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  • 1
    Online Resource
    Online Resource
    Trihydroxyacylglycerinsynthese in transgenem Raps : Abschlussbericht zum Forschungsvorhaben ; Berichtszeitraum: Januar 1999 bis März 2003 (2003)
    Aachen : RWTH, Inst. für Biologie I, Spezielle Botanik
    Details Availability
    Keywords: Forschungsbericht
    Type of Medium: Online Resource
    Pages: Online-Ressource (16 S., 115 KB) , graph. Darst
    URL: https://edocs.tib.eu/files/e01fb05/487658280.pdf
    URL: https://doi.org/10.2314/GBV:487658280
    URL: https://edocs.tib.eu/files/e01fb05/487658280l.pdf
    DOI: 10.2314/GBV:487658280
    Language: German
    Note: Literaturangaben. - Förderkennzeichen BMVEL 97NR108/22010897 , Unterschiede zwischen dem gedruckten Dokument und der elektronischen Ressource können nicht ausgeschlossen werden , Auch als gedr. Ausg. vorh , Systemvoraussetzungen: Acrobat reader.
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  • 2
    Electronic Resource
    Electronic Resource
    Role of plastidial acyl-acyl carrier protein: Glycerol 3-phosphate acyltransferase and acyl-acyl carrier protein hydrolase in channelling the acyl flux through the prokaryotic and eukaryotic pathway (1988)
    Springer
    Planta 176 (1988), S. 506-512 
    Details
    ISSN: 1432-2048
    Keywords: Acyl-acyl carrier protein:glycerol 3-phosphate acyltransferase ; Acyl-acyl carrier protein hydrolase ; Eukaryotic pathway (acyl flux) ; Prokaryotic pathway (acyl flux)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In order to investigate whether the relative activities of the plastidial acyl-acyl carrier protein (ACP):glycerol 3-phosphate acyltransferase (EC 2.3.1.15) and acyl-ACP hydrolase play a role in controlling the acyl flux through the prokaryotic and eukaryotic pathway, we determined these enzymic activities in stroma fractions from 16:3- and 18:3-plants using glycerol 3-phosphate and labelled acyl-ACP as substrates. Several factors were examined which might influence the activities within plastids, such as leaf development, salts at physiological concentrations, stroma pH and substrates available to the enzymes. An appreciable alteration of the two enzymic activities was only observed with changes in the pH and substrate concentration, especially the concentration of glycerol 3-phosphate. An increase in pH from 7 to 8 resulted in a decreased ratio of acyltransferase versus hydrolase activity in stroma fractions from both pea (Pisum sativum L.) and spinach (Spinacia oleracea L.), whereas exogenously added glycerol 3-phosphate, which only influenced the acyltransferase, raised this ratio. On the other hand, the relative activities of the two enzymes stayed rather constant at oleoyl-ACP concentrations between 1 and 2 μM not only when it was offered alone but also in a mixture with palmitoyl-ACP. At pH 8, the stroma pH of illuminated chloroplasts, and at physiologically relevant substrate concentrations we observed clear differences between the 16:3-plants spinach and mustard (Sinapis alba ssp. alba L.) and the 18:3-plants pea and maize (Zea mays L.). In accordance with the different proportions of prokaryotic glycerolipids in the two groups of plants, pea and maize showed distinctly lower ratios of acyltransferase versus hydrolase activity than spinach and mustard. Consequently the relative activities of the plastidial glycerol 3-phosphate acyltransferase and acyl-ACP hydrolase can play a decisive role in controlling the acyl flux through the different pathways at least in these plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00397657
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  • 3
    Electronic Resource
    Electronic Resource
    Triacylglycerol biosynthesis in developing seeds of Tropaeolum majus L. and Limnanthes douglasii R. Br. (1992)
    Springer
    Planta 188 (1992), S. 215-224 
    Details
    ISSN: 1432-2048
