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Jong Seong Kang – One of the best experts on this subject based on the ideXlab platform.

  • Quantitative determination of psoralen and Angelicin from some medicinal herbs by high performance liquid chromatography
    Archives of Pharmacal Research, 2003
    Co-Authors: Nguyen Thanh Dong, Gwi Seo Hwang, Jong Seong Kang

    Abstract:

    A reversed-phase high performance liquid chromatographic method was developed to determine the contents of psoralen and Angelicin from some medicinal herbs. The optimum eluent for chromatography was 20 v/v% acetonitrile in water on a Zorbax 300SB C_18 column. The identification was carried out by comparing the retention time and mass spectra of the relevant peaks with their standards. The variation of the concentration of psoralen and Angelicin was wide between different species. The seeds of Psoralea corylifolia showed the highest contents of psoralen (7.8 mg/g) and Angelicin (2.3 mg/g) among the tested herbs.

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Frederic Bourgaud – One of the best experts on this subject based on the ideXlab platform.

  • Isolation and Functional Characterization of CYP71AJ4 Encoding for the First P450 Monooxygenase of Angular Furanocoumarin Biosynthesis
    Journal of Biological Chemistry, 2009
    Co-Authors: Romain Larbat, Alain Hehn, Joachim Hans, Sarah Schneider, Hélène Jugdé, Bernd Schneider, Ulrich Matern, Frederic Bourgaud

    Abstract:

    The biosynthesis of linear and angular furanocoumarins is still poorly understood at the molecular level, with only psoralen synthase (CYP71AJ1) identified from Ammi majus. Using cDNA probes inferred from CYP71AJ1, three orthologs were isolated from Apium graveolens (CYP71AJ2) and Pastinaca sativa (CYP71AJ3 and-4) and functionally expressed in yeast cells. CYP71AJ2 and CYP71AJ3 displayed psoralen synthase activity, whereas CYP71AJ4 only catalyzed the conversion of ()-colum-bianetin to Angelicin and negligible amounts of a hydroxylated columbianetin by-product. CYP71AJ4 thus constitutes the first fully characterized P450 monooxygenase specific for the angular furanocoumarin pathway. The Angelicin synthase exhibited an apparent K m of 2.1 0.4 M for ()-columbianetin and a k cat of 112 14 min 1. Moreover, the use of 3-deuterated ()-columbianetin as substrate led to an almost complete ” metabolic switch, ” resulting in the synthesis of anti-3-hydroxy-3-deuterated()-columbianetin. This confirms that Angelicin synthase attacks columbianetin by syn-elimination of hydrogen from C-3. Sequence comparison between psoralen synthase (CYP71AJ3) and Angelicin synthase (CYP71AJ4) showed 70% identity, whereas the identity dropped to 40% in those regions thought to provide the substrate recognition sites. Accordingly, CYP71AJ3 and CYP71AJ4 might be derived from a common ancestor of unknown functionality by gene duplication and subsequent molecular evolution. Furanocoumarins are natural plant metabolites characterized by a furane moiety fused to benzopyran-2-one. The position of the furane substitution distinguishes two large groups of compounds, the linear (psoralens) and the angular furanocou-marins (Angelicin and derivatives) (Fig.

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  • Isolation and Functional Characterization of CYP71AJ4 Encoding for the First P450 Monooxygenase of Angular Furanocoumarin Biosynthesis
    Journal of Biological Chemistry, 2008
    Co-Authors: Romain Larbat, Alain Hehn, Joachim Hans, Sarah Schneider, Hélène Jugdé, Bernd Schneider, Ulrich Matern, Frederic Bourgaud

    Abstract:

    The biosynthesis of linear and angular furanocoumarins is still poorly understood at the molecular level, with only psoralen synthase (CYP71AJ1) identified from Ammi majus. Using cDNA probes inferred from CYP71AJ1, three orthologs were isolated from Apium graveolens (CYP71AJ2) and Pastinaca sativa (CYP71AJ3 and -4) and functionally expressed in yeast cells. CYP71AJ2 and CYP71AJ3 displayed psoralen synthase activity, whereas CYP71AJ4 only catalyzed the conversion of (+)-columbianetin to Angelicin and negligible amounts of a hydroxylated columbianetin by-product. CYP71AJ4 thus constitutes the first fully characterized P450 monooxygenase specific for the angular furanocoumarin pathway. The Angelicin synthase exhibited an apparent K(m) of 2.1 +/- 0.4 microm for (+)-columbianetin and a k(cat) of 112 +/- 14 min(-1). Moreover, the use of 3′-deuterated (+)-columbianetin as substrate led to an almost complete “metabolic switch,” resulting in the synthesis of anti-3′-hydroxy-3′-deuterated(+)-columbianetin. This confirms that Angelicin synthase attacks columbianetin by syn-elimination of hydrogen from C-3′. Sequence comparison between psoralen synthase (CYP71AJ3) and Angelicin synthase (CYP71AJ4) showed 70% identity, whereas the identity dropped to 40% in those regions thought to provide the substrate recognition sites. Accordingly, CYP71AJ3 and CYP71AJ4 might be derived from a common ancestor of unknown functionality by gene duplication and subsequent molecular evolution.

