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  • 95
    Millipore acetyl coa
    Acetyl Coa, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 1624 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore coenzyme a
    Substrate binding and conformational changes of the central β hairpin and C extension. ( A ) Details of <t>xEco2-K105-CoA</t> interaction showing substrate hairpin (yellow) coordinated by the C extension (red) in form of a β sheet. ( B ) Conserved surface rendition of K105-CoA bound to xEco2. ( C ) Details of xEco2-K106-CoA interaction showing substrate peptide (yellow) coordinated by the central β hairpin (orange) in form of a β sheet. ( D ) Conserved surface rendition of K106-CoA bound to xEco2. ( E ) Superimposition of peptide-free (red), K105-CoA (green), and K106-CoA (salmon) bound xEco2 structures showing occupation of and displacement of W623 from the central hydrophobic pocket. ( F ) Superimposition of the C extension in peptide-free (red), K105-CoA (green), and K106-CoA (salmon) bound conformations. The C extension shows a 180° flip from coordinating W623 at the hydrophobic pocket to an open conformation upon K106-CoA binding.
    Coenzyme A, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 460 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Cell Signaling Technology Inc acetyl coa carboxylase acc
    Substrate binding and conformational changes of the central β hairpin and C extension. ( A ) Details of <t>xEco2-K105-CoA</t> interaction showing substrate hairpin (yellow) coordinated by the C extension (red) in form of a β sheet. ( B ) Conserved surface rendition of K105-CoA bound to xEco2. ( C ) Details of xEco2-K106-CoA interaction showing substrate peptide (yellow) coordinated by the central β hairpin (orange) in form of a β sheet. ( D ) Conserved surface rendition of K106-CoA bound to xEco2. ( E ) Superimposition of peptide-free (red), K105-CoA (green), and K106-CoA (salmon) bound xEco2 structures showing occupation of and displacement of W623 from the central hydrophobic pocket. ( F ) Superimposition of the C extension in peptide-free (red), K105-CoA (green), and K106-CoA (salmon) bound conformations. The C extension shows a 180° flip from coordinating W623 at the hydrophobic pocket to an open conformation upon K106-CoA binding.
    Acetyl Coa Carboxylase Acc, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 564 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Cell Signaling Technology Inc acetyl coa carboxylase
    Molecular characterization of hepatocellular carcinomas developed in sgPten/c-Met mice. ( a ) Levels of activation of AKT/mTOR and Ras/MAPK pathways in wild-type (WT) and sgPten/c-Met mouse livers, as detected by western blot analysis. Representative blots are shown. GAPDH and β-actin were used as loading controls. ( b ) Immunohistochemical staining of WT and sgPten/c-Met mouse livers. Original magnifications: × 100 for Pten, p-AKT S473 , fatty acid <t>synthase</t> (FASN) and <t>acetyl-CoA</t> carboxylase (ACC) proteins; × 200 for Ki67. p, phosphorylated; t, total.
    Acetyl Coa Carboxylase, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 381 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore malonyl coa
    Molecular characterization of hepatocellular carcinomas developed in sgPten/c-Met mice. ( a ) Levels of activation of AKT/mTOR and Ras/MAPK pathways in wild-type (WT) and sgPten/c-Met mouse livers, as detected by western blot analysis. Representative blots are shown. GAPDH and β-actin were used as loading controls. ( b ) Immunohistochemical staining of WT and sgPten/c-Met mouse livers. Original magnifications: × 100 for Pten, p-AKT S473 , fatty acid <t>synthase</t> (FASN) and <t>acetyl-CoA</t> carboxylase (ACC) proteins; × 200 for Ki67. p, phosphorylated; t, total.
    Malonyl Coa, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 453 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Cell Signaling Technology Inc phospho acetyl coa carboxylase
    Molecular characterization of hepatocellular carcinomas developed in sgPten/c-Met mice. ( a ) Levels of activation of AKT/mTOR and Ras/MAPK pathways in wild-type (WT) and sgPten/c-Met mouse livers, as detected by western blot analysis. Representative blots are shown. GAPDH and β-actin were used as loading controls. ( b ) Immunohistochemical staining of WT and sgPten/c-Met mouse livers. Original magnifications: × 100 for Pten, p-AKT S473 , fatty acid <t>synthase</t> (FASN) and <t>acetyl-CoA</t> carboxylase (ACC) proteins; × 200 for Ki67. p, phosphorylated; t, total.
    Phospho Acetyl Coa Carboxylase, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 184 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore palmitoyl coa
    Molecular characterization of hepatocellular carcinomas developed in sgPten/c-Met mice. ( a ) Levels of activation of AKT/mTOR and Ras/MAPK pathways in wild-type (WT) and sgPten/c-Met mouse livers, as detected by western blot analysis. Representative blots are shown. GAPDH and β-actin were used as loading controls. ( b ) Immunohistochemical staining of WT and sgPten/c-Met mouse livers. Original magnifications: × 100 for Pten, p-AKT S473 , fatty acid <t>synthase</t> (FASN) and <t>acetyl-CoA</t> carboxylase (ACC) proteins; × 200 for Ki67. p, phosphorylated; t, total.
