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The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
No full textEggers, Reinmar, Jammer, Alexandra, Jha, Shalinee, Kerschbaumer, Bianca, Lahham, Majd, Strandback, Emilia, Toplak, Marina, Wallner, Silvia, Winkler, Andreas, Macheroux, Peter (2021): The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana. Phytochemistry (112822) 189: 1-42, DOI: 10.1016/j.phytochem.2021.112822, URL: http://dx.doi.org/10.1016/j.phytochem.2021.11282
Fig. 19 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
No full textFig. 19. Reaction catalyzed by squalene epoxidase. The reducing equivalents are delivered by NADPH, and therefore, the enzyme was assigned to subclass A of flavin-dependent monooxygenases (Paul et al., 2021). Similar to zeaxanthine epoxidase the enzyme forms an unusual epoxide (see Fig. 31).Published as part of Eggers, Reinmar, Jammer, Alexandra, Jha, Shalinee, Kerschbaumer, Bianca, Lahham, Majd, Strandback, Emilia, Toplak, Marina, Wallner, Silvia, Winkler, Andreas & Macheroux, Peter, 2021, The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana, pp. 1-42 in Phytochemistry (112822) 189 on page 13, DOI: 10.1016/j.phytochem.2021.112822, http://zenodo.org/record/825945
Fig. 7 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
No full textFig. 7. Reactions catalyzed by isovaleryl-CoA dehydrogenase in valine and isoleucine degradation. Reoxidation of reduced FAD occurs by electron donation to ETF, which in turn feeds the electrons into the mETC via ETF-QO.Published as part of Eggers, Reinmar, Jammer, Alexandra, Jha, Shalinee, Kerschbaumer, Bianca, Lahham, Majd, Strandback, Emilia, Toplak, Marina, Wallner, Silvia, Winkler, Andreas & Macheroux, Peter, 2021, The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana, pp. 1-42 in Phytochemistry (112822) 189 on page 9, DOI: 10.1016/j.phytochem.2021.112822, http://zenodo.org/record/825945
Fig. 46 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
No full textFig. 46. Reactions catalyzed by NADPH oxidases. The two electrons delivered by NADPH are either used for the reduction of dioxygen to hydrogen peroxide (top reaction) or the reduction of two molecules of dioxygen to two molecules of superoxide (bottom reaction).Published as part of Eggers, Reinmar, Jammer, Alexandra, Jha, Shalinee, Kerschbaumer, Bianca, Lahham, Majd, Strandback, Emilia, Toplak, Marina, Wallner, Silvia, Winkler, Andreas & Macheroux, Peter, 2021, The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana, pp. 1-42 in Phytochemistry (112822) 189 on page 25, DOI: 10.1016/j.phytochem.2021.112822, http://zenodo.org/record/825945
Fig. 59 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
No full textFig. 59. Putative reaction catalyzed by HTH (HOTHEAD). Shown are the successive oxidations of the ω-hydroxyl group to the aldehyde and eventually, to the carboxy-group, leading to an α,ω-dicarboxylic acid. Members of the GMC oxidoreductases typically react readily with dioxygen to produce hydrogen peroxide.Published as part of Eggers, Reinmar, Jammer, Alexandra, Jha, Shalinee, Kerschbaumer, Bianca, Lahham, Majd, Strandback, Emilia, Toplak, Marina, Wallner, Silvia, Winkler, Andreas & Macheroux, Peter, 2021, The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana, pp. 1-42 in Phytochemistry (112822) 189 on page 32, DOI: 10.1016/j.phytochem.2021.112822, http://zenodo.org/record/825945
Fig. 47 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
No full textFig. 47. Reaction catalyzed by D-amino acid oxidase. Regeneration of the reduced FAD occurs by dioxygen leading to the production of hydrogen peroxide (top). Note that the direct product of the oxidation, the corresponding imino acid, is non-enzymatically hydrolyzed to yield the α-keto acid and ammonia.Published as part of Eggers, Reinmar, Jammer, Alexandra, Jha, Shalinee, Kerschbaumer, Bianca, Lahham, Majd, Strandback, Emilia, Toplak, Marina, Wallner, Silvia, Winkler, Andreas & Macheroux, Peter, 2021, The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana, pp. 1-42 in Phytochemistry (112822) 189 on page 25, DOI: 10.1016/j.phytochem.2021.112822, http://zenodo.org/record/825945
Fig. 32 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
No full textFig. 32. Last step in abscisic acid biosynthesis catalyzed by abscisic aldehyde oxidase. Note that substrate oxidation occurs at the Moco and electrons are transferred to the FAD cofactor via two iron-sulfur-clusters, i.e. the same reaction mechanism as found in xanthine dehydrogenase. Reoxidation of reduced FAD occurs by dioxygen generating hydrogen peroxide.Published as part of Eggers, Reinmar, Jammer, Alexandra, Jha, Shalinee, Kerschbaumer, Bianca, Lahham, Majd, Strandback, Emilia, Toplak, Marina, Wallner, Silvia, Winkler, Andreas & Macheroux, Peter, 2021, The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana, pp. 1-42 in Phytochemistry (112822) 189 on page 18, DOI: 10.1016/j.phytochem.2021.112822, http://zenodo.org/record/825945
Fig. 37 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
No full textFig. 37. Reaction of cytokinin dehydrogenase. Note that the electron acceptor for the reoxidation of the covalently bound FAD cofactor remains unknown. However, quinones efficiently oxidize the reduced FAD, and thus, are likely candidates as electron acceptors, at least for some of the cytokinin dehydrogenases (Fr´ebortov´a et al., 2004).Published as part of Eggers, Reinmar, Jammer, Alexandra, Jha, Shalinee, Kerschbaumer, Bianca, Lahham, Majd, Strandback, Emilia, Toplak, Marina, Wallner, Silvia, Winkler, Andreas & Macheroux, Peter, 2021, The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana, pp. 1-42 in Phytochemistry (112822) 189 on page 20, DOI: 10.1016/j.phytochem.2021.112822, http://zenodo.org/record/825945
Fig. 33 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
No full textFig. 33. Reaction of flavin-dependent monooxygenases involved in auxin biosynthesis. All enzymes forming clade 2 were shown to play an important role in auxin biosynthesis, as they were identified to mediate the conversion of indole-3-pyruvic acid to indole-3-acetic acid (Dai et al., 2013; Mashiguchi et al., 2011).Published as part of Eggers, Reinmar, Jammer, Alexandra, Jha, Shalinee, Kerschbaumer, Bianca, Lahham, Majd, Strandback, Emilia, Toplak, Marina, Wallner, Silvia, Winkler, Andreas & Macheroux, Peter, 2021, The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana, pp. 1-42 in Phytochemistry (112822) 189 on page 19, DOI: 10.1016/j.phytochem.2021.112822, http://zenodo.org/record/825945
Fig. 5 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana
No full textFig. 5. Reaction of glycerol 3-phosphate dehydrogenase. The secondary alcohol group is oxidized to the keto-group (shown in red) generating dihydroxyacetone phosphate, which is further converted by triose phosphate isomerase, a glycolytic enzyme, to glyceraldehyde 3-phosphate. The reduced FAD is reoxidized by membrane-associated CoQ and thus the electrons enter the mETC. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)Published as part of Eggers, Reinmar, Jammer, Alexandra, Jha, Shalinee, Kerschbaumer, Bianca, Lahham, Majd, Strandback, Emilia, Toplak, Marina, Wallner, Silvia, Winkler, Andreas & Macheroux, Peter, 2021, The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana, pp. 1-42 in Phytochemistry (112822) 189 on page 8, DOI: 10.1016/j.phytochem.2021.112822, http://zenodo.org/record/825945
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