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efv metabolites h941830  (Toronto Research Chemicals)


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    Toronto Research Chemicals efv metabolites h941830
    Computational models of <t>(S)-EFV</t> (A) and L-Glu (B) binding to the allosteric sites on CYP46A1, showing some of the amino acid residues involved in the interaction with these compounds. The loop (from G417 to T426) separating the two allosteric sites is also shown and colored in magenta. The nitrogen, oxygen, chlorine, and fluorine atoms are in blue, red, light green, and cyan, respectively. The allosteric site mapping and compound docking were carried out in our previous work (Anderson et al., 2016; Mast et al., 2017a, 2020).
    Efv Metabolites H941830, supplied by Toronto Research Chemicals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/efv metabolites h941830/product/Toronto Research Chemicals
    Average 90 stars, based on 1 article reviews
    efv metabolites h941830 - by Bioz Stars, 2026-02
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    1) Product Images from "The Hydroxylation Position Rather than Chirality Determines How Efavirenz Metabolites Activate Cytochrome P450 46A1 In Vitro"

    Article Title: The Hydroxylation Position Rather than Chirality Determines How Efavirenz Metabolites Activate Cytochrome P450 46A1 In Vitro

    Journal: Drug Metabolism and Disposition

    doi: 10.1124/dmd.122.000874

    Computational models of (S)-EFV (A) and L-Glu (B) binding to the allosteric sites on CYP46A1, showing some of the amino acid residues involved in the interaction with these compounds. The loop (from G417 to T426) separating the two allosteric sites is also shown and colored in magenta. The nitrogen, oxygen, chlorine, and fluorine atoms are in blue, red, light green, and cyan, respectively. The allosteric site mapping and compound docking were carried out in our previous work (Anderson et al., 2016; Mast et al., 2017a, 2020).
    Figure Legend Snippet: Computational models of (S)-EFV (A) and L-Glu (B) binding to the allosteric sites on CYP46A1, showing some of the amino acid residues involved in the interaction with these compounds. The loop (from G417 to T426) separating the two allosteric sites is also shown and colored in magenta. The nitrogen, oxygen, chlorine, and fluorine atoms are in blue, red, light green, and cyan, respectively. The allosteric site mapping and compound docking were carried out in our previous work (Anderson et al., 2016; Mast et al., 2017a, 2020).

    Techniques Used: Binding Assay

    Phase 1 metabolic products of (S)-EFV generated by cytochrome P450 enzymes as suggested by previous studies (Avery et al., 2013b). The major P450s metabolizing (S)-EFV are shown in bold.
    Figure Legend Snippet: Phase 1 metabolic products of (S)-EFV generated by cytochrome P450 enzymes as suggested by previous studies (Avery et al., 2013b). The major P450s metabolizing (S)-EFV are shown in bold.

    Techniques Used: Generated

    Dependence of in vitro activation of CYP46A1 on the concentration of EFV (A), its mono- (B) and dihydroxylated (C) metabolites. The Y-axis is identical for all three graphs and represents CYP46A1 activity as nanomoles of 24-hydoxycholsterol (24HC) formed per nmole of CYP46A1 per minute. The results are the mean ±S.D. of the measurements from the three independent experiments. Statistically significant differences between (S)-EFV versus (R)-EFV were assessed by two-way ANOVA with Bonferroni multiple comparisons. No significant differences were found between the (S) enantiomer versus racemate of the same EFV metabolite * P ≤ 0.05.
    Figure Legend Snippet: Dependence of in vitro activation of CYP46A1 on the concentration of EFV (A), its mono- (B) and dihydroxylated (C) metabolites. The Y-axis is identical for all three graphs and represents CYP46A1 activity as nanomoles of 24-hydoxycholsterol (24HC) formed per nmole of CYP46A1 per minute. The results are the mean ±S.D. of the measurements from the three independent experiments. Statistically significant differences between (S)-EFV versus (R)-EFV were assessed by two-way ANOVA with Bonferroni multiple comparisons. No significant differences were found between the (S) enantiomer versus racemate of the same EFV metabolite * P ≤ 0.05.

