Long-chain fatty acyl-CoA esters induce lipase activation in the absence of a water-lipid interface.
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.
Bañó
M Carmen
MC
Departament de Bioquímica i Biologia Molecular, Facultat de Biologia, Universitat de València, E-46100 Burjassot, València, Spain.
González-Navarro
Herminia
H
Abad
Concepción
C
D000214:Acyl Coenzyme A / Q000378:metabolism*; D004789:Enzyme Activation / Q000187:drug effects*; D004952:Esters / Q000378:metabolism; D005848:Geotrichum / Q000201:enzymology; D008049:Lipase / Q000737:chemistry / Q000378:metabolism*; D050356:Lipid Metabolism; D008055:Lipids / Q000737:chemistry; D012233:Rhizopus / Q000201:enzymology; D012996:Solutions; D013379:Substrate Specificity; D014867:Water
D000214:Acyl Coenzyme A; D004952:Esters; D008055:Lipids; D012996:Solutions; D014867:Water; D008049:Lipase