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A natural heme‐signature variant of CYP267A1 from Sorangium cellulosum So ce56 executes diverse ω‐hydroxylation
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| Zeitschriftentitel: | The FEBS Journal |
|---|---|
| Personen und Körperschaften: | , , , , , , |
| In: | The FEBS Journal, 282, 2015, 1, S. 74-88 |
| Medientyp: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
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| Schlagwörter: |
| author_facet |
Khatri, Yogan Hannemann, Frank Girhard, Marco Kappl, Reinhard Hutter, Michael Urlacher, Vlada B. Bernhardt, Rita Khatri, Yogan Hannemann, Frank Girhard, Marco Kappl, Reinhard Hutter, Michael Urlacher, Vlada B. Bernhardt, Rita |
|---|---|
| author |
Khatri, Yogan Hannemann, Frank Girhard, Marco Kappl, Reinhard Hutter, Michael Urlacher, Vlada B. Bernhardt, Rita |
| spellingShingle |
Khatri, Yogan Hannemann, Frank Girhard, Marco Kappl, Reinhard Hutter, Michael Urlacher, Vlada B. Bernhardt, Rita The FEBS Journal A natural heme‐signature variant of CYP267A1 from Sorangium cellulosum So ce56 executes diverse ω‐hydroxylation Cell Biology Molecular Biology Biochemistry |
| author_sort |
khatri, yogan |
| spelling |
Khatri, Yogan Hannemann, Frank Girhard, Marco Kappl, Reinhard Hutter, Michael Urlacher, Vlada B. Bernhardt, Rita 1742-464X 1742-4658 Wiley Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1111/febs.13104 <jats:p>A novel naturally occurring heme‐signature variant of <jats:styled-content style="fixed-case">CYP</jats:styled-content>267A1 from myxobacterium <jats:italic>Sorangium cellulosum</jats:italic> So ce56 and its mutant L366F, the actual mimic of the ‘conserved’ heme‐signature of cytochromes P450, were heterologously expressed in <jats:italic>Escherichia coli</jats:italic> in a soluble form and purified. The <jats:styled-content style="fixed-case">UV</jats:styled-content>–visible characteristics of both variants were highly similar. Although leucine replaced the phenylalanine in the heme‐signature domain of <jats:styled-content style="fixed-case">CYP</jats:styled-content>267A1, <jats:styled-content style="fixed-case">EPR</jats:styled-content> measurements of the ligand‐free wild‐type <jats:styled-content style="fixed-case">CYP</jats:styled-content>267A1 and the mutant L366F showed low‐spin rhombic species suggesting a conserved heme environment of the P450s. The need of primary redox partners for the orphan P450 was sustained by the bovine redox system and a class‐I electron transfer path was provided during fatty acid hydroxylation. <jats:styled-content style="fixed-case">CYP</jats:styled-content>267A1 showed higher activity and produced more diverse ω‐hydroxylated products compared with L366F. In both enzymes the regioselectivity of the fatty acid hydroxylation shifted towards the inner carbon atoms of the fatty acid chains with increasing carbon chain lengths. Our docking results in a homology model of the protein showed that longer fatty acids need to be folded to fit into the binding pocket. In the mutant L366F, the ω‐1 and ω‐2 positions which exhibit the largest electron density of the highest occupied molecular orbital are preferred. It is speculated that the leucine heme‐signature variant of P450 might have evolved under selective evolutionary pressure, which confers an increased advantage to generate a broader spectrum of related alcohols and carboxylic acids required for the bacterial homeostasis or metabolism in a particular ecological niche.</jats:p> A natural heme‐signature variant of <scp>CYP</scp>267A1 from <i>Sorangium cellulosum</i> So ce56 executes diverse ω‐hydroxylation The FEBS Journal |
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Biologie Chemie und Pharmazie |
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Wiley, 2015 |
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| title |
A natural heme‐signature variant of CYP267A1 from Sorangium cellulosum So ce56 executes diverse ω‐hydroxylation |
| title_unstemmed |
A natural heme‐signature variant of CYP267A1 from Sorangium cellulosum So ce56 executes diverse ω‐hydroxylation |
| title_full |
A natural heme‐signature variant of CYP267A1 from Sorangium cellulosum So ce56 executes diverse ω‐hydroxylation |
| title_fullStr |
A natural heme‐signature variant of CYP267A1 from Sorangium cellulosum So ce56 executes diverse ω‐hydroxylation |
