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Wyszukujesz frazę "diadinoxanthin cycle" wg kryterium: Temat


Wyświetlanie 1-2 z 2
Tytuł:
Violaxanthin and diadinoxanthin de-epoxidation in various model lipid systems
Autorzy:
Latowski, Dariusz
Goss, Reimund
Bojko, Monika
Strzałka, Kazimierz
Powiązania:
https://bibliotekanauki.pl/articles/1039787.pdf
Data publikacji:
2012
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
lipids
de-epoxidation
diadinoxanthin cycle
violaxanthin cycle
Opis:
The xanthophyll cycle is an important photoprotective process functioning in plants. One of its forms, the violaxanthin (Vx) cycle, involves interconversion between: Vx, antheraxanthin (Ax) and zeaxanthin (Zx). Another kind of the xanthophyll cycle is the diadinoxanthin (Ddx) cycle in which interconversion between Ddx and diatoxanthin (Dtx) occurs. In this study an information on molecular mechanism and regulation of these two types of the xanthophyll cycle is presented. The influence of lipids on the de-epoxidation of the xanthophyll cycle pigments was investigated, with special focus put on the significance of physical properties of the aggregates formed by inverted lipid micelles, which are necessary for activity of the xanthophyll cycle enzymes. In particular, thickness of the hydrophobic fraction of the aggregates, size of the inverted micelles, suggested by mathematical description of the structures and solubility of Vx and Ddx in various kind of lipids were studied. Obtained results show that the rate of de-epoxidation is strongly dependent on the physicochemical properties of the lipids used. The key role for enzyme activation play non-bilayer lipids and the parameters of inverted micelles such as thickness, fluidity of hydrophobic core and their diameter. The presented results show that MGDG and other non-lamellar lipids like different forms of phosphatidylethanolamine are necessary for the Vx and Ddx de-epoxidation because they provide the three-dimensional structures, which are needed for the binding of de-epoxidases and for the accessibility of Vx and Ddx to these enzymes.
Źródło:
Acta Biochimica Polonica; 2012, 59, 1; 101-103
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Expression of three diadinoxanthin de-epoxidase genes of Phaeodacylum tricornutum in Escherichia coli Origami b and BL21 strain
Autorzy:
Bojko, Monika
Olchawa-Pajor, Monika
Tuleja, Urszula
Kuczyńska, Paulina
Strzałka, Wojciech
Latowski, Dariusz
Strzałka, Kazimierz
Powiązania:
https://bibliotekanauki.pl/articles/1039507.pdf
Data publikacji:
2013
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
diadinoxanthin cycle
marine diatoms
violaxanthin
de-epoxidation
Opis:
In the diadinoxanthin cycle the epoxy group is removed from diadinoxanthin and diatoxanthin is created. This conversion takes place e.g. in diatoms with the involvement of the enzyme diadinoxanthin de-epoxidase. In one of the diatom species, Phaeodactylum tricornutum (CCAP 1055/1 strain with genome sequenced) three de-epoxidase genes (PtVDE, PtVDL1, PtVDL2) have been identified, but only one of them (PtVDE) corresponds to violaxanthin de-epoxidase, an enzyme which is commonly found in higher plants. In these studies, the expression of two de-epoxidase genes of another Phaeodactylum tricornutum strain (UTEX 646), which is commonly used in diatom studies, were obtained in Origami b and BL21 E. coli strains. The molecular masses of the mature proteins are about 49 kDa and 60 kDa, respectively, for VDE and VDL2. Both enzymes are active with violaxanthin as a substrate.
Źródło:
Acta Biochimica Polonica; 2013, 60, 4; 857-860
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-2 z 2

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