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RESEARCH PRODUCT
Long-chain fatty acyl-CoA esters induce lipase activation in the absence of a water-lipid interface.
M. Carmen BañóHerminia González-navarroConcepción Abadsubject
Conformational changeCatalysisSubstrate SpecificityAcyl-CoAchemistry.chemical_compoundAmphiphileLipaseMolecular Biologychemistry.chemical_classificationAqueous solutionbiologyChemistryWaterEstersCell BiologyLipaseLipid MetabolismGeotrichumLipidsEnzyme ActivationSolutionsEnzymeBiochemistrybiology.proteinAcyl Coenzyme ALong chainRhizopusdescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2003-06-01 | Biochimica et biophysica acta |