Substrate specificity of lysophospholipase-transacylase from rat lung and its action on various physical forms of lysophosphatidylcholine |
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| Affiliation: | 1. Lipid Metabolism, Nestlé Research, EPFL Innovation Park, 1015, Switzerland;2. Nestlé Research, EPFL Innovation Park, 1015, Lausanne, Switzerland;3. Eidea Bioscience Ltd., Cambridge, United Kingdom;4. Department of Pediatrics and Department of Health Sciences, Ribeirão Preto Medical School, University of São Paulo, Bandeirantes Avenue, 3900, Ribeirão Preto, 14049-900, Brazil;5. Institute of Clinical Chemistry, Inselspital, Bern University Hospital, Bern, Switzerland;1. Allergy, Immunology and Pediatric Pulmonary Institute, Shamir Medical Center, Zerifin, Israel;2. Department of Pediatrics, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, Israel;1. Finnish Institute of Occupational Health, Helsinki, Finland;2. Fundación Jiménez Díaz, Department of Allergy, Department of Medicine, Universidad Autónoma de Madrid, CIBERES, Instituto Carlos III, Madrid, Spain;1. Newcastle University Translational and Clinical Research Institute, Newcastle upon Tyne, United Kingdom;2. Versus Arthritis Centre for Genetics and Genomics, Centre for Musculoskeletal Research, Institute of Inflammation and Repair, University of Manchester Manchester, United Kingdom;3. NIHR Manchester Musculoskeletal BRC, Manchester University NHS Foundation Trust, Manchester, United Kingdom;4. Bioinformatics Support Unit, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne, United Kingdom;5. Musculoskeletal Services Directorate, Newcastle upon Tyne Hospitals NHS Trust, Newcastle upon Tyne, United Kingdom;6. Newcastle University Biosciences Institute, Newcastle upon Tyne, United Kingdom;1. Population Health Science and Policy, Icahn School of Medicine at Mount Sinai, New York, NY;2. Genetics and Genomics, Icahn School of Medicine at Mount Sinai, New York, NY;3. Pediatrics, Allergy and Immunology, Icahn School of Medicine at Mount Sinai, New York, NY;4. AllerGenis, Hatfield, Pa;5. Department of Pediatrics, Stanford University School of Medicine, Stanford, Calif;6. Department of Pediatrics, Division of Allergy/Immunology, Johns Hopkins University School of Medicine, Baltimore, Md;1. Department of Dermatology, Guangdong Academy of Medical Sciences and Guangdong General Hospital, Guangzhou, Guangdong 510080, PR China;2. Department of General Internal Medicine, The First Affiliated Hospital of Sun Yat-sen University, Guangzhou, Guangdong 510080, PR China;3. Research Center of Intelligent Transportation System, School of Engineering, Sun Yat-sen University, Guangzhou, Guangdong 510275, PR China |
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| Abstract: | Lysophospholipase-transacylase (lysolecithin acylhydrolase, EC 3.1.1.5) from rat lung catalyzes the transfer of acyl groups from lysophosphatidylcholine to either water or another molecule of lysophosphatidylcholine. Studies on the substrate specificity of the purified enzyme showed that a phosphate group in the substrate is essential for enzymatic activity; monoacylglycerol is not hydrolyzed, nor does it serve as an acceptor of acyl groups. The influence of the acyl chain in lysophosphatidylcholine was investigated by using mixtures of differently labelled lysophosphatidylcholine species, or by studying the transfer of [1-14C]Palmitate from [1-14C]palmitoylpropane (1,3)diol-phosphocholine to various 1-acyl-sn-glycero-3-phosphocholines. Lysophosphatidylcholines with acyl chains comprised of ten or more C-atoms were found to serve as acyl acceptors. This finding was used to determine the action of the enzyme on 1-[1-14C]lauroyl- and 1[1-14C]myristoyl-sn-glycero-3-phosphocholine both below and above the critical micelle concentration of the substrate. Monomeric substrate was effectively hydrolyzed, but the transacylase activity of the enzyme was only expressed when substrate micelles were present. Likewise, no transacylase activity was found when lysophosphatidylcholine was embedded in liposomal membranes prepared from lung total lipids. These findings, which persist with crude enzyme preparations (100 000 × g supernatant), are discussed in relation to the putative function of the lysophospholipase-transacylase in the synthesis of disaturated phosphatidylcholine in lung. |
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