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Literature summary extracted from

  • Gorinova, N.; Nedkovska, M.; Atanassov, A.
    Cytochrome P450 monooxygenase as a tool for metabolizing of herbicides in plants (2005), Biotechnol. Biotechnol. Equip., 19, 105-115.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.14.1 additional information chlorotoluron metabolism in sensitive plants is induced by blue light, induction of P450 in wounded tissues, all plant P450s depend on NADPH-cytochrome P450 reductase for providing the reducing equivalents needed to activate molecular oxygen, induction of the enzyme by light due to coupling of P450 monooxygenase to photosynthetic electron transfer systems in chloroplasts, overview Lolium rigidum
1.14.14.1 additional information induction of P450 in wounded tissues, all plant P450s depend on NADPH-cytochrome P450 reductase for providing the reducing equivalents needed to activate molecular oxygen, induction of the enzyme by light due to coupling of P450 monooxygenase to photosynthetic electron transfer systems in chloroplasts, overview Triticum aestivum
1.14.14.1 additional information induction of P450 in wounded tissues, all plant P450s depend on NADPH-cytochrome P450 reductase for providing the reducing equivalents needed to activate molecular oxygen, induction of the enzyme by light due to coupling of P450 monooxygenase to photosynthetic electron transfer systems in chloroplasts, overview Zea mays
1.14.14.1 additional information induction of P450 in wounded tissues, all plant P450s depend on NADPH-cytochrome P450 reductase for providing the reducing equivalents needed to activate molecular oxygen, induction of the enzyme by light due to coupling of P450 monooxygenase to photosynthetic electron transfer systems in chloroplasts, overview Solanum tuberosum
1.14.14.1 additional information induction of P450 in wounded tissues, all plant P450s depend on NADPH-cytochrome P450 reductase for providing the reducing equivalents needed to activate molecular oxygen, induction of the enzyme by light due to coupling of P450 monooxygenase to photosynthetic electron transfer systems in chloroplasts, overview Nicotiana tabacum
1.14.14.1 additional information induction of P450 in wounded tissues, all plant P450s depend on NADPH-cytochrome P450 reductase for providing the reducing equivalents needed to activate molecular oxygen, induction of the enzyme by light due to coupling of P450 monooxygenase to photosynthetic electron transfer systems in chloroplasts, overview Sorghum sp.
1.14.14.1 additional information induction of P450 in wounded tissues, all plant P450s depend on NADPH-cytochrome P450 reductase for providing the reducing equivalents needed to activate molecular oxygen, induction of the enzyme by light due to coupling of P450 monooxygenase to photosynthetic electron transfer systems in chloroplasts, overview Phelipanche ramosa

Application

EC Number Application Comment Organism
1.14.14.1 agriculture cytochrome P450 monooxygenase as a tool for metabolizing of herbicides in plants Solanum tuberosum
1.14.14.1 agriculture cytochrome P450 monooxygenase as a tool for metabolizing of herbicides in plants Nicotiana tabacum
1.14.14.1 agriculture the enzyme is of great importance commercially not only from the point of view of herbicide resistance but also in terms of ecotoxicology Triticum aestivum
1.14.14.1 agriculture the enzyme is of great importance commercially not only from the point of view of herbicide resistance but also in terms of ecotoxicology Zea mays
1.14.14.1 biotechnology cytochrome P450 monooxygenase as a tool for metabolizing of herbicides in plants Solanum tuberosum
1.14.14.1 biotechnology cytochrome P450 monooxygenase as a tool for metabolizing of herbicides in plants Nicotiana tabacum
1.14.14.1 environmental protection the enzyme is of great importance commercially not only from the point of view of herbicide resistance but also in terms of ecotoxicology Triticum aestivum
1.14.14.1 environmental protection the enzyme is of great importance commercially not only from the point of view of herbicide resistance but also in terms of ecotoxicology Zea mays
1.14.14.1 additional information the use of genetically engineered herbicide resistant plants is one of the most effective ways for broomrape control, since the parasitic plant damages the agriculturally important tobacco plants in Bulgaria, overview Phelipanche ramosa

