beetalaktamasientsyymien

Beta-lactamase enzymes, also known as beta-lactamases, are a diverse class of enzymes produced by bacteria. Their primary function is to hydrolyze the beta-lactam ring, a crucial structural component of beta-lactam antibiotics. This hydrolysis renders the antibiotic inactive, conferring resistance to the bacteria. This mechanism is a major cause of antibiotic resistance worldwide, posing a significant challenge to treating bacterial infections.

Beta-lactamase enzymes are classified based on their structure and function. The Ambler classification system, based on amino acid sequence homology, is widely used, categorizing them into four main classes: A, B, C, and D. Class A, C, and D enzymes are serine beta-lactamases, utilizing a serine residue in their active site for hydrolysis. Class B beta-lactamases are metalloenzymes, requiring a metal ion, typically zinc, for their catalytic activity.

The genes encoding beta-lactamases are often located on mobile genetic elements such as plasmids, facilitating their rapid spread among bacterial populations through horizontal gene transfer. This has led to the emergence of bacteria producing enzymes capable of degrading a wide range of beta-lactam antibiotics, including penicillins, cephalosporins, and carbapenems. The continuous discovery and evolution of new beta-lactamases necessitate ongoing research into novel antibiotics and strategies to overcome bacterial resistance.