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  • Molecular Cloning and Functional Characterization of Psoralen Synthase, the First Committed Monooxygenase of Furanocoumarin Biosynthesis
    Journal of Biological Chemistry, 2007
    Co-Authors: Romain Larbat, Frederic Bourgaud, Alain Hehn, Joachim Hans, Sandra Kellner, Silvia Specker, Eric Gontier, Ulrich Matern

    Abstract:

    Ammi majus L. accumulates linear furanocoumarins by cyto-chrome P450 (CYP)-dependent conversion of 6-prenylumbellif-erone via ()-marmesin to psoralen. Relevant activities, i.e. pso-ralen synthase, are induced rapidly from negligible background levels upon elicitation of A. majus cultures with transient maxima at 9 –10 h and were recovered in labile microsomes. Expressed sequence tags were cloned from elicited Ammi cells by a nested DD-RT-PCR strategy with CYP-specific primers, and full-size cDNAs were generated from those fragments correlated in abundance with the induction profile of furanocou-marin-specific activities. One of these cDNAs representing a transcript of maximal abundance at 4 h of elicitation was assigned CYP71AJ1. Functional expression in Escherichia coli or yeast cells initially failed but was accomplished eventually in yeast cells after swapping the N-terminal membrane anchor domain with that of CYP73A1. The recombinant enzyme was identified as psoralen synthase with narrow substrate specificity for ()-marmesin. Psoralen synthase catalyzes a unique carbon-chain cleavage reaction concomitantly releasing acetone by syn-elimination. Related plants, i.e. Heracleum mantegazzianum, are known to produce both linear and angular furanocoumarins by analogous conversion of 8-prenylumbelliferone via ()-columbianetin to Angelicin, and it was suggested that Angelicin synthase has evolved from psoralen synthase. However, ()-columbianetin failed as sub-strate but competitively inhibited psoralen synthase activity. Analogy modeling and docked solutions defined the conditions for high affinity substrate binding and predicted the minimal requirements to accommodate ()-columbianetin in the active site cavity. The studies suggested that several point mutations are necessary to pave the road toward Angelicin synthase evolution.

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Ulrich Matern – One of the best experts on this subject based on the ideXlab platform.

  • Isolation and Functional Characterization of CYP71AJ4 Encoding for the First P450 Monooxygenase of Angular Furanocoumarin Biosynthesis
    Journal of Biological Chemistry, 2009
    Co-Authors: Romain Larbat, Alain Hehn, Joachim Hans, Sarah Schneider, Hélène Jugdé, Bernd Schneider, Ulrich Matern, Frederic Bourgaud

    Abstract:

    The biosynthesis of linear and angular furanocoumarins is still poorly understood at the molecular level, with only psoralen synthase (CYP71AJ1) identified from Ammi majus. Using cDNA probes inferred from CYP71AJ1, three orthologs were isolated from Apium graveolens (CYP71AJ2) and Pastinaca sativa (CYP71AJ3 and-4) and functionally expressed in yeast cells. CYP71AJ2 and CYP71AJ3 displayed psoralen synthase activity, whereas CYP71AJ4 only catalyzed the conversion of ()-colum-bianetin to Angelicin and negligible amounts of a hydroxylated columbianetin by-product. CYP71AJ4 thus constitutes the first fully characterized P450 monooxygenase specific for the angular furanocoumarin pathway. The Angelicin synthase exhibited an apparent K m of 2.1 0.4 M for ()-columbianetin and a k cat of 112 14 min 1. Moreover, the use of 3-deuterated ()-columbianetin as substrate led to an almost complete ” metabolic switch, ” resulting in the synthesis of anti-3-hydroxy-3-deuterated()-columbianetin. This confirms that Angelicin synthase attacks columbianetin by syn-elimination of hydrogen from C-3. Sequence comparison between psoralen synthase (CYP71AJ3) and Angelicin synthase (CYP71AJ4) showed 70% identity, whereas the identity dropped to 40% in those regions thought to provide the substrate recognition sites. Accordingly, CYP71AJ3 and CYP71AJ4 might be derived from a common ancestor of unknown functionality by gene duplication and subsequent molecular evolution. Furanocoumarins are natural plant metabolites characterized by a furane moiety fused to benzopyran-2-one. The position of the furane substitution distinguishes two large groups of compounds, the linear (psoralens) and the angular furanocou-marins (Angelicin and derivatives) (Fig.