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.1 expression of recombinant human P4502B6 and yeast reductase fused enzyme in transgenic tobacco plants, integration into the tobacco genome, functional expression of CYP1A1 and CYP1A1-yeast reductase fused enzyme in transgenic potato plants, genetic transformation is mediated by Agrobacterium tumefaciens Homo sapiens
1.14.14.1 functional expression of the fused enzyme between rat CYP1A1 and rat or yeast reductase in transgenic tobacco and potato plants mainly in microsomes Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
1.14.14.1 additional information construction of a fused enzyme between rat CYP1A1 and rat reductase on microsomes in the recombinant yeast cells, which showed enhanced specific activity as compared with the original enzyme system Rattus norvegicus
1.14.14.1 additional information the herbicide chlorotoluron delayed the germination and development of Orobanche ramosa seeds in case of use of transgenic plants tolerant to the herbicide Phelipanche ramosa
1.14.14.1 additional information transgenic potato plants expressing CYP1A1 and its fused enzyme with yeast reductase showed tolerance to the herbicide chlorotoluron, some of them are tolerant to the herbicides diuron and atrazine, the transgenic plants also show increased activity against 7-ethoxycoumarin, overview Solanum tuberosum
1.14.14.1 additional information transgenic tobacco plants expressing rat CYP1A1 and its fused enzyme with yeast reductase showed tolerance to the herbicide chlorotoluron, some of them are tolerant to the herbicides diuron and atrazine, the transgenic plants also show increased activity against 7-ethoxycoumarin, overview Nicotiana tabacum

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.1 Atrazine a herbicide Nicotiana tabacum
1.14.14.1 Atrazine a herbicide Solanum tuberosum
1.14.14.1 chlorotoluron metabolism in sensitive plants is induced by blue light Lolium rigidum
1.14.14.1 chlorotoluron a herbicide Nicotiana tabacum
1.14.14.1 chlorotoluron chlorotoluron treatment of the transgenic plants could lead to inhibition of the germination of broomrape, overview Phelipanche ramosa
1.14.14.1 chlorotoluron a herbicide Solanum tuberosum
1.14.14.1 Diuron a herbicide Nicotiana tabacum
1.14.14.1 Diuron a herbicide Solanum tuberosum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.14.1 microsome membrane-bound Homo sapiens
-
-
1.14.14.1 microsome membrane-bound Rattus norvegicus
-
-
1.14.14.1 microsome membrane-bound Triticum aestivum
-
-
1.14.14.1 microsome membrane-bound Zea mays
-
-
1.14.14.1 microsome membrane-bound Solanum tuberosum
-
-
1.14.14.1 microsome membrane-bound Nicotiana tabacum
-
-
1.14.14.1 microsome membrane-bound Sorghum sp.
-
-
1.14.14.1 microsome membrane-bound Phelipanche ramosa
-
-
1.14.14.1 microsome membrane-bound Lolium rigidum
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.14.1 Fe2+ heme iron Homo sapiens
1.14.14.1 Fe2+ heme iron Rattus norvegicus
1.14.14.1 Fe2+ heme iron Triticum aestivum
1.14.14.1 Fe2+ heme iron Zea mays
1.14.14.1 Fe2+ heme iron Solanum tuberosum
1.14.14.1 Fe2+ heme iron Nicotiana tabacum
1.14.14.1 Fe2+ heme iron Sorghum sp.
1.14.14.1 Fe2+ heme iron Phelipanche ramosa
1.14.14.1 Fe2+ heme iron Lolium rigidum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.1 7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2 Rattus norvegicus wild-type enzyme and recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants 7-hydroxycoumarin + [oxidized NADPH-hemoprotein reductase] + H2O + ?
-
?
1.14.14.1 7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2 Homo sapiens wild-type enzyme and recombinant enzyme P4502B6 fused to yeast reductase and expressed in transgenic tobacco plants 7-hydroxycoumarin + [oxidized NADPH-hemoprotein reductase] + H2O + ?
-
?
1.14.14.1 bentazon + [reduced NADPH-hemoprotein reductase] + O2 Zea mays ring-hydroxylation ?
-
?
1.14.14.1 benzo-pyrene + [reduced NADPH-hemoprotein reductase] + O2 Rattus norvegicus recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants ?
-
?
1.14.14.1 chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 Triticum aestivum a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group ?
-
?
1.14.14.1 chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 Solanum tuberosum a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group ?
-
?
1.14.14.1 chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 Nicotiana tabacum a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group ?
-
?
1.14.14.1 chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 Rattus norvegicus a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group, recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants ?
-
?
1.14.14.1 chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 Homo sapiens recombinant wild-type enzyme and enzyme mutant fused to yeast reductase expressed in transgenic potato plants ?
-
?
1.14.14.1 chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 Zea mays ring methyl-hydroxylation ?
-
?
1.14.14.1 chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 Lolium rigidum ring methyl-hydroxylation ?
-
?
1.14.14.1 diclofop + [reduced NADPH-hemoprotein reductase] + O2 Triticum aestivum ring-hydroxylation ?
-
?
1.14.14.1 metolachlor + [reduced NADPH-hemoprotein reductase] + O2 Sorghum sp. de-ethylation ?
-
?
1.14.14.1 additional information Triticum aestivum the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview ?
-
?
1.14.14.1 additional information Zea mays the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview ?
-
?
1.14.14.1 additional information Solanum tuberosum the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview ?
-
?
1.14.14.1 additional information Nicotiana tabacum the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview ?
-
?
1.14.14.1 additional information Sorghum sp. the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview ?
-
?
1.14.14.1 additional information Phelipanche ramosa the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview ?
-
?
1.14.14.1 additional information Lolium rigidum the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.1 Homo sapiens
-
-
-
1.14.14.1 Lolium rigidum
-
-
-
1.14.14.1 Nicotiana tabacum
-
-
-
1.14.14.1 Phelipanche ramosa
-
broomrape, a root parasitic weed often in tobacco plants
-
1.14.14.1 Rattus norvegicus
-
-
-
1.14.14.1 Solanum tuberosum
-
-
-
1.14.14.1 Sorghum sp.
-
-
-
1.14.14.1 Triticum aestivum
-
-
-
1.14.14.1 Zea mays
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.14.1 RH + [reduced NADPH-hemoprotein reductase] + O2 = ROH + [oxidized NADPH-hemoprotein reductase] + H2O reaction mechanism Triticum aestivum
1.14.14.1 RH + [reduced NADPH-hemoprotein reductase] + O2 = ROH + [oxidized NADPH-hemoprotein reductase] + H2O reaction mechanism Zea mays
1.14.14.1 RH + [reduced NADPH-hemoprotein reductase] + O2 = ROH + [oxidized NADPH-hemoprotein reductase] + H2O reaction mechanism Solanum tuberosum
1.14.14.1 RH + [reduced NADPH-hemoprotein reductase] + O2 = ROH + [oxidized NADPH-hemoprotein reductase] + H2O reaction mechanism Nicotiana tabacum
1.14.14.1 RH + [reduced NADPH-hemoprotein reductase] + O2 = ROH + [oxidized NADPH-hemoprotein reductase] + H2O reaction mechanism Sorghum sp.
1.14.14.1 RH + [reduced NADPH-hemoprotein reductase] + O2 = ROH + [oxidized NADPH-hemoprotein reductase] + H2O reaction mechanism Phelipanche ramosa
1.14.14.1 RH + [reduced NADPH-hemoprotein reductase] + O2 = ROH + [oxidized NADPH-hemoprotein reductase] + H2O reaction mechanism Lolium rigidum

