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Literature summary for 1.14.14.1 extracted from
- 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
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 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 | |
| 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 | |
| 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 | |
| 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 | |
| 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 | |
| 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. | |
| 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
| Application | Comment | Organism |
|---|---|---|
| agriculture | cytochrome P450 monooxygenase as a tool for metabolizing of herbicides in plants | Solanum tuberosum |
| agriculture | cytochrome P450 monooxygenase as a tool for metabolizing of herbicides in plants | Nicotiana tabacum |
| 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 |
| 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 |
| biotechnology | cytochrome P450 monooxygenase as a tool for metabolizing of herbicides in plants | Solanum tuberosum |
| biotechnology | cytochrome P450 monooxygenase as a tool for metabolizing of herbicides in plants | Nicotiana tabacum |
| 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 |
| 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 |
| 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)
| Cloned (Comment) | Organism |
|---|---|
| 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 |
| 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
| Protein Variants | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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 |
| 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
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Atrazine | a herbicide | Nicotiana tabacum |  |
| Atrazine | a herbicide | Solanum tuberosum | |
| chlorotoluron | metabolism in sensitive plants is induced by blue light | Lolium rigidum | |
| chlorotoluