Multiple phospholipid substrates of phospholipase C/sphingomyelinase HR2 from Pseudomonas aeruginosa |
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| Authors: | López David J Collado M Isabel Ibarguren Maitane Vasil Adriana I Vasil Michael L Goñi Félix M Alonso Alicia |
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| Affiliation: | aUnidad de Biofísica (Centro Mixto CSIC-UPV/EHU), and Departamento de Bioquímica, Universidad del País Vasco, Barrio Sarriena s/n, 48940 Leioa, Bilbao, Spain;bServicio General de Resonancia Magnética Nuclear, Universidad del País Vasco, Bilbao, Spain;cDepartment of Microbiology, University of Colorado Denver, Anschutz Medical Center, Aurora, CO, USA |
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| Abstract: | The activity of phospholipase C/sphingomyelinase HR2 (PlcHR2) from Pseudomonas aeruginosa was characterized on a variety of substrates. The enzyme was assayed on liposomes (large unilamellar vesicles) composed of PC:SM:Ch:X (1:1:1:1; mol ratio) where X could be PE, PS, PG, or CL. Activity was measured directly as disappearance of substrate after TLC lipid separation. Previous studies had suggested that PlcHR2 was active only on PC or SM. However we found that, of the various phospholipids tested, only PS was not a substrate for PlcHR2. All others were degraded, in an order of preference PC > SM > CL > PE > PG. PlcHR2 activity was sensitive to the overall lipid composition of the bilayer, including non-substrate lipids. |
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| Keywords: | Abbreviations: Cer, ceramide Ch, cholesterol CL, cardiolipin DAG, diacylglycerol LUV, large unilamellar vesicles SM, sphingomyelin PC, phosphatidylcholine PE, phosphatidylethanolamine PG, phosphatidylglycerol PS, phosphatidylserine PLC, phospholipase C PlcHR2, phospholipase C/sphingomyelinase HR2 |
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