    Techniques Used: In Vitro, Activation Assay, Concentration Assay, Activity Assay

    Effect of the allosteric site mutations on basal CYP46A1 activity and enzyme activation by L-Glu, EFV, and EFV metabolites. CYP46A1 activity is presented as nanomoles of 24-hydoxycholsterol (24HC) formed per nmole of CYP46A1 per minute. The results are the mean ±S.D. of the measurements from the three independent experiments. Statistically significant differences were assessed by one-way ANOVA with Tuckey multiple comparisons versus basal activity of WT or the CYP46A1 mutant. ** P ≤ 0.01; *** P ≤ 0.001.
    Figure Legend Snippet: Effect of the allosteric site mutations on basal CYP46A1 activity and enzyme activation by L-Glu, EFV, and EFV metabolites. CYP46A1 activity is presented as nanomoles of 24-hydoxycholsterol (24HC) formed per nmole of CYP46A1 per minute. The results are the mean ±S.D. of the measurements from the three independent experiments. Statistically significant differences were assessed by one-way ANOVA with Tuckey multiple comparisons versus basal activity of WT or the CYP46A1 mutant. ** P ≤ 0.01; *** P ≤ 0.001.

    Techniques Used: Activity Assay, Activation Assay, Mutagenesis

    A summary of compound activation and binding to purified CYP46A1
    Figure Legend Snippet: A summary of compound activation and binding to purified CYP46A1

    Techniques Used: Activation Assay, Binding Assay, Purification

    Effect of L-Glu or (S)-EFV on CYP46A1 activation by EFV metabolites. CYP46A1 activity is presented as nanomoles of 24-hydoxycholsterol (24HC) formed per nmole of CYP46A1 per minute. The results are the mean ±S.D. of the measurements from the three independent experiments. Statistically significant differences were assessed by one-way ANOVA with Tuckey multiple comparisons versus CYP46A1 activity when only compound in question was present. *** P ≤ 0.001.
    Figure Legend Snippet: Effect of L-Glu or (S)-EFV on CYP46A1 activation by EFV metabolites. CYP46A1 activity is presented as nanomoles of 24-hydoxycholsterol (24HC) formed per nmole of CYP46A1 per minute. The results are the mean ±S.D. of the measurements from the three independent experiments. Statistically significant differences were assessed by one-way ANOVA with Tuckey multiple comparisons versus CYP46A1 activity when only compound in question was present. *** P ≤ 0.001.

    Techniques Used: Activation Assay, Activity Assay

    Spectral titrations of substrate-free CYP46A1 (A) and cholesterol-bound CYP46A1 (B) by EFV and some of its metabolites. Fit of spectral changes (ΔA, the amplitude of spectral response in the CYP46A1 difference spectrum) either to a hyperbolic equation or to the Hill equation, when cooperative binding was observed, is shown on the left, and the spectral response type in the CYP46A1 difference spectrum is shown on the right. The results are the mean ±S.D. of the measurements from the three independent titrations. Data for (S)-EFV are taken from (Mast et al., 2020).
    Figure Legend Snippet: Spectral titrations of substrate-free CYP46A1 (A) and cholesterol-bound CYP46A1 (B) by EFV and some of its metabolites. Fit of spectral changes (ΔA, the amplitude of spectral response in the CYP46A1 difference spectrum) either to a hyperbolic equation or to the Hill equation, when cooperative binding was observed, is shown on the left, and the spectral response type in the CYP46A1 difference spectrum is shown on the right. The results are the mean ±S.D. of the measurements from the three independent titrations. Data for (S)-EFV are taken from (Mast et al., 2020).

    Techniques Used: Binding Assay



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    Computational models of <t>(S)-EFV</t> (A) and L-Glu (B) binding to the allosteric sites on CYP46A1, showing some of the amino acid residues involved in the interaction with these compounds. The loop (from G417 to T426) separating the two allosteric sites is also shown and colored in magenta. The nitrogen, oxygen, chlorine, and fluorine atoms are in blue, red, light green, and cyan, respectively. The allosteric site mapping and compound docking were carried out in our previous work (Anderson et al., 2016; Mast et al., 2017a, 2020).
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    Image Search Results


    Computational models of (S)-EFV (A) and L-Glu (B) binding to the allosteric sites on CYP46A1, showing some of the amino acid residues involved in the interaction with these compounds. The loop (from G417 to T426) separating the two allosteric sites is also shown and colored in magenta. The nitrogen, oxygen, chlorine, and fluorine atoms are in blue, red, light green, and cyan, respectively. The allosteric site mapping and compound docking were carried out in our previous work (Anderson et al., 2016; Mast et al., 2017a, 2020).