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.14.1 seed
-
Sorghum sp.
-
1.14.14.1 seed
-
Phelipanche ramosa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.1 7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2 wild-type enzyme and recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants Rattus norvegicus 7-hydroxycoumarin + [oxidized NADPH-hemoprotein reductase] + H2O + ?
-
?
1.14.14.1 7-ethoxycoumarin + [reduced NADPH-hemoprotein reductase] + O2 wild-type enzyme and recombinant enzyme P4502B6 fused to yeast reductase and expressed in transgenic tobacco plants Homo sapiens 7-hydroxycoumarin + [oxidized NADPH-hemoprotein reductase] + H2O + ?
-
?
1.14.14.1 bentazon + [reduced NADPH-hemoprotein reductase] + O2 ring-hydroxylation Zea mays ?
-
?
1.14.14.1 benzo-pyrene + [reduced NADPH-hemoprotein reductase] + O2 recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants Rattus norvegicus ?
-
?
1.14.14.1 chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group Triticum aestivum ?
-
?
1.14.14.1 chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group Solanum tuberosum ?
-
?
1.14.14.1 chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group Nicotiana tabacum ?
-
?
1.14.14.1 chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group, recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants Rattus norvegicus ?
-
?
1.14.14.1 chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 recombinant wild-type enzyme and enzyme mutant fused to yeast reductase expressed in transgenic potato plants Homo sapiens ?
-
?
1.14.14.1 chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 ring methyl-hydroxylation Zea mays ?
-
?
1.14.14.1 chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 ring methyl-hydroxylation Lolium rigidum ?
-
?
1.14.14.1 diclofop + [reduced NADPH-hemoprotein reductase] + O2 ring-hydroxylation Triticum aestivum ?
-
?
1.14.14.1 metolachlor + [reduced NADPH-hemoprotein reductase] + O2 de-ethylation Sorghum sp. ?
-
?
1.14.14.1 additional information the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview Triticum aestivum ?
-
?
1.14.14.1 additional information the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview Zea mays ?
-
?
1.14.14.1 additional information the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview Solanum tuberosum ?
-
?
1.14.14.1 additional information the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview Nicotiana tabacum ?
-
?
1.14.14.1 additional information the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview Sorghum sp. ?
-
?
1.14.14.1 additional information the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview Phelipanche ramosa ?
-
?
1.14.14.1 additional information the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview Lolium rigidum ?
-
?