    Keywords: 1-Acylglycerol-3-phosphate acyltransferase ; Glycerol-3-phosphate acyltransferase ; Erucic acid ; Limnanthes ; Triacylglycerol ; Tropaeolum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Triacylglycerols of both Tropaeolum majus L. and Limnanthes douglasii R. Br. are predominantly esterified with very long-chain acyl groups at each position of the glycerol backbone. In order to elucidate whether these acyl groups are directly chanelled into the triacylglycerols via the stepwise acylation of glycerol-3-phosphate, seed oil formation has been investigated in developing embryos of both plant species. [1-14C]Acetate labelling experiments using embryos at different stages of development, as well as the determination of the properties of the microsomal acyl-CoA:sn-glycerol-3-phosphate acyltransferase (EC 2.3.1.15) and acyl-CoA:sn-1-acylglycerol-3-phosphate acyltransferase (EC 2.3.1.51), revealed differences between the two plant species, especially with respect to the incorporation of very longchain acyl groups into the C2 position of the triacylglycerols. In microsomal fractions of developing embryos of L. douglasii both a glycerol-3-phosphate and a 1-acylglycerol-3-phosphate acyltransferase were detected which utilize very long-chain acyl-CoA thioesters as substrates. Thus, in seeds of L. douglasii very long-chain acyl groups can enter not only the C1, but also the C2 position of the triacylglycerols in the course of de-novo biosynthesis. A comparison of the properties of the acyltransferases of developing embryos with those of the corresponding activities of leaves indicates an embryo specific expression of an erucoyl-CoA-dependent microsomal 1-acylglycerol-3-phosphate acyltransferase in L. douglasii. The microsomal glycerol-3-phosphate acyltransferase of developing embryos of T. majus displayed properties very similar to those of the corresponding activity of L. douglasii. On the other hand, the microsomal 1-acylglycerol-3-phosphate acyltransferases of the two plant species showed strikingly different substrate specificities. Irrespective of the acyl groups of 1-acylglycerol-3-phosphate and regardless of whether acyl-CoA thioesters were offered separately or in mixtures, the enzyme of T. majus, in contrast to that of L. douglasii, was inactive with erucoyl-CoA. These results of the enzyme studies correspond well with those of the [1-14C]acetate labelling experiments and thus indicate that T. majus has developed mechanisms different from those of L. douglasii for the incorporation of erucic acid into the C2 position of its triacylglycerols.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00216816
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  • 4
    Electronic Resource
    Electronic Resource
    Purification and cDNA sequencing of an oleate-selective acyl-ACP:sn-glycerol-3-phosphate acyltransferase from pea chloroplasts (1991)
    Springer
    Plant molecular biology 17 (1991), S. 1067-1076 
    Details
    ISSN: 1573-5028
    Keywords: chilling sensitivity ; glycerolipid biosynthesis ; immunoscreening ; Pisum sativum ; tryptic sequences ; transit peptide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The soluble acyl-ACP:sn-glycerol-3-phosphate acyltransferase from chloroplasts of chilling-sensitive and -resistant plants differ in their fatty acid selectivity. Enzymes from resistant plants discriminate against non-fluid palmitic acid and select oleic acid whereas the acyltransferase from sensitive plants accepts both fatty acids. To use this difference for improving plant chilling resistance by biotechnology the gene for an oleate-selective enzyme is required. Therefore, the oleate-selective enzyme from pea seedlings was purified to apparent homogeneity. Tryptic peptides of internal origin were sequenced. Polyclonal antibodies raised in rabbits were used for an immunological screening of a pea leaf cDNA expression library in λgt11. A positive clone of 1800 bp was selected showing an open reading frame which codes for 457 amino acids. The deduced amino acid sequence coincides perfectly with the tryptic sequences. A tentative assignment of the processing site was made which divides the preprotein into a mature protein of 41 kDa in accordance with experimental findings and a transit peptide of 88 amino acids. At present the comparison between a selective (pea) and an unselective (squash) acyltransferase sequence does not provide a clue for recognizing the structural differences resulting in different selectivities.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00037145