    Palmitoyl Coa, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 348 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore oleoyl coa
    Circular dichroic spectra of a mixture of hPPARα and hLXRα in the absence and presence of LCFA and <t>LCFA-CoA.</t> Far-UV spectra obtained experimentally of a mixture of equal amino acid molarities of hPPARα and hLXRα in the absence of ligands (▼), experimentally observed spectra of a mixture of equal amino acid molarities of hPPARα and hLXRα in the presence of ligands (Obs, ●), and the calculated average of the two proteins individually examined in the presence of ligand (Calc, ○). Ligands include (A) palmitic acid (C16:0), (B) palmitoyl-CoA (C16:0-CoA), (C) oleic acid (C18:1), (D) oleoyl-CoA (C18:1-CoA), (E) linoleic acid (C18:2), (F) linoleoyl-CoA (C18:2-CoA), (G) <t>eicosapentaenoic</t> acid (C20:5), and (H) eicosapentaenoyl-CoA (C20:5-CoA). Each spectrum is representative of an average of 10 scans taken from at least three replicates.
    Oleoyl Coa, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 203 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Millipore hmg coa reductase assay kit
    Env9 is an oxidoreductase and requires conserved oxidoreductase domains for its enzymatic activity in vitro. Reductase activity is expressed as the rate of decrease of NADPH absorbance and expressed in percentage of the initial value. a Control reactions contained purified <t>HMG-CoA</t> reductase (2.5–3.5 μg), 400 μM NADPH, and 0.3 μg/μl HMG-CoA incubated for 30 min at 30 °C. P13 fractions (containing 27–30 μg protein) with or without Env9-HA were incubated with 400 μM NADPH and 0.3 μg/μl HMG-CoA ( b ) or 0.3 μg/μl 4-hydroxynonenal ( c ) for 30 min at 30 °C and rate of decrease in absorbance at 340 nm was recorded every 15 min for 30 min. d LD-enriched fractions (containing 12 μg protein) with or without Env9-HA were incubated with 400 μM NADPH and 0.3 μg/μl 4-HNE for 120 min at 30 °C. Rate of decrease in absorbance at 340 nm was recorded at 0, 30, 60, and 120 min. P13 fractions (containing 27–30 μg protein) from ENV9 -overexpressing cells (ENV9-HA) or indicated mutants were assayed for reductase activities using 0.3 μg/μl HMG-CoA ( e ) or 0.3 μg/μl 4-hydroxynonenal ( f ) as described in b , c . g LD-enriched fractions (containing 12 μg protein) from ENV9 -overexpressing cells (ENV9-HA) or indicated mutants were assayed for reductase activities using 0.3 μg/μl 4-HNE as described in d . Data shown are average of at least two independent experiments
    Hmg Coa Reductase Assay Kit, supplied by Millipore, used in various techniques. Bioz Stars score: 98/100, based on 385 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Millipore acetyl coenzyme a assay kit
    Env9 is an oxidoreductase and requires conserved oxidoreductase domains for its enzymatic activity in vitro. Reductase activity is expressed as the rate of decrease of NADPH absorbance and expressed in percentage of the initial value. a Control reactions contained purified <t>HMG-CoA</t> reductase (2.5–3.5 μg), 400 μM NADPH, and 0.3 μg/μl HMG-CoA incubated for 30 min at 30 °C. P13 fractions (containing 27–30 μg protein) with or without Env9-HA were incubated with 400 μM NADPH and 0.3 μg/μl HMG-CoA ( b ) or 0.3 μg/μl 4-hydroxynonenal ( c ) for 30 min at 30 °C and rate of decrease in absorbance at 340 nm was recorded every 15 min for 30 min. d LD-enriched fractions (containing 12 μg protein) with or without Env9-HA were incubated with 400 μM NADPH and 0.3 μg/μl 4-HNE for 120 min at 30 °C. Rate of decrease in absorbance at 340 nm was recorded at 0, 30, 60, and 120 min. P13 fractions (containing 27–30 μg protein) from ENV9 -overexpressing cells (ENV9-HA) or indicated mutants were assayed for reductase activities using 0.3 μg/μl HMG-CoA ( e ) or 0.3 μg/μl 4-hydroxynonenal ( f ) as described in b , c . g LD-enriched fractions (containing 12 μg protein) from ENV9 -overexpressing cells (ENV9-HA) or indicated mutants were assayed for reductase activities using 0.3 μg/μl 4-HNE as described in d . Data shown are average of at least two independent experiments
    Acetyl Coenzyme A Assay Kit, supplied by Millipore, used in various techniques. Bioz Stars score: 98/100, based on 48 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Avanti Polar acyl coas
    Env9 is an oxidoreductase and requires conserved oxidoreductase domains for its enzymatic activity in vitro. Reductase activity is expressed as the rate of decrease of NADPH absorbance and expressed in percentage of the initial value. a Control reactions contained purified <t>HMG-CoA</t> reductase (2.5–3.5 μg), 400 μM NADPH, and 0.3 μg/μl HMG-CoA incubated for 30 min at 30 °C. P13 fractions (containing 27–30 μg protein) with or without Env9-HA were incubated with 400 μM NADPH and 0.3 μg/μl HMG-CoA ( b ) or 0.3 μg/μl 4-hydroxynonenal ( c ) for 30 min at 30 °C and rate of decrease in absorbance at 340 nm was recorded every 15 min for 30 min. d LD-enriched fractions (containing 12 μg protein) with or without Env9-HA were incubated with 400 μM NADPH and 0.3 μg/μl 4-HNE for 120 min at 30 °C. Rate of decrease in absorbance at 340 nm was recorded at 0, 30, 60, and 120 min. P13 fractions (containing 27–30 μg protein) from ENV9 -overexpressing cells (ENV9-HA) or indicated mutants were assayed for reductase activities using 0.3 μg/μl HMG-CoA ( e ) or 0.3 μg/μl 4-hydroxynonenal ( f ) as described in b , c . g LD-enriched fractions (containing 12 μg protein) from ENV9 -overexpressing cells (ENV9-HA) or indicated mutants were assayed for reductase activities using 0.3 μg/μl 4-HNE as described in d . Data shown are average of at least two independent experiments