    Journal: Drug Metabolism and Disposition

    Article Title: The Hydroxylation Position Rather than Chirality Determines How Efavirenz Metabolites Activate Cytochrome P450 46A1 In Vitro

    doi: 10.1124/dmd.122.000874

    Figure Lengend Snippet: Computational models of (S)-EFV (A) and L-Glu (B) binding to the allosteric sites on CYP46A1, showing some of the amino acid residues involved in the interaction with these compounds. The loop (from G417 to T426) separating the two allosteric sites is also shown and colored in magenta. The nitrogen, oxygen, chlorine, and fluorine atoms are in blue, red, light green, and cyan, respectively. The allosteric site mapping and compound docking were carried out in our previous work (Anderson et al., 2016; Mast et al., 2017a, 2020).

    Article Snippet: All EFV metabolites were obtained from Toronto Research Chemicals (H805345, H941820, H941830, H941825, D452979, D46250 , D468240, D452800).

    Techniques: Binding Assay

    Phase 1 metabolic products of (S)-EFV generated by cytochrome P450 enzymes as suggested by previous studies (Avery et al., 2013b). The major P450s metabolizing (S)-EFV are shown in bold.

    Journal: Drug Metabolism and Disposition

    Article Title: The Hydroxylation Position Rather than Chirality Determines How Efavirenz Metabolites Activate Cytochrome P450 46A1 In Vitro

    doi: 10.1124/dmd.122.000874

    Figure Lengend Snippet: Phase 1 metabolic products of (S)-EFV generated by cytochrome P450 enzymes as suggested by previous studies (Avery et al., 2013b). The major P450s metabolizing (S)-EFV are shown in bold.

    Article Snippet: All EFV metabolites were obtained from Toronto Research Chemicals (H805345, H941820, H941830, H941825, D452979, D46250 , D468240, D452800).

    Techniques: Generated

    Dependence of in vitro activation of CYP46A1 on the concentration of EFV (A), its mono- (B) and dihydroxylated (C) metabolites. The Y-axis is identical for all three graphs and represents CYP46A1 activity as nanomoles of 24-hydoxycholsterol (24HC) formed per nmole of CYP46A1 per minute. The results are the mean ±S.D. of the measurements from the three independent experiments. Statistically significant differences between (S)-EFV versus (R)-EFV were assessed by two-way ANOVA with Bonferroni multiple comparisons. No significant differences were found between the (S) enantiomer versus racemate of the same EFV metabolite * P ≤ 0.05.

    Journal: Drug Metabolism and Disposition

    Article Title: The Hydroxylation Position Rather than Chirality Determines How Efavirenz Metabolites Activate Cytochrome P450 46A1 In Vitro

    doi: 10.1124/dmd.122.000874

    Figure Lengend Snippet: Dependence of in vitro activation of CYP46A1 on the concentration of EFV (A), its mono- (B) and dihydroxylated (C) metabolites. The Y-axis is identical for all three graphs and represents CYP46A1 activity as nanomoles of 24-hydoxycholsterol (24HC) formed per nmole of CYP46A1 per minute. The results are the mean ±S.D. of the measurements from the three independent experiments. Statistically significant differences between (S)-EFV versus (R)-EFV were assessed by two-way ANOVA with Bonferroni multiple comparisons. No significant differences were found between the (S) enantiomer versus racemate of the same EFV metabolite * P ≤ 0.05.

    Article Snippet: All EFV metabolites were obtained from Toronto Research Chemicals (H805345, H941820, H941830, H941825, D452979, D46250 , D468240, D452800).

    Techniques: In Vitro, Activation Assay, Concentration Assay, Activity Assay

    Effect of the allosteric site mutations on basal CYP46A1 activity and enzyme activation by L-Glu, EFV, and EFV metabolites. CYP46A1 activity is presented as nanomoles of 24-hydoxycholsterol (24HC) formed per nmole of CYP46A1 per minute. The results are the mean ±S.D. of the measurements from the three independent experiments. Statistically significant differences were assessed by one-way ANOVA with Tuckey multiple comparisons versus basal activity of WT or the CYP46A1 mutant. ** P ≤ 0.01; *** P ≤ 0.001.

