Beta-lactamase Class C (AmpC)

Class C β-lactamases, also known as AmpC β-lactamases or cephalosporinases, are enzymes produced by many Gram-negative bacteria that confer resistance to a broad range of β-lactam antibiotics. These enzymes hydrolyze the amide bond in the β-lactam ring of antibiotics, rendering them ineffective. They are serine hydrolases, utilizing a serine residue to attack and hydrolyze the β-lactam ring. AmpC beta-lactamases are not inhibited by classic inhibitors such as clavulanic acid, sulbactam, or tazobactam; some newer inhibitors like avibactam can inhibit AmpC enzymes. These enzymes are a major cause of resistance to extended-spectrum cephalosporins in clinical isolates.

Other names

AmpC beta-lactamaseCephalosporinase

Hydrolyzes the beta-lactam ring of antibiotics, rendering them inactive.