    Acyl Coas, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 91/100, based on 49 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Moravek Biochemicals c acetyl coa
    <t>hMOF</t> Lys-274 mutants are thermally destabilized, but are still able to bind cofactor. Normalized thermal denaturation curves for hMOF Lys-274 mutants in the absence ( A ) and presence ( B ) of 100 μ m <t>CoA</t> are shown. SYPRO Orange fluorescence is shown,
    C Acetyl Coa, supplied by Moravek Biochemicals, used in various techniques. Bioz Stars score: 90/100, based on 79 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore acetoacetyl coa
    <t>hMOF</t> Lys-274 mutants are thermally destabilized, but are still able to bind cofactor. Normalized thermal denaturation curves for hMOF Lys-274 mutants in the absence ( A ) and presence ( B ) of 100 μ m <t>CoA</t> are shown. SYPRO Orange fluorescence is shown,
    Acetoacetyl Coa, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 105 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Santa Cruz Biotechnology hmg coa reductase
    A diagram of the mevalonate cascade and the structure of the <t>HMG-CoA</t> reductase inhibitor ATST used in this study (modified from Holstein et al ).
    Hmg Coa Reductase, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 84 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Mine Safety Appliances propionyl coa
    Influence of overexpression of a <t>propionyl-CoA</t> synthetase on 3-ethylphenol ( A ) and 3-methylphenol ( B ) formation with and without supplementation of external propionate. Yeast strains CEN.PK2-1C expressing the 3-methylphenol pathway ( Ppopt <t>MSAS</t> , opt npgA and opt patG 14 ) and additionally the propionyl-CoA synthase opt prpE , with or without the Δcit2Δcit3 double deletion (strains JHY185 and JHY218, respectively), were inoculated at an OD of 5 and cultivated for 144 h in KP i buffered YPD medium (pH 6.5) with or without supplementation of 10 mM propionate. Culture supernatants were analysed via HPLC for 3-alkylphenol production. Error bars represent standard deviations of biological duplicates.
    Propionyl Coa, supplied by Mine Safety Appliances, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Millipore acetyl coenzyme a sodium salt
    Influence of overexpression of a <t>propionyl-CoA</t> synthetase on 3-ethylphenol ( A ) and 3-methylphenol ( B ) formation with and without supplementation of external propionate. Yeast strains CEN.PK2-1C expressing the 3-methylphenol pathway ( Ppopt <t>MSAS</t> , opt npgA and opt patG 14 ) and additionally the propionyl-CoA synthase opt prpE , with or without the Δcit2Δcit3 double deletion (strains JHY185 and JHY218, respectively), were inoculated at an OD of 5 and cultivated for 144 h in KP i buffered YPD medium (pH 6.5) with or without supplementation of 10 mM propionate. Culture supernatants were analysed via HPLC for 3-alkylphenol production. Error bars represent standard deviations of biological duplicates.
    Acetyl Coenzyme A Sodium Salt, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 51 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore coenzyme a trilithium salt
    Influence of overexpression of a <t>propionyl-CoA</t> synthetase on 3-ethylphenol ( A ) and 3-methylphenol ( B ) formation with and without supplementation of external propionate. Yeast strains CEN.PK2-1C expressing the 3-methylphenol pathway ( Ppopt <t>MSAS</t> , opt npgA and opt patG 14 ) and additionally the propionyl-CoA synthase opt prpE , with or without the Δcit2Δcit3 double deletion (strains JHY185 and JHY218, respectively), were inoculated at an OD of 5 and cultivated for 144 h in KP i buffered YPD medium (pH 6.5) with or without supplementation of 10 mM propionate. Culture supernatants were analysed via HPLC for 3-alkylphenol production. Error bars represent standard deviations of biological duplicates.
    Coenzyme A Trilithium Salt, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 71 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Substrate binding and conformational changes of the central β hairpin and C extension. ( A ) Details of xEco2-K105-CoA interaction showing substrate hairpin (yellow) coordinated by the C extension (red) in form of a β sheet. ( B ) Conserved surface rendition of K105-CoA bound to xEco2. ( C ) Details of xEco2-K106-CoA interaction showing substrate peptide (yellow) coordinated by the central β hairpin (orange) in form of a β sheet. ( D ) Conserved surface rendition of K106-CoA bound to xEco2. ( E ) Superimposition of peptide-free (red), K105-CoA (green), and K106-CoA (salmon) bound xEco2 structures showing occupation of and displacement of W623 from the central hydrophobic pocket. ( F ) Superimposition of the C extension in peptide-free (red), K105-CoA (green), and K106-CoA (salmon) bound conformations. The C extension shows a 180° flip from coordinating W623 at the hydrophobic pocket to an open conformation upon K106-CoA binding.

