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Fig. 20 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana

Fig. 20. Two flavoenzymes involved in ascorbate biosynthesis and maintenance. L-Galactono-1,4-lacton dehydrogenase catalyzes the last step in the Smirnoff-Wheeler pathway to yield ascorbate from L-galactono-1,4-lactone (top). The substrate-derived electrons are passed on to cytochrome c and thus enter the mETC. The detoxification of ROS or ferric iron leads to the generation of the monodehydroascorbate radical (right), which is recycled to ascorbate by the action of monodehydroascorbate dehydrogenase (left-center). For details of the latter reaction see text.

Fig. 44 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana

Fig. 44. Reaction of flavin-containing monooxygenases (clade 3). The seven enzymes characterized so far were all shown to be S-glucosinolate oxidases that catalyze the S-monooxygenation of methylthioalkyl glucosinolates to the corresponding methylsulfinyl glucosinolates (Hansen et al., 2007; Kong et al., 2016; Li et al., 2008). For the nine uncharacterized members a similar catalytic function is hypothesized, but remains to be confirmed.

Fig. 23 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana

Fig. 23. Reaction catalyzed by NDC1/demethylphylloquinone reductase. The penultimate step in the biosynthesis of phylloquinol affords demethylphylloquinol by two-electron reduction of the demetyhlphylloquinone (top reaction). Through nucleophilic attack of the aromatic ring onto the methyl group (in red) of SAM the final methylated product, phylloquinol is formed and S-adenosylhomocysteine (SAH) is released (R = prenyl side chain). (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 24 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana

Fig. 24. Reaction catalyzed by COQ6 in ubiquinone biosynthesis. The FAD-dependent hydroxylation occurs in the 5-position of the aromatic ring as indicated (highlighted in red). COQ6 belongs to the class A FPMOs and depends on NAD(P)H as reductant. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig. 29 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana

Fig. 29. Reaction catalyzed by carotene cis-trans isomerase. The reaction shown requires reduced FAD for the redox-neutral cis-to-trans isomerization at position 9 and 9′ of prolycopene and generates the linear all-trans-lycopene. The reduced FAD is probably generated at the expense of NAD(P)H. Thus, the enzyme appears to possess a second activity that enables the transfer of a hydride from the reduced nicotinamide to the bound FAD cofactor.

Fig. 2 in Multiple free radical scavenging reactions of aurones

Fig. 2. The mechanisms proposed for the radical scavenge reaction of maritimetol (compound 1) in different phases. The arrows in black color indicate the most likely reaction mechanism in the gas and benzene phases. Those in magenda color indicate the most likely reaction mechanism in the water phase. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 1 in Multiple free radical scavenging reactions of aurones

Fig. 1. The most stable structures of the investigated aurones. The atom numberings for the studied compounds are labelled in Maritimetol. The hydrogen-bonds are marked by dashed lines, and the corresponding H⋅⋅⋅O distances are labelled in the optimized geometries.

Fig. 4 in Multiple free radical scavenging reactions of aurones

Fig. 4. The mechanisms proposed for the radical scavenge reaction of sulfuretin (compound 5) in different phases. The arrows in black color indicate the most likely reaction mechanism in the gas and benzene phases. Those in magenda color indicate the most likely reaction mechanism in the water phase. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 47 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana

Fig. 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.

Fig. 33 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana

Fig. 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).

Fig. 28 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana

Fig. 28. Reaction of phytoene dehydrogenase/desaturase. The enzyme introduces two double bonds at position 11 and 11′ and mediates the concomitant trans-to-cis isomerization at position 9 and 9'. Reoxidation of the reduced cofactor is achieved by electron transfer to plastoquinone in the plastid membrane.

Fig. 7 in The scope of flavin-dependent reactions and processes in the model plant Arabidopsis thaliana

Fig. 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.

Fig. 5 in How is the activity of shikimate dehydrogenase from the root of Petroselinum crispum (parsley) regulated and which side reactions are catalyzed?