| title_full_unstemmed |
A natural heme‐signature variant of CYP267A1 from Sorangium cellulosum So ce56 executes diverse ω‐hydroxylation |
| title_short |
A natural heme‐signature variant of CYP267A1 from Sorangium cellulosum So ce56 executes diverse ω‐hydroxylation |
| title_sort |
a natural heme‐signature variant of <scp>cyp</scp>267a1 from <i>sorangium cellulosum</i> so ce56 executes diverse ω‐hydroxylation |
| topic |
Cell Biology Molecular Biology Biochemistry |
| url |
http://dx.doi.org/10.1111/febs.13104 |
| publishDate |
2015 |
| physical |
74-88 |
| description |
<jats:p>A novel naturally occurring heme‐signature variant of <jats:styled-content style="fixed-case">CYP</jats:styled-content>267A1 from myxobacterium <jats:italic>Sorangium cellulosum</jats:italic> So ce56 and its mutant L366F, the actual mimic of the ‘conserved’ heme‐signature of cytochromes P450, were heterologously expressed in <jats:italic>Escherichia coli</jats:italic> in a soluble form and purified. The <jats:styled-content style="fixed-case">UV</jats:styled-content>–visible characteristics of both variants were highly similar. Although leucine replaced the phenylalanine in the heme‐signature domain of <jats:styled-content style="fixed-case">CYP</jats:styled-content>267A1, <jats:styled-content style="fixed-case">EPR</jats:styled-content> measurements of the ligand‐free wild‐type <jats:styled-content style="fixed-case">CYP</jats:styled-content>267A1 and the mutant L366F showed low‐spin rhombic species suggesting a conserved heme environment of the P450s. The need of primary redox partners for the orphan P450 was sustained by the bovine redox system and a class‐I electron transfer path was provided during fatty acid hydroxylation. <jats:styled-content style="fixed-case">CYP</jats:styled-content>267A1 showed higher activity and produced more diverse ω‐hydroxylated products compared with L366F. In both enzymes the regioselectivity of the fatty acid hydroxylation shifted towards the inner carbon atoms of the fatty acid chains with increasing carbon chain lengths. Our docking results in a homology model of the protein showed that longer fatty acids need to be folded to fit into the binding pocket. In the mutant L366F, the ω‐1 and ω‐2 positions which exhibit the largest electron density of the highest occupied molecular orbital are preferred. It is speculated that the leucine heme‐signature variant of P450 might have evolved under selective evolutionary pressure, which confers an increased advantage to generate a broader spectrum of related alcohols and carboxylic acids required for the bacterial homeostasis or metabolism in a particular ecological niche.</jats:p> |
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| description | <jats:p>A novel naturally occurring heme‐signature variant of <jats:styled-content style="fixed-case">CYP</jats:styled-content>267A1 from myxobacterium <jats:italic>Sorangium cellulosum</jats:italic> So ce56 and its mutant L366F, the actual mimic of the ‘conserved’ heme‐signature of cytochromes P450, were heterologously expressed in <jats:italic>Escherichia coli</jats:italic> in a soluble form and purified. The <jats:styled-content style="fixed-case">UV</jats:styled-content>–visible characteristics of both variants were highly similar. Although leucine replaced the phenylalanine in the heme‐signature domain of <jats:styled-content style="fixed-case">CYP</jats:styled-content>267A1, <jats:styled-content style="fixed-case">EPR</jats:styled-content> measurements of the ligand‐free wild‐type <jats:styled-content style="fixed-case">CYP</jats:styled-content>267A1 and the mutant L366F showed low‐spin rhombic species suggesting a conserved heme environment of the P450s. The need of primary redox partners for the orphan P450 was sustained by the bovine redox system and a class‐I electron transfer path was provided during fatty acid hydroxylation. <jats:styled-content style="fixed-case">CYP</jats:styled-content>267A1 showed higher activity and produced more diverse ω‐hydroxylated products compared with L366F. In both enzymes the regioselectivity of the fatty acid hydroxylation shifted towards the inner carbon atoms of the fatty acid chains with increasing carbon chain lengths. Our docking results in a homology model of the protein showed that longer fatty acids need to be folded to fit into the binding pocket. In the mutant L366F, the ω‐1 and ω‐2 positions which exhibit the largest electron density of the highest occupied molecular orbital are preferred. It is speculated that the leucine heme‐signature variant of P450 might have evolved under selective evolutionary pressure, which confers an increased advantage to generate a broader spectrum of related alcohols and carboxylic acids required for the bacterial homeostasis or metabolism in a particular ecological niche.</jats:p> |