    Journal: Scientific Reports

    Article Title: Structural Basis of Eco1-Mediated Cohesin Acetylation

    doi: 10.1038/srep44313

    Figure Lengend Snippet: Substrate binding and conformational changes of the central β hairpin and C extension. ( A ) Details of xEco2-K105-CoA interaction showing substrate hairpin (yellow) coordinated by the C extension (red) in form of a β sheet. ( B ) Conserved surface rendition of K105-CoA bound to xEco2. ( C ) Details of xEco2-K106-CoA interaction showing substrate peptide (yellow) coordinated by the central β hairpin (orange) in form of a β sheet. ( D ) Conserved surface rendition of K106-CoA bound to xEco2. ( E ) Superimposition of peptide-free (red), K105-CoA (green), and K106-CoA (salmon) bound xEco2 structures showing occupation of and displacement of W623 from the central hydrophobic pocket. ( F ) Superimposition of the C extension in peptide-free (red), K105-CoA (green), and K106-CoA (salmon) bound conformations. The C extension shows a 180° flip from coordinating W623 at the hydrophobic pocket to an open conformation upon K106-CoA binding.

    Article Snippet: Conjugation of the purified bromopropionyl-peptide to Coenzyme A was achieved by adding 25 mg (5 eq) of Coenzyme A hydrate (Sigma) dissolved in 1M triethylammonium bicarbonate, pH 8.4–8.6 (Fluka) with 20 mg of peptide in 1 ml dimethylsuphoxide and stirring at room temperature for 18 h. Following lyophilization of the solution, the conjugated peptide was solubilized in H2 0 and purified by RP-HPLC as previously described using a gradient of 0% to 40% Buffer B over 40 min.

    Techniques: Binding Assay

    Mechanism of Eco1-mediated Smc3 acetylation. ( A ) Speculative model for Eco1-Smc3 interaction created by docking of xEco2-K105-CoA structure (salmon and blue) onto the S. cerevisiae Smc3-Scc1 (Smc3 is green; Scc1 is cyan) structure with reference to the relative positions of the tandem lysines ( S. cerevisiae K112 and K113). ( B ) Speculative model for Eco1-Smc3 interaction created by docking of xEco2-K106-CoA structure (salmon and blue) onto the S. cerevisiae Smc3-Scc1 (Smc3 is green; Scc1 is cyan) structure with reference to the relative positions of the tandem lysines ( S. cerevisiae K112 and K113). xEco2 rotates by 180° along the plane of the β sheet of Smc3 ATPase domain. ( C ) Schematics of Eco1 substrate specificity conferred by the concerted conformational changes of the central β hairpin (orange) and the C extension (red). The conserved hydrophobic pocket is occupied by W623 of xEco2 in the peptide-free and K105 targeting configurations, and by Y109 from Smc3 during K106 targeting respectively.

    Journal: Scientific Reports

    Article Title: Structural Basis of Eco1-Mediated Cohesin Acetylation

    doi: 10.1038/srep44313

    Figure Lengend Snippet: Mechanism of Eco1-mediated Smc3 acetylation. ( A ) Speculative model for Eco1-Smc3 interaction created by docking of xEco2-K105-CoA structure (salmon and blue) onto the S. cerevisiae Smc3-Scc1 (Smc3 is green; Scc1 is cyan) structure with reference to the relative positions of the tandem lysines ( S. cerevisiae K112 and K113). ( B ) Speculative model for Eco1-Smc3 interaction created by docking of xEco2-K106-CoA structure (salmon and blue) onto the S. cerevisiae Smc3-Scc1 (Smc3 is green; Scc1 is cyan) structure with reference to the relative positions of the tandem lysines ( S. cerevisiae K112 and K113). xEco2 rotates by 180° along the plane of the β sheet of Smc3 ATPase domain. ( C ) Schematics of Eco1 substrate specificity conferred by the concerted conformational changes of the central β hairpin (orange) and the C extension (red). The conserved hydrophobic pocket is occupied by W623 of xEco2 in the peptide-free and K105 targeting configurations, and by Y109 from Smc3 during K106 targeting respectively.

    Article Snippet: Conjugation of the purified bromopropionyl-peptide to Coenzyme A was achieved by adding 25 mg (5 eq) of Coenzyme A hydrate (Sigma) dissolved in 1M triethylammonium bicarbonate, pH 8.4–8.6 (Fluka) with 20 mg of peptide in 1 ml dimethylsuphoxide and stirring at room temperature for 18 h. Following lyophilization of the solution, the conjugated peptide was solubilized in H2 0 and purified by RP-HPLC as previously described using a gradient of 0% to 40% Buffer B over 40 min.