    Journal: Drug Metabolism and Disposition

    Article Title: The Hydroxylation Position Rather than Chirality Determines How Efavirenz Metabolites Activate Cytochrome P450 46A1 In Vitro

    doi: 10.1124/dmd.122.000874

    Figure Lengend Snippet: Effect of the allosteric site mutations on basal CYP46A1 activity and enzyme activation by L-Glu, EFV, and EFV metabolites. CYP46A1 activity is presented as nanomoles of 24-hydoxycholsterol (24HC) formed per nmole of CYP46A1 per minute. The results are the mean ±S.D. of the measurements from the three independent experiments. Statistically significant differences were assessed by one-way ANOVA with Tuckey multiple comparisons versus basal activity of WT or the CYP46A1 mutant. ** P ≤ 0.01; *** P ≤ 0.001.

    Article Snippet: All EFV metabolites were obtained from Toronto Research Chemicals (H805345, H941820, H941830, H941825, D452979, D46250 , D468240, D452800).

    Techniques: Activity Assay, Activation Assay, Mutagenesis

    A summary of compound activation and binding to purified CYP46A1

    Journal: Drug Metabolism and Disposition

    Article Title: The Hydroxylation Position Rather than Chirality Determines How Efavirenz Metabolites Activate Cytochrome P450 46A1 In Vitro

    doi: 10.1124/dmd.122.000874

    Figure Lengend Snippet: A summary of compound activation and binding to purified CYP46A1

    Article Snippet: All EFV metabolites were obtained from Toronto Research Chemicals (H805345, H941820, H941830, H941825, D452979, D46250 , D468240, D452800).

    Techniques: Activation Assay, Binding Assay, Purification

    Effect of L-Glu or (S)-EFV on CYP46A1 activation by EFV metabolites. CYP46A1 activity is presented as nanomoles of 24-hydoxycholsterol (24HC) formed per nmole of CYP46A1 per minute. The results are the mean ±S.D. of the measurements from the three independent experiments. Statistically significant differences were assessed by one-way ANOVA with Tuckey multiple comparisons versus CYP46A1 activity when only compound in question was present. *** P ≤ 0.001.

    Journal: Drug Metabolism and Disposition

    Article Title: The Hydroxylation Position Rather than Chirality Determines How Efavirenz Metabolites Activate Cytochrome P450 46A1 In Vitro

    doi: 10.1124/dmd.122.000874

    Figure Lengend Snippet: Effect of L-Glu or (S)-EFV on CYP46A1 activation by EFV metabolites. CYP46A1 activity is presented as nanomoles of 24-hydoxycholsterol (24HC) formed per nmole of CYP46A1 per minute. The results are the mean ±S.D. of the measurements from the three independent experiments. Statistically significant differences were assessed by one-way ANOVA with Tuckey multiple comparisons versus CYP46A1 activity when only compound in question was present. *** P ≤ 0.001.

    Article Snippet: All EFV metabolites were obtained from Toronto Research Chemicals (H805345, H941820, H941830, H941825, D452979, D46250 , D468240, D452800).

    Techniques: Activation Assay, Activity Assay

    Spectral titrations of substrate-free CYP46A1 (A) and cholesterol-bound CYP46A1 (B) by EFV and some of its metabolites. Fit of spectral changes (ΔA, the amplitude of spectral response in the CYP46A1 difference spectrum) either to a hyperbolic equation or to the Hill equation, when cooperative binding was observed, is shown on the left, and the spectral response type in the CYP46A1 difference spectrum is shown on the right. The results are the mean ±S.D. of the measurements from the three independent titrations. Data for (S)-EFV are taken from (Mast et al., 2020).

    Journal: Drug Metabolism and Disposition

    Article Title: The Hydroxylation Position Rather than Chirality Determines How Efavirenz Metabolites Activate Cytochrome P450 46A1 In Vitro

    doi: 10.1124/dmd.122.000874

    Figure Lengend Snippet: Spectral titrations of substrate-free CYP46A1 (A) and cholesterol-bound CYP46A1 (B) by EFV and some of its metabolites. Fit of spectral changes (ΔA, the amplitude of spectral response in the CYP46A1 difference spectrum) either to a hyperbolic equation or to the Hill equation, when cooperative binding was observed, is shown on the left, and the spectral response type in the CYP46A1 difference spectrum is shown on the right. The results are the mean ±S.D. of the measurements from the three independent titrations. Data for (S)-EFV are taken from (Mast et al., 2020).

    Article Snippet: All EFV metabolites were obtained from Toronto Research Chemicals (H805345, H941820, H941830, H941825, D452979, D46250 , D468240, D452800).

    Techniques: Binding Assay