Formation of complex ether lipids from 1-O-alkylglycerols in cell suspension cultures of rape |
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Authors: | Nikolaus Weber Helmut K Mangold |
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Institution: | 1. Bundesanstalt für Fettforschung, Institut für Biochemie und Technologie, H.P. Kaufmann Institut, Piusallee 68, D-4400, Münster, Federal Republic of Germany
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Abstract: | Photomixotrophic cell suspension cultures of rape, Brassica napus, were incubated with rac-1-O-1′-14C]hexadecylglycerol. Radioactivity was incorporated predominantly into choline glycerophospholipids. Prolonged incubation led also to considerable proportions of labeled ethanolamine glycerophospholipids. In addition to these ionic lipids,isomeric hexadecylacylglycerols as well as hexadecyldiacylglycerols were formed. About a third of the hexadecylglycerol supplied as substrate was cleaved within 48 h incubation. The palmitic acid formed by oxidative cleavage of the substrate was incorporated predominantly into choline glycerophospholipids, ethanolamine glycerophospholipids, and triacylglycerols. Incubation of an equimolar mixture of homologous saturated rac-1-O-1′14C]alkylglycerols (C14, C16, C18, C20) with rape cells showed that alkylglycerols with alkyl moieties having 16 and 18 carbon atoms were incorporated preferentially. Incubation of labeled hexadecyglycerol with a homogenate of rape cells led also predominantly to choline glycerophospholipids; highest yields were obtained at pH 7. Neither the 1-O-alkyl moieties in choline glycerophospholipis nor those in ethanolamine glycerophospholipids were desaturated to 1-O-alk-1′-enylmoieties. The results of these experiments led to the following conclusions: (1) The acylation of 1-O-alkylglycerols to isomeric alkylacylglycerols is catalyzed by two acyltransferases differing in their specificity with regard to the chain length of the alkyl moiety in the substrate. (2) CDP-Choline: diacylglycerol cholinephosphotransferase and CDP-ethanolamine: diacylglycerol ethanolaminephosphotransferase are two enzymes differing in various respects. Cholinephosphotransferase exhibits a much higher affinity for 1-O-alkyl-2-O-acylglycerols than ethanolaminephosphotransferase. The two enzymes show marked differences with regard to their specificity for 1-O-alkyl-2-O-acylglycerols differing in the chain lengths of their alkyl moieties. |
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