Beta-lactamase AmpC (AmpC)

Beta-lactamase AmpC is a clinically significant bacterial enzyme belonging to the Ambler Class C group of serine beta-lactamases (NIH, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2650514/). It is primarily produced by Gram-negative bacteria, including members of the Enterobacteriaceae family and Pseudomonas aeruginosa, where it serves as a major mechanism of antibiotic resistance (MDPI, https://www.mdpi.com/2079-6382/11/8/1095). The enzyme functions by hydrolyzing the beta-lactam ring of various antibiotics, such as penicillins, cephamycins, and most cephalosporins, thereby rendering them inactive (Gosset, https://gosset.ai/target/Beta%20Lactamase%20Enzyme%20Ambler%20Class%20C%20(AmpC)). AmpC expression can be chromosomally encoded and inducible in response to certain antibiotics or constitutively expressed via plasmid-mediated genes (NIH, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6522639/). Unlike Class A beta-lactamases, AmpC is typically not inhibited by traditional inhibitors like clavulanic acid or tazobactam, posing a significant therapeutic challenge (NIH, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3862620/). Modern treatment strategies often involve the use of carbapenems or newer beta-lactamase inhibitor combinations, such as ceftazidime-avibactam, which are specifically designed to overcome AmpC-mediated resistance (MDPI, https://www.mdpi.com/2076-0817/13/4/318).

Other names

Class C beta-lactamaseCephalosporinaseAmbler Class C beta-lactamaseGroup 1 beta-lactamaseblaAmpC

Inhibition of beta-lactamase activity through covalent or non-covalent binding to the active-site serine, preventing the hydrolysis of beta-lactam antibiotics (MDPI, https://www.mdpi.com/2079-6382/11/8/1095).