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  • Isolation and Functional Characterization of CYP71AJ4 Encoding for the First P450 Monooxygenase of Angular Furanocoumarin Biosynthesis
    Journal of Biological Chemistry, 2008
    Co-Authors: Romain Larbat, Alain Hehn, Joachim Hans, Sarah Schneider, Hélène Jugdé, Bernd Schneider, Ulrich Matern, Frederic Bourgaud

    Abstract:

    The biosynthesis of linear and angular furanocoumarins is still poorly understood at the molecular level, with only psoralen synthase (CYP71AJ1) identified from Ammi majus. Using cDNA probes inferred from CYP71AJ1, three orthologs were isolated from Apium graveolens (CYP71AJ2) and Pastinaca sativa (CYP71AJ3 and -4) and functionally expressed in yeast cells. CYP71AJ2 and CYP71AJ3 displayed psoralen synthase activity, whereas CYP71AJ4 only catalyzed the conversion of (+)-columbianetin to Angelicin and negligible amounts of a hydroxylated columbianetin by-product. CYP71AJ4 thus constitutes the first fully characterized P450 monooxygenase specific for the angular furanocoumarin pathway. The Angelicin synthase exhibited an apparent K(m) of 2.1 +/- 0.4 microm for (+)-columbianetin and a k(cat) of 112 +/- 14 min(-1). Moreover, the use of 3′-deuterated (+)-columbianetin as substrate led to an almost complete “metabolic switch,” resulting in the synthesis of anti-3′-hydroxy-3′-deuterated(+)-columbianetin. This confirms that Angelicin synthase attacks columbianetin by syn-elimination of hydrogen from C-3′. Sequence comparison between psoralen synthase (CYP71AJ3) and Angelicin synthase (CYP71AJ4) showed 70% identity, whereas the identity dropped to 40% in those regions thought to provide the substrate recognition sites. Accordingly, CYP71AJ3 and CYP71AJ4 might be derived from a common ancestor of unknown functionality by gene duplication and subsequent molecular evolution.

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  • Molecular Cloning and Functional Characterization of Psoralen Synthase, the First Committed Monooxygenase of Furanocoumarin Biosynthesis
    Journal of Biological Chemistry, 2007
    Co-Authors: Romain Larbat, Frederic Bourgaud, Alain Hehn, Joachim Hans, Sandra Kellner, Silvia Specker, Eric Gontier, Ulrich Matern

    Abstract:

    Ammi majus L. accumulates linear furanocoumarins by cyto-chrome P450 (CYP)-dependent conversion of 6-prenylumbellif-erone via ()-marmesin to psoralen. Relevant activities, i.e. pso-ralen synthase, are induced rapidly from negligible background levels upon elicitation of A. majus cultures with transient maxima at 9 –10 h and were recovered in labile microsomes. Expressed sequence tags were cloned from elicited Ammi cells by a nested DD-RT-PCR strategy with CYP-specific primers, and full-size cDNAs were generated from those fragments correlated in abundance with the induction profile of furanocou-marin-specific activities. One of these cDNAs representing a transcript of maximal abundance at 4 h of elicitation was assigned CYP71AJ1. Functional expression in Escherichia coli or yeast cells initially failed but was accomplished eventually in yeast cells after swapping the N-terminal membrane anchor domain with that of CYP73A1. The recombinant enzyme was identified as psoralen synthase with narrow substrate specificity for ()-marmesin. Psoralen synthase catalyzes a unique carbon-chain cleavage reaction concomitantly releasing acetone by syn-elimination. Related plants, i.e. Heracleum mantegazzianum, are known to produce both linear and angular furanocoumarins by analogous conversion of 8-prenylumbelliferone via ()-columbianetin to Angelicin, and it was suggested that Angelicin synthase has evolved from psoralen synthase. However, ()-columbianetin failed as sub-strate but competitively inhibited psoralen synthase activity. Analogy modeling and docked solutions defined the conditions for high affinity substrate binding and predicted the minimal requirements to accommodate ()-columbianetin in the active site cavity. The studies suggested that several point mutations are necessary to pave the road toward Angelicin synthase evolution.

    Free Register to Access Article