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| spelling | Khatri, Yogan Hannemann, Frank Girhard, Marco Kappl, Reinhard Hutter, Michael Urlacher, Vlada B. Bernhardt, Rita 1742-464X 1742-4658 Wiley Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1111/febs.13104 <jats:p>A novel naturally occurring heme‐signature variant of <jats:styled-content style="fixed-case">CYP</jats:styled-content>267A1 from myxobacterium <jats:italic>Sorangium cellulosum</jats:italic> So ce56 and its mutant L366F, the actual mimic of the ‘conserved’ heme‐signature of cytochromes P450, were heterologously expressed in <jats:italic>Escherichia coli</jats:italic> in a soluble form and purified. The <jats:styled-content style="fixed-case">UV</jats:styled-content>–visible characteristics of both variants were highly similar. Although leucine replaced the phenylalanine in the heme‐signature domain of <jats:styled-content style="fixed-case">CYP</jats:styled-content>267A1, <jats:styled-content style="fixed-case">EPR</jats:styled-content> measurements of the ligand‐free wild‐type <jats:styled-content style="fixed-case">CYP</jats:styled-content>267A1 and the mutant L366F showed low‐spin rhombic species suggesting a conserved heme environment of the P450s. The need of primary redox partners for the orphan P450 was sustained by the bovine redox system and a class‐I electron transfer path was provided during fatty acid hydroxylation. <jats:styled-content style="fixed-case">CYP</jats:styled-content>267A1 showed higher activity and produced more diverse ω‐hydroxylated products compared with L366F. In both enzymes the regioselectivity of the fatty acid hydroxylation shifted towards the inner carbon atoms of the fatty acid chains with increasing carbon chain lengths. Our docking results in a homology model of the protein showed that longer fatty acids need to be folded to fit into the binding pocket. In the mutant L366F, the ω‐1 and ω‐2 positions which exhibit the largest electron density of the highest occupied molecular orbital are preferred. It is speculated that the leucine heme‐signature variant of P450 might have evolved under selective evolutionary pressure, which confers an increased advantage to generate a broader spectrum of related alcohols and carboxylic acids required for the bacterial homeostasis or metabolism in a particular ecological niche.</jats:p> A natural heme‐signature variant of <scp>CYP</scp>267A1 from <i>Sorangium cellulosum</i> So ce56 executes diverse ω‐hydroxylation The FEBS Journal |
| spellingShingle | Khatri, Yogan, Hannemann, Frank, Girhard, Marco, Kappl, Reinhard, Hutter, Michael, Urlacher, Vlada B., Bernhardt, Rita, The FEBS Journal, A natural heme‐signature variant of CYP267A1 from Sorangium cellulosum So ce56 executes diverse ω‐hydroxylation, Cell Biology, Molecular Biology, Biochemistry |
| title | A natural heme‐signature variant of CYP267A1 from Sorangium cellulosum So ce56 executes diverse ω‐hydroxylation |
| title_full | A natural heme‐signature variant of CYP267A1 from Sorangium cellulosum So ce56 executes diverse ω‐hydroxylation |
| title_fullStr | A natural heme‐signature variant of CYP267A1 from Sorangium cellulosum So ce56 executes diverse ω‐hydroxylation |
| title_full_unstemmed | A natural heme‐signature variant of CYP267A1 from Sorangium cellulosum So ce56 executes diverse ω‐hydroxylation |
| title_short | A natural heme‐signature variant of CYP267A1 from Sorangium cellulosum So ce56 executes diverse ω‐hydroxylation |
| title_sort | a natural heme‐signature variant of <scp>cyp</scp>267a1 from <i>sorangium cellulosum</i> so ce56 executes diverse ω‐hydroxylation |
| title_unstemmed | A natural heme‐signature variant of CYP267A1 from Sorangium cellulosum So ce56 executes diverse ω‐hydroxylation |
| topic | Cell Biology, Molecular Biology, Biochemistry |
| url | http://dx.doi.org/10.1111/febs.13104 |