    Techniques:

    Identified catabolic pathways of HNE/HNA via ω- and ω-1-oxidations in the perfused rat livers. Compounds 1–13 are as follows: HNE ( 1 ), HNA ( 2 ), 4,8-DHNA ( 3 ), 4,9-DHNA ( 4 ), 6-hydroxynonenodioyl-CoA ( 5 ), 4-hydroxyheptanedioyl-CoA

    Journal: The Journal of Biological Chemistry

    Article Title: Catabolism of (2E)-4-Hydroxy-2-nonenal via ω- and ω-1-Oxidation Stimulated by Ketogenic Diet *

    doi: 10.1074/jbc.M114.602458

    Figure Lengend Snippet: Identified catabolic pathways of HNE/HNA via ω- and ω-1-oxidations in the perfused rat livers. Compounds 1–13 are as follows: HNE ( 1 ), HNA ( 2 ), 4,8-DHNA ( 3 ), 4,9-DHNA ( 4 ), 6-hydroxynonenodioyl-CoA ( 5 ), 4-hydroxyheptanedioyl-CoA

    Article Snippet: General chemicals, including acyl-coenzyme A, were purchased from Sigma-Aldrich.

    Techniques:

    Molecular characterization of hepatocellular carcinomas developed in sgPten/c-Met mice. ( a ) Levels of activation of AKT/mTOR and Ras/MAPK pathways in wild-type (WT) and sgPten/c-Met mouse livers, as detected by western blot analysis. Representative blots are shown. GAPDH and β-actin were used as loading controls. ( b ) Immunohistochemical staining of WT and sgPten/c-Met mouse livers. Original magnifications: × 100 for Pten, p-AKT S473 , fatty acid synthase (FASN) and acetyl-CoA carboxylase (ACC) proteins; × 200 for Ki67. p, phosphorylated; t, total.

    Journal: Experimental & Molecular Medicine

    Article Title: Loss of Pten synergizes with c-Met to promote hepatocellular carcinoma development via mTORC2 pathway

    doi: 10.1038/emm.2017.158

    Figure Lengend Snippet: Molecular characterization of hepatocellular carcinomas developed in sgPten/c-Met mice. ( a ) Levels of activation of AKT/mTOR and Ras/MAPK pathways in wild-type (WT) and sgPten/c-Met mouse livers, as detected by western blot analysis. Representative blots are shown. GAPDH and β-actin were used as loading controls. ( b ) Immunohistochemical staining of WT and sgPten/c-Met mouse livers. Original magnifications: × 100 for Pten, p-AKT S473 , fatty acid synthase (FASN) and acetyl-CoA carboxylase (ACC) proteins; × 200 for Ki67. p, phosphorylated; t, total.

    Article Snippet: Immunohistochemistry (IHC) was performed as previously described., The primary antibodies against c-Met (Abcam, Cambridge, MA, USA; 1:100), p-AKTS473 (Cell Signaling Technology, Danvers, MA, USA; 1:100), Pten (Cell Signaling Technology; 1:100), fatty acid synthase (FASN; Cell Signaling Technology; 1:150), acetyl-CoA carboxylase (ACC; Cell Signaling Technology; 1:100), p-ERK (Cell Signaling Technology; 1:100), and Ki67 (Thermo Fisher Scientific, Waltham, MA, USA; 1:150) were used in the present investigation.

    Techniques: Mouse Assay, Activation Assay, Western Blot, Immunohistochemistry, Staining

    Circular dichroic spectra of a mixture of hPPARα and hLXRα in the absence and presence of LCFA and LCFA-CoA. Far-UV spectra obtained experimentally of a mixture of equal amino acid molarities of hPPARα and hLXRα in the absence of ligands (▼), experimentally observed spectra of a mixture of equal amino acid molarities of hPPARα and hLXRα in the presence of ligands (Obs, ●), and the calculated average of the two proteins individually examined in the presence of ligand (Calc, ○). Ligands include (A) palmitic acid (C16:0), (B) palmitoyl-CoA (C16:0-CoA), (C) oleic acid (C18:1), (D) oleoyl-CoA (C18:1-CoA), (E) linoleic acid (C18:2), (F) linoleoyl-CoA (C18:2-CoA), (G) eicosapentaenoic acid (C20:5), and (H) eicosapentaenoyl-CoA (C20:5-CoA). Each spectrum is representative of an average of 10 scans taken from at least three replicates.

    Journal: Biochemistry

    Article Title: Ligand-Regulated Heterodimerization of Peroxisome Proliferator-Activated Receptor α with Liver X Receptor α

    doi: 10.1021/bi401679y

    Figure Lengend Snippet: Circular dichroic spectra of a mixture of hPPARα and hLXRα in the absence and presence of LCFA and LCFA-CoA. Far-UV spectra obtained experimentally of a mixture of equal amino acid molarities of hPPARα and hLXRα in the absence of ligands (▼), experimentally observed spectra of a mixture of equal amino acid molarities of hPPARα and hLXRα in the presence of ligands (Obs, ●), and the calculated average of the two proteins individually examined in the presence of ligand (Calc, ○). Ligands include (A) palmitic acid (C16:0), (B) palmitoyl-CoA (C16:0-CoA), (C) oleic acid (C18:1), (D) oleoyl-CoA (C18:1-CoA), (E) linoleic acid (C18:2), (F) linoleoyl-CoA (C18:2-CoA), (G) eicosapentaenoic acid (C20:5), and (H) eicosapentaenoyl-CoA (C20:5-CoA). Each spectrum is representative of an average of 10 scans taken from at least three replicates.

