Paper Report for: Bano_2003_Biochim.Biophys.Acta_1632_55
Reference
Title: Long-chain fatty acyl-CoA esters induce lipase activation in the absence of a water-lipid interface Bano MC, Gonzalez-Navarro H, Abad C Ref: Biochimica & Biophysica Acta, 1632:55, 2003 : PubMed
In most lipases a mobile element or lid domain covers the catalytic site of the enzyme and the lid opening event, which usually proceed at a lipid-water interface, is required to form the catalytically competent lipase. We report here a noticeable increase in activity of two fungal lipases assayed in aqueous solution in absence of any interface when adding submicellar concentrations of amphipathic physiological molecules like long-chain acyl-CoAs. The catalytic activity was dramatically dependent on the acyl chain length of the amphiphile and could be related with a lid-opening process. Our data support that lipase activation can be triggered in the absence of a well-defined interface, and stresses the notion that other non-aggregated amphipathic constituents of the local microenvironment can act as putative regulators of lipase activity.
        
Related information
Citations formats
Bano MC, Gonzalez-Navarro H, Abad C (2003) Long-chain fatty acyl-CoA esters induce lipase activation in the absence of a water-lipid interface Biochimica & Biophysica Acta1632: 55-61
Bano MC, Gonzalez-Navarro H, Abad C (2003) Biochimica & Biophysica Acta1632: 55-61