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Literature summary for 1.14.14.141 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
Search for more literature for 1.14.14.141

Activating Compound

Activating Compound Comment Organism Structure
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)

Cloned (Comment) Organism
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

Protein Variants Comment Organism
M120V site-directed mutagenesis Ammi majus

Inhibitors

Inhibitors Comment Organism Structure
(+)-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
additional information no inhibition by 5- and 8-methoxypsoralen, and angelicin Ammi majus

KM Value [mM]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
 Ammi majus
-
-

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(+)-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
-
 ?
5-hydroxymarmesin + [reduced NADPH-hemoprotein reductase] + O2 Ammi majus low activity, psoralen 5-monoxygenase activity bergaptol + acetone + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Ammi majus Q6QNI4 CYP71AJ1; gene CYP71AJ1
-

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
(+)-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

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
CYP71AJ1
-
 Ammi majus

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

Cofactor

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

pI Value

Organism Comment pI Value Maximum pI Value
Ammi majus sequence calculation
-
 6.49