    Article Snippet: Chemicals Coenzyme A, palmitic acid, oleic acid, linoleic acid, eicosapentaenoic acid, palmitoyl-CoA, oleoyl-CoA, linoleoyl-CoA, and clofibrate were from Sigma (St. Louis, MO).

    Techniques:

    Fluorescent protein–protein binding assays of Cy5-labeled hPPARα titrated against increasing concentrations of unlabeled hLXRα in the presence of LCFA and LCFA-CoA. The change in fluorescence intensity of 25 nM Cy5-labeled hPPARα titrated with increasing concentrations (0–250 nM) of hLXRα in the presence of 25 nM (A) palmitic acid, (B) palmitoyl-CoA, (C) oleic acid, (D) oleoyl-CoA, (E) linoleic acid, (F) linoleoyl-CoA, (G) eicosapentaenoic acid, and (H) eicosapentaenoyl-CoA. Insets represent double-reciprocal linear plots of each binding curve. Values represent means ± the standard error ( n = 3–5).

    Journal: Biochemistry

    Article Title: Ligand-Regulated Heterodimerization of Peroxisome Proliferator-Activated Receptor α with Liver X Receptor α

    doi: 10.1021/bi401679y

    Figure Lengend Snippet: Fluorescent protein–protein binding assays of Cy5-labeled hPPARα titrated against increasing concentrations of unlabeled hLXRα in the presence of LCFA and LCFA-CoA. The change in fluorescence intensity of 25 nM Cy5-labeled hPPARα titrated with increasing concentrations (0–250 nM) of hLXRα in the presence of 25 nM (A) palmitic acid, (B) palmitoyl-CoA, (C) oleic acid, (D) oleoyl-CoA, (E) linoleic acid, (F) linoleoyl-CoA, (G) eicosapentaenoic acid, and (H) eicosapentaenoyl-CoA. Insets represent double-reciprocal linear plots of each binding curve. Values represent means ± the standard error ( n = 3–5).

    Article Snippet: Chemicals Coenzyme A, palmitic acid, oleic acid, linoleic acid, eicosapentaenoic acid, palmitoyl-CoA, oleoyl-CoA, linoleoyl-CoA, and clofibrate were from Sigma (St. Louis, MO).

    Techniques: Protein Binding, Labeling, Fluorescence, Binding Assay

    Env9 is an oxidoreductase and requires conserved oxidoreductase domains for its enzymatic activity in vitro. Reductase activity is expressed as the rate of decrease of NADPH absorbance and expressed in percentage of the initial value. a Control reactions contained purified HMG-CoA reductase (2.5–3.5 μg), 400 μM NADPH, and 0.3 μg/μl HMG-CoA incubated for 30 min at 30 °C. P13 fractions (containing 27–30 μg protein) with or without Env9-HA were incubated with 400 μM NADPH and 0.3 μg/μl HMG-CoA ( b ) or 0.3 μg/μl 4-hydroxynonenal ( c ) for 30 min at 30 °C and rate of decrease in absorbance at 340 nm was recorded every 15 min for 30 min. d LD-enriched fractions (containing 12 μg protein) with or without Env9-HA were incubated with 400 μM NADPH and 0.3 μg/μl 4-HNE for 120 min at 30 °C. Rate of decrease in absorbance at 340 nm was recorded at 0, 30, 60, and 120 min. P13 fractions (containing 27–30 μg protein) from ENV9 -overexpressing cells (ENV9-HA) or indicated mutants were assayed for reductase activities using 0.3 μg/μl HMG-CoA ( e ) or 0.3 μg/μl 4-hydroxynonenal ( f ) as described in b , c . g LD-enriched fractions (containing 12 μg protein) from ENV9 -overexpressing cells (ENV9-HA) or indicated mutants were assayed for reductase activities using 0.3 μg/μl 4-HNE as described in d . Data shown are average of at least two independent experiments

    Journal: Current genetics

    Article Title: Yeast ENV9 encodes a conserved lipid droplet (LD) short-chain dehydrogenase involved in LD morphology

    doi: 10.1007/s00294-017-0702-y

    Figure Lengend Snippet: Env9 is an oxidoreductase and requires conserved oxidoreductase domains for its enzymatic activity in vitro. Reductase activity is expressed as the rate of decrease of NADPH absorbance and expressed in percentage of the initial value. a Control reactions contained purified HMG-CoA reductase (2.5–3.5 μg), 400 μM NADPH, and 0.3 μg/μl HMG-CoA incubated for 30 min at 30 °C. P13 fractions (containing 27–30 μg protein) with or without Env9-HA were incubated with 400 μM NADPH and 0.3 μg/μl HMG-CoA ( b ) or 0.3 μg/μl 4-hydroxynonenal ( c ) for 30 min at 30 °C and rate of decrease in absorbance at 340 nm was recorded every 15 min for 30 min. d LD-enriched fractions (containing 12 μg protein) with or without Env9-HA were incubated with 400 μM NADPH and 0.3 μg/μl 4-HNE for 120 min at 30 °C. Rate of decrease in absorbance at 340 nm was recorded at 0, 30, 60, and 120 min. P13 fractions (containing 27–30 μg protein) from ENV9 -overexpressing cells (ENV9-HA) or indicated mutants were assayed for reductase activities using 0.3 μg/μl HMG-CoA ( e ) or 0.3 μg/μl 4-hydroxynonenal ( f ) as described in b , c . g LD-enriched fractions (containing 12 μg protein) from ENV9 -overexpressing cells (ENV9-HA) or indicated mutants were assayed for reductase activities using 0.3 μg/μl 4-HNE as described in d . Data shown are average of at least two independent experiments

    Article Snippet: Reductase activities were determined spectrophotometrically using HMG-CoA Reductase Assay kit (Sigma, St. Louis, MO, USA).

