboxyl group which is involved in the reactivation process.
D000581:Amidohydrolases / Q000302:isolation & purification / Q000378:metabolism*; D000667:Ampicillin / Q000494:pharmacology*; D001409:Bacillus cereus / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009573:Nitrites / Q000494:pharmacology*; D010400:Penicillin G
D009573:Nitrites; D000667:Ampicillin; D000581:Amidohydrolases; D010400:Penicillin G