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| Verfasst von: | Pilati, Stefania [VerfasserIn]  |
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| | Wild, Klemens [VerfasserIn] |
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| | Gumiero, Andrea [VerfasserIn] |
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| | Holdermann, Iris Valerie [VerfasserIn] |
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| | Hackmann, Yvonne [VerfasserIn] |
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| | Serra, Mauro Dalla [VerfasserIn] |
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| | Guella, Graziano [VerfasserIn] |
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| | Moser, Claudio [VerfasserIn] |
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| | Sinning, Irmgard [VerfasserIn] |
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| Titel: | Vitis vinifera lipoxygenase LoxA is an allosteric dimer activated by lipidic surfaces |
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| Verf.angabe: | Stefania Pilati, Klemens Wild, Andrea Gumiero, Iris Holdermann, Yvonne Hackmann, Mauro Dalla Serra, Graziano Guella, Claudio Moser, Irmgard Sinning |
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| E-Jahr: | 2024 |
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| Jahr: | 15 November 2024 |
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| Umfang: | 18 S. |
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| Illustrationen: | Illustrationen, Diagramme |
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| Fussnoten: | Gesehen am 25.06.2025 |
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| Titel Quelle: | Enthalten in: Journal of molecular biology |
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| Ort Quelle: | Amsterdam [u.a.] : Elsevier, 1959 |
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| Jahr Quelle: | 2024 |
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| Band/Heft Quelle: | 436(2024), 22 vom: Nov., Artikel-ID 168821, Seite [1]-18 |
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| ISSN Quelle: | 1089-8638 |
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| Abstract: | Lipoxygenases catalyze the peroxidation of poly-unsaturated fatty acid chains either free or esterified in membrane lipids. Vitis vinifera LoxA is transcriptionally induced at ripening onset and localizes at the inner chloroplast membrane where it is responsible for galactolipid regiospecific mono- and di-peroxidation. Here we present a kinetic and structural characterization of LoxA. Our X-ray structures reveal a constitutive dimer with detergent induced conformational changes affecting substrate binding and catalysis. In a closed conformation, a LID domain prevents substrate access to the catalytic site by steric hindrance. Detergent addition above the CMC destabilizes the LID and opens the dimer with both catalytic sites accessible from the same surface framed by the PLAT domains. As a consequence, detergent molecules occupy allosteric sites in the PLAT/catalytic domain interface. These structural changes are mirrored by increased enzymatic activity and positive cooperativity when the substrate is provided in micelles. The ability to interact with micelles is lost upon dimer destabilization by site-directed mutagenesis as assessed by tryptophan fluorescence. Our data allow to propose a model for protein activation at the membrane, classifying LoxA as an interfacial enzyme acting on fatty acid chains directly from the membrane similar to mammalian 15-LOX and 5-LOX. |
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| DOI: | doi:10.1016/j.jmb.2024.168821 |
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| URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
kostenfrei: Volltext: https://doi.org/10.1016/j.jmb.2024.168821 |
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| | kostenfrei: Volltext: https://www.sciencedirect.com/science/article/pii/S0022283624004431 |
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| | DOI: https://doi.org/10.1016/j.jmb.2024.168821 |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| Sach-SW: | (grapevine) |
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| | allosteric enzyme |
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| | crystal structure |
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| | interfacial activation |
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| | lipid peroxidation |
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| | lipoxygenase (LOX) |
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| K10plus-PPN: | 1929075588 |
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| Verknüpfungen: | → Zeitschrift |
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Vitis vinifera lipoxygenase LoxA is an allosteric dimer activated by lipidic surfaces / Pilati, Stefania [VerfasserIn]; 15 November 2024 (Online-Ressource)
