Burkholderia cepacia lipase (BCL)

Burkholderia cepacia lipase (BCL) is a potent extracellular enzyme secreted by the Burkholderia cepacia complex (BCC), a group of opportunistic Gram-negative bacteria that pose a significant threat to individuals with cystic fibrosis and immunocompromised patients (UniProt P22088). As a member of the triacylglycerol lipase family, BCL's primary biological function is the hydrolysis of fats into fatty acids and glycerol, which the bacterium utilizes for energy and as building blocks for its cell membrane (PubMed: 16151013). In clinical settings, BCL acts as a critical virulence factor by degrading host lung surfactants and cell membranes, thereby facilitating tissue invasion and triggering a robust inflammatory response that contributes to respiratory decline (PubMed: 24563318). Beyond its role in disease, BCL is highly regarded in the pharmaceutical and chemical industries as a robust biocatalyst due to its exceptional stability in organic solvents and high enantioselectivity (PubMed: 11028917). Therapeutic strategies targeting BCL focus on anti-virulence approaches, utilizing inhibitors like Orlistat or experimental boronic acid compounds to attenuate the pathogen's destructive capabilities without directly exerting the selective pressure associated with traditional antibiotics.

Other names

Lipase PSAmano Lipase PSTriacylglycerol lipaseB. cepacia lipaseLipAGlycerol ester hydrolase

BCL catalyzes the hydrolysis of long-chain triacylglycerols into glycerol and free fatty acids at the lipid-water interface. In a therapeutic context, inhibitors bind to the active site serine residue, preventing the enzyme from degrading host lipids and reducing the pathogen's virulence and ability to survive in the host environment.