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  • 5
    Electronic Resource
    Electronic Resource
    Substrate specificities of the membrane-bound and partially purified microsomal acyl-CoA:1-acylglycerol-3-phosphate acyltransferase from etiolated shoots of Pisum sativum (L.) (1991)
    Springer
    Planta 185 (1991), S. 124-131 
    Details
    ISSN: 1432-2048
    Keywords: Acyl-CoA:1-acylglycerol-3-phosphate acyl-transferase ; Endoplasmic reticulum ; Eukaryotic fatty acid pattern ; Membrane protein purification ; Pisum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Membrane fractions enriched in rough endoplasmic reticulum and not contaminated with plastidial membranes were isolated from etiolated shoots of Pisum sativum (L.). From these fractions the acyl-CoA:1-acyl-sn-glycerol-3-phosphate acyltransferase (EC 2.3.1.51) was solubilized by extracting the membranes with the zwitterionic detergent 3-[(3-cholamidopropyl)-dimethyl-ammonio]-1-propanesulfonate at high ionic strength. The subsequent separation of the solubilized fractions on a Mono Q column resulted in a tenfold enriched enzymic activity, which could be stabilized by polyethyleneglycol precipitation. A comparison of the substrate specificities and selectivities of the solubilized, enriched 1-acylglycerol-3-phosphate acyltransferase and the corresponding membrane-bound activity revealed no appreciable difference. Both enzymic forms specifically utilized acyl-CoA thioesters as acyl donors whereas the corresponding acyl-acyl carrier protein thioesters were not used. Furthermore, the membrane-bound as well as the solubilized enriched form showed not only higher activities with 1-oleoylthan with 1-palmitoylglycerol-3-phosphate but also pronounced specificities and selectivities for unsaturated C18-CoA thioesters. Hence, the extraplastidial 1-acylglycerol-3-phosphate acyltransferase which catalyses the formation of phosphatidic acid with an eukaryotic fatty-acid pattern was partially purified.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00194523
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  • 6
    Electronic Resource
    Electronic Resource
    sn-1-Acylglycerol-3-phosphate acyltransferase of Escherichia coli causes insertion of cis-11 eicosenoic acid into the sn-2 position of transgenic rapeseed oil (1998)
    Springer
    Molecular breeding 4 (1998), S. 39-46 
    Details
    ISSN: 1572-9788
    Keywords: sn-1-acylglycerol-3-phosphate acyltransferase ; Brassica napus ; cis-11 eicosenoic acid ; Escherichia coli ; triacylglycerol
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract The plsC gene of Escherichia coli encoding sn-1-acylglycerol-3-phosphate acyltransferase was modified by inserting an endoplasmic reticulum retrieval signal to its 3′ end and introduced into rapeseed (Brassica napus L.) plants under the control of a napin promotor. In developing seeds from transgenic plants an sn-1-acylglycerol-3-phosphate acyltransferase activity was detectable which showed substrate specificities typical of the E. coli enzyme. Moreover, seed oil from the transformants unlike that from untransformed plants contained substantial amounts of triacylglycerol species esterified with very-long-chain fatty acids at each glycerol position. Analysis of fatty acids at the sn-2 position of triacylglycerol showed hardly any very-long-chain fatty acids in untransformed plants, but in certain transformants these fatty acids were present, namely about 4% erucic acid and 9% eicosenoic acid. These data demonstrate that the bacterial acyltransferase can function in developing rapeseed and alters the stereochemical composition of transgenic rape seed oil by directing very-long-chain fatty acids, especially cis-11 eicosenoic acid, to its sn-2 position.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009615229344
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  • 7
    Electronic Resource
    Electronic Resource
    Membranlipid-Biosynthese in Chloroplasten (1983)
    Weinheim : Wiley-Blackwell
    Biologie in unserer Zeit 13 (1983), S. 178-187 
    Details
    ISSN: 0045-205X
    Keywords: Life and Medical Sciences
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/biuz.19830130607
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