    Techniques: Activity Assay, In Vitro, Purification, Incubation

    hMOF Lys-274 mutants are thermally destabilized, but are still able to bind cofactor. Normalized thermal denaturation curves for hMOF Lys-274 mutants in the absence ( A ) and presence ( B ) of 100 μ m CoA are shown. SYPRO Orange fluorescence is shown,

    Journal: The Journal of Biological Chemistry

    Article Title: Structural and Functional Role of Acetyltransferase hMOF K274 Autoacetylation *

    doi: 10.1074/jbc.M116.736264

    Figure Lengend Snippet: hMOF Lys-274 mutants are thermally destabilized, but are still able to bind cofactor. Normalized thermal denaturation curves for hMOF Lys-274 mutants in the absence ( A ) and presence ( B ) of 100 μ m CoA are shown. SYPRO Orange fluorescence is shown,

    Article Snippet: Briefly, 50 n m hMOF or 200 n m MOZ was incubated with 400 μ m substrate peptide (H4(1–19) peptide for hMOF and H3(1–19) for MOZ) (GenScript) and 50 μ m [14 C]acetyl-CoA (50–60 mCi/mmol, Moravek) in reaction buffer (100 m m acetate, 50 m m Bistris, 50 m m Tris at various pH values 100 m m NaCl, 800 μ m cysteine, and 0.25 mg/ml of BSA for hMOF and 40 m m Tris-HCl (pH 8.0), 100 m m NaCl, 1 m m DTT for MOZ) at a final volume of 50 μl and incubated at room temperature for 1 h. To quench the reaction, 20 μl of the reaction mixture was added to negatively charged P81 paper (Millipore).

    Techniques: Fluorescence

    hMOF WT and hMOF K268M share very similar kinetic profiles. Michaelis-Menten curves are shown for hMOF-WT and hMOF-K268M against acetyl-CoA ( A ) and histone H4 peptide ( B ). Different k cat values were calculated for data in each graph to demonstrate similarities

    Journal: The Journal of Biological Chemistry

    Article Title: Structural and Functional Role of Acetyltransferase hMOF K274 Autoacetylation *

    doi: 10.1074/jbc.M116.736264

    Figure Lengend Snippet: hMOF WT and hMOF K268M share very similar kinetic profiles. Michaelis-Menten curves are shown for hMOF-WT and hMOF-K268M against acetyl-CoA ( A ) and histone H4 peptide ( B ). Different k cat values were calculated for data in each graph to demonstrate similarities

    Article Snippet: Briefly, 50 n m hMOF or 200 n m MOZ was incubated with 400 μ m substrate peptide (H4(1–19) peptide for hMOF and H3(1–19) for MOZ) (GenScript) and 50 μ m [14 C]acetyl-CoA (50–60 mCi/mmol, Moravek) in reaction buffer (100 m m acetate, 50 m m Bistris, 50 m m Tris at various pH values 100 m m NaCl, 800 μ m cysteine, and 0.25 mg/ml of BSA for hMOF and 40 m m Tris-HCl (pH 8.0), 100 m m NaCl, 1 m m DTT for MOZ) at a final volume of 50 μl and incubated at room temperature for 1 h. To quench the reaction, 20 μl of the reaction mixture was added to negatively charged P81 paper (Millipore).

    Techniques:

    A diagram of the mevalonate cascade and the structure of the HMG-CoA reductase inhibitor ATST used in this study (modified from Holstein et al ).

    Journal: International journal of cancer. Journal international du cancer

    Article Title: Synergistic Actions of Atorvastatin with ?-Tocotrienol and Celecoxib against Human Colon Cancer HT29 and HCT116 Cells

    doi: 10.1002/ijc.24766

    Figure Lengend Snippet: A diagram of the mevalonate cascade and the structure of the HMG-CoA reductase inhibitor ATST used in this study (modified from Holstein et al ).

    Article Snippet: These results suggest that ATST inhibited HMG-CoA reductase activity, depleted downstream isoprenoids, and elevated the levels of HMG-CoA reductase, whereas γ-TT neutralized the upregulated level of HMG-CoA reductase, resulting in a synergistic action between the two compounds

    Techniques: Modification

    Effects of ATST, γ-TT, and their combination on the level of HMG-CoA reductase and the cellular distribution of RhoA. (A) HT29 cells were treated with ATST, γ-TT, and their combination for 24 h at the concentrations indicated. The protein

    Journal: International journal of cancer. Journal international du cancer

    Article Title: Synergistic Actions of Atorvastatin with ?-Tocotrienol and Celecoxib against Human Colon Cancer HT29 and HCT116 Cells

    doi: 10.1002/ijc.24766

    Figure Lengend Snippet: Effects of ATST, γ-TT, and their combination on the level of HMG-CoA reductase and the cellular distribution of RhoA. (A) HT29 cells were treated with ATST, γ-TT, and their combination for 24 h at the concentrations indicated. The protein

