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Literature summary extracted from

  • Larbat, R.; Kellner, S.; Specker, S.; Hehn, A.; Gontier, E.; Hans, J.; Bourgaud, F.; Matern, U.
    Molecular cloning and functional characterization of psoralen synthase, the first committed monooxygenase of furanocoumarin biosynthesis (2007), J. Biol. Chem., 282, 542-554.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.14.141 additional information psoralen synthase is induced rapidly from negligible background levels upon elicitation, e.g. by crude Phytophthora sojae cell wall elicitor fraction, of cell cultures with transient maxima at 9-10 h, furanocoumarin composition in induced cells, overview Ammi majus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.141 gene CYP71AJ1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, functional expression of the wild-type enzyme in Escherichia coli and Saccharomyces cerevisiae strain WAT11 requiring swapping the N-terminal membrane anchor domain with that of CYP73A1, expression of the enzyme mutant in yeast cells Ammi majus

Protein Variants

EC Number Protein Variants Comment Organism
1.14.14.141 M120V site-directed mutagenesis Ammi majus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.141 (+)-columbianetin i.e. (+)-3,4,2',3'-D4-columbianetin, competitive inhibition, binds to the active site, analogy modeling and docking analysis, mechanism-based inactivation Ammi majus
1.14.14.141 additional information no inhibition by 5- and 8-methoxypsoralen, and angelicin Ammi majus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.14.141 0.0015
-
 (+)-marmesin pH 7.0, 27°C, recombinant enzyme in microsomes Ammi majus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.14.141 microsome
-
 Ammi majus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.14.141 Iron the psoralen synthase is a cytochrome-P450-dependent monooxygenase Ammi majus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.14.141 55891
-
 x * 55891, sequence calculation Ammi majus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.141 (+)-marmesin + [reduced NADPH-hemoprotein reductase] + O2 Ammi majus the enzyme is the first committed monooxygenase of linear furanocoumarin biosynthesis, pathway overview psoralen + [oxidized NADPH-hemoprotein reductase] + acetone + 2 H2O
-
 ?
1.14.14.141 5-hydroxymarmesin + [reduced NADPH-hemoprotein reductase] + O2 Ammi majus low activity, psoralen 5-monoxygenase activity bergaptol + acetone + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.141 Ammi majus Q6QNI4 CYP71AJ1; gene CYP71AJ1
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.14.141 native enzyme partially by preparation of microsomes Ammi majus

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.14.141 (+)-marmesin + [reduced NADPH-hemoprotein reductase] + O2 = psoralen + [oxidized NADPH-hemoprotein reductase] + acetone + 2 H2O reaction mechanism, analogy modeling and docking analysis of substrate binding, alignmant of recognition sites, modeling of the catalytic site, overview Ammi majus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.14.141 cell suspension culture
-
 Ammi majus
-
1.14.14.141 leaf
-
 Ammi majus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.141 (+)-marmesin + [reduced NADPH-hemoprotein reductase] + O2 the enzyme is the first committed monooxygenase of linear furanocoumarin biosynthesis, pathway overview Ammi majus psoralen + [oxidized NADPH-hemoprotein reductase] + acetone + 2 H2O
-
 ?
1.14.14.141 (+)-marmesin + [reduced NADPH-hemoprotein reductase] + O2 release of acetone by syn-elimination Ammi majus psoralen + [oxidized NADPH-hemoprotein reductase] + acetone + 2 H2O
-
 ?
1.14.14.141 5-hydroxymarmesin + [reduced NADPH-hemoprotein reductase] + O2 low activity, psoralen 5-monoxygenase activity Ammi majus bergaptol + acetone + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
1.14.14.141 additional information no activity with (+)-columbianetin, the psoralen synthase is a cytochrome-P450-dependent monooxygenase Ammi majus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.14.141 ? x * 55891, sequence calculation Ammi majus
1.14.14.141 More three-dimensional active site structure Ammi majus

Synonyms

EC Number Synonyms Comment Organism
1.14.14.141 CYP71AJ1
-
 Ammi majus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.14.141 27
-
 assay at Ammi majus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.14.141 340
-
 (+)-marmesin pH 7.0, 27°C, recombinant enzyme in microsomes Ammi majus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.14.141 7
-
 assay at Ammi majus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.141 additional information the psoralen synthase is a cytochrome-P450-dependent monooxygenase Ammi majus

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.14.14.141 Ammi majus sequence calculation
-
 6.49