Subunits

EC Number Subunits Comment Organism
1.14.14.1 More the enzyme is a membrane-bound heme protein, that consists of a protoporphyrin IX and an apoprotein, which confers the substrate specificity Triticum aestivum
1.14.14.1 More the enzyme is a membrane-bound heme protein, that consists of a protoporphyrin IX and an apoprotein, which confers the substrate specificity Zea mays
1.14.14.1 More the enzyme is a membrane-bound heme protein, that consists of a protoporphyrin IX and an apoprotein, which confers the substrate specificity Solanum tuberosum
1.14.14.1 More the enzyme is a membrane-bound heme protein, that consists of a protoporphyrin IX and an apoprotein, which confers the substrate specificity Nicotiana tabacum
1.14.14.1 More the enzyme is a membrane-bound heme protein, that consists of a protoporphyrin IX and an apoprotein, which confers the substrate specificity Sorghum sp.
1.14.14.1 More the enzyme is a membrane-bound heme protein, that consists of a protoporphyrin IX and an apoprotein, which confers the substrate specificity Phelipanche ramosa
1.14.14.1 More the enzyme is a membrane-bound heme protein, that consists of a protoporphyrin IX and an apoprotein, which confers the substrate specificity Lolium rigidum

Synonyms

EC Number Synonyms Comment Organism
1.14.14.1 Cyp
-
Homo sapiens
1.14.14.1 CYP1A1
-
Rattus norvegicus
1.14.14.1 cytochrome P450 monooxygenase
-
Homo sapiens
1.14.14.1 cytochrome P450 monooxygenase
-
Rattus norvegicus
1.14.14.1 cytochrome P450 monooxygenase
-
Triticum aestivum
1.14.14.1 cytochrome P450 monooxygenase
-
Zea mays
1.14.14.1 cytochrome P450 monooxygenase
-
Solanum tuberosum
1.14.14.1 cytochrome P450 monooxygenase
-
Nicotiana tabacum
1.14.14.1 cytochrome P450 monooxygenase
-
Sorghum sp.
1.14.14.1 cytochrome P450 monooxygenase
-
Phelipanche ramosa
1.14.14.1 cytochrome P450 monooxygenase
-
Lolium rigidum

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.1 FAD
-
Homo sapiens
1.14.14.1 FAD
-
Rattus norvegicus
1.14.14.1 FAD
-
Triticum aestivum
1.14.14.1 FAD
-
Zea mays
1.14.14.1 FAD
-
Solanum tuberosum
1.14.14.1 FAD
-
Nicotiana tabacum
1.14.14.1 FAD
-
Sorghum sp.
1.14.14.1 FAD
-
Phelipanche ramosa
1.14.14.1 FAD
-
Lolium rigidum
1.14.14.1 NADPH
-
Homo sapiens
1.14.14.1 NADPH
-
Rattus norvegicus
1.14.14.1 NADPH
-
Triticum aestivum
1.14.14.1 NADPH
-
Zea mays
1.14.14.1 NADPH
-
Solanum tuberosum
1.14.14.1 NADPH
-
Nicotiana tabacum
1.14.14.1 NADPH
-
Sorghum sp.
1.14.14.1 NADPH
-
Phelipanche ramosa
1.14.14.1 NADPH
-
Lolium rigidum