    Article Snippet: These results suggest that ATST inhibited HMG-CoA reductase activity, depleted downstream isoprenoids, and elevated the levels of HMG-CoA reductase, whereas γ-TT neutralized the upregulated level of HMG-CoA reductase, resulting in a synergistic action between the two compounds

    Techniques:

    Influence of overexpression of a propionyl-CoA synthetase on 3-ethylphenol ( A ) and 3-methylphenol ( B ) formation with and without supplementation of external propionate. Yeast strains CEN.PK2-1C expressing the 3-methylphenol pathway ( Ppopt MSAS , opt npgA and opt patG 14 ) and additionally the propionyl-CoA synthase opt prpE , with or without the Δcit2Δcit3 double deletion (strains JHY185 and JHY218, respectively), were inoculated at an OD of 5 and cultivated for 144 h in KP i buffered YPD medium (pH 6.5) with or without supplementation of 10 mM propionate. Culture supernatants were analysed via HPLC for 3-alkylphenol production. Error bars represent standard deviations of biological duplicates.

    Journal: Scientific Reports

    Article Title: Substrate promiscuity of polyketide synthase enables production of tsetse fly attractants 3-ethylphenol and 3-propylphenol by engineering precursor supply in yeast

    doi: 10.1038/s41598-020-66997-5

    Figure Lengend Snippet: Influence of overexpression of a propionyl-CoA synthetase on 3-ethylphenol ( A ) and 3-methylphenol ( B ) formation with and without supplementation of external propionate. Yeast strains CEN.PK2-1C expressing the 3-methylphenol pathway ( Ppopt MSAS , opt npgA and opt patG 14 ) and additionally the propionyl-CoA synthase opt prpE , with or without the Δcit2Δcit3 double deletion (strains JHY185 and JHY218, respectively), were inoculated at an OD of 5 and cultivated for 144 h in KP i buffered YPD medium (pH 6.5) with or without supplementation of 10 mM propionate. Culture supernatants were analysed via HPLC for 3-alkylphenol production. Error bars represent standard deviations of biological duplicates.

    Article Snippet: Conclusions In this work we show that yeast engineered to provide increased intracellular formation of propionyl-CoA or butyryl-CoA and expressing MSAS and MSA decarboxylase can be exploited to produce 3-EP and 3-PP from sugars.

    Techniques: Over Expression, Expressing, High Performance Liquid Chromatography

    Metabolic pathways for 3-alkylphenol production in S. cerevisiae . In S. cerevisiae the heterologous polyketide synthase MSAS, activated by phosphopantetheinyl transferase (NpgA), catalyses the formation of 6-methylsalicylic acid (6-MSA) utilizing malonyl-CoA as extender unit and acetyl-CoA as priming unit. Intracellular propionyl-CoA can be increased by expression of a bacterial propionyl-CoA synthase (PrpE), propionate feeding and deletion of (methyl) citrate synthase genes CIT2/3 to abolish its degradation. MSAS can then utilize propionyl-CoA as priming unit to catalyse the formation of 6-ethylsalicylic acid (6-ESA). The heterologous ‘reverse ß-oxidation’ pathway 21 , 22 is providing the priming unit butyryl-CoA from acetyl-CoA for the formation of 6-propylsalicylic acid (6-PSA). Finally, 6-MSA decarboxylase (PatG) converts the 6-alkylsalicylic acids, 6-MSA, 6-ESA or 6-PSA, to their respective 3-alkylphenols (3-methylphenol, 3-ethylphenol or 3-propylphenol) that are valuable tsetse fly attractants.

    Journal: Scientific Reports

    Article Title: Substrate promiscuity of polyketide synthase enables production of tsetse fly attractants 3-ethylphenol and 3-propylphenol by engineering precursor supply in yeast

    doi: 10.1038/s41598-020-66997-5

    Figure Lengend Snippet: Metabolic pathways for 3-alkylphenol production in S. cerevisiae . In S. cerevisiae the heterologous polyketide synthase MSAS, activated by phosphopantetheinyl transferase (NpgA), catalyses the formation of 6-methylsalicylic acid (6-MSA) utilizing malonyl-CoA as extender unit and acetyl-CoA as priming unit. Intracellular propionyl-CoA can be increased by expression of a bacterial propionyl-CoA synthase (PrpE), propionate feeding and deletion of (methyl) citrate synthase genes CIT2/3 to abolish its degradation. MSAS can then utilize propionyl-CoA as priming unit to catalyse the formation of 6-ethylsalicylic acid (6-ESA). The heterologous ‘reverse ß-oxidation’ pathway 21 , 22 is providing the priming unit butyryl-CoA from acetyl-CoA for the formation of 6-propylsalicylic acid (6-PSA). Finally, 6-MSA decarboxylase (PatG) converts the 6-alkylsalicylic acids, 6-MSA, 6-ESA or 6-PSA, to their respective 3-alkylphenols (3-methylphenol, 3-ethylphenol or 3-propylphenol) that are valuable tsetse fly attractants.

    Article Snippet: Conclusions In this work we show that yeast engineered to provide increased intracellular formation of propionyl-CoA or butyryl-CoA and expressing MSAS and MSA decarboxylase can be exploited to produce 3-EP and 3-PP from sugars.

    Techniques: Expressing