Fig. 5. Inhibition effect of various phenylpropanoids on the activity of P. crispum SDH. The specific activity of the enzyme preparations was 0.17 ± 0.07 μmol. min-1mg-1. Controls in 96 and 50 % ethanol were only slightly different from the distilled water control, with specific activities of 0.18 0.06 and 0.19 0.11 μmol. ± ± min-1mg-1, respectively. IC was calculated from nonlinear regression with Eq. (1). Each determination was done at least 3-times, the average values and standard 50 deviations are shown.

Fig. 1 in How is the activity of shikimate dehydrogenase from the root of Petroselinum crispum (parsley) regulated and which side reactions are catalyzed?

Fig. 1. Determination of the type of SDH reaction mechanism based on Lineweaver-Burk diagnostical plots for the direction from SA to DHS (A,B) and from DHS to SA (C,D) Double reciprocal plots are fitted to an equation corresponding to a sequential mechanism.

Fig. 2 in How is the activity of shikimate dehydrogenase from the root of Petroselinum crispum (parsley) regulated and which side reactions are catalyzed?

Fig. 2. Product inhibition analysis for the determination of the mechanism of bisubstrate reaction in the direction from SA to DHS (A-F) and in the direction from DHS to SA (G-J). Experimental data are fitted with calculated values determined by non-linear regression using equations charactering competitive and non-competitive inhibition, respectively. SDH products DHS (A,B,C) and NADPH (D,E,F) served as competitive (B,C,D,F) and non-competitive (A,E) inhibitors. The saturating (C,F) and subsaturating (A,B,D,E) concentrations of SA and NADP were 20 mM and 2 mM, and 0.3 mM and 0.5 mM, respectively. Saturating concentrations of NADP and variable concentrations of SA caused no inhibition (N.I.) of NADPH and saturating concentrations of SA and variable concentrations of NADP caused N.I. of DHS (data not shown). SDH products SA (G,H) and NADP (I,J) served as competitive (G,I) and non-competitive (H,J) inhibitors at 0.75 mM (subsaturating concentration) DHS (G,I) and 0.2 mM (subsaturating concentration) NADPH (H,J) as a second substrate. Ki indicates inhibition constants in mM. NC - noncompetitive and C - competitive inhibition. Measurements were performed in doublets (S.D. are shown) and at least 2-4 times (enzyme preparations from different isolations).

Fig. 4 in How is the activity of shikimate dehydrogenase from the root of Petroselinum crispum (parsley) regulated and which side reactions are catalyzed?

Fig. 4. Identification of P. crispum SDH products by reversed-phase liquid chromatography coupled to electrospray mass spectrometry. The symbol ∅ indicates that no potential P. crispum SDH byproduct was identified in the reaction mixtures by mass spectrometry. QDH, quinate dehydrogenase; QD, quinate dehydratase; DHSD, dehydroshikimate dehydratase.

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Ultrahigh Mass Activity Pt Entities Consisting of Pt Single atoms, Clusters, and Nanoparticles for Improved Hydrogen Evolution Reaction

X-ray absorption spectroscopy data in an Athena project file.

opennotspecifiedNov 2020View details →

Fig. 1. Derivatisation reaction conditions for bilocularin A in Synthesis of bilocularin A carbamate derivatives and their evaluation as leucine transport inhibitors in prostate cancer cells

Fig. 1. Derivatisation reaction conditions for bilocularin A (1) and the resulting semi-synthetic carbamate library (2–9).

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A Customized Bayesian Algorithm to Optimize Enzyme-Catalyzed Reactions

Data underlying the figures in the publication "A Customized Bayesian Algorithm to Optimize Enzyme-Catalyzed Reactions" published in ACS Sustain. Chem. Eng., 2023, <a href="https://doi.org/10.1021/acssuschemeng.3c02402">https://doi.org/10.1021/acssuschemeng.3c02402</a>. Table of contents: <ul> <li>sc3c02402_si_001.pdf, sc3c02402_si_002.pdf, sc3c02402_si_003.pdf, sc3c02402_si_004.pdf: DNA sequences, supplementary figures, materials, methods, availability of the program, synthesis protocols</li> <li>sc3c02402_raw_data.zip: Raw data</li> </ul>