Bacterial hydrolase

Bacterial hydrolases are a broad and diverse group of enzymes that catalyze the hydrolytic cleavage of chemical bonds, such as those found in proteins, lipids, carbohydrates, and nucleic acids (NCBI, 2023). In bacteria, these enzymes are essential for fundamental processes including nutrient acquisition, signal transduction, and the constant remodeling of the peptidoglycan cell wall (Vollmer et al., 2008). Many bacterial hydrolases also function as virulence factors, facilitating the invasion of host tissues and the evasion of the immune system. From a clinical perspective, the most prominent members of this class are beta-lactamases, which hydrolyze the beta-lactam ring of antibiotics, rendering them inactive and leading to widespread antimicrobial resistance (Bush & Bradford, 2016). Therapeutic strategies often involve the use of hydrolase inhibitors, such as avibactam or vaborbactam, which are administered alongside antibiotics to protect them from degradation (StatPearls, 2023). While targeting these enzymes is highly effective for treating infections, challenges include the rapid evolution of new enzyme variants and the potential for disrupting the host's beneficial commensal microbiota.

Other names

Bacterial hydrolytic enzymeBacterial esteraseBacterial proteaseBacterial glycosidaseBacterial lipase

Inhibition of enzymatic hydrolysis of substrates, often through covalent or non-covalent binding to the active site to prevent the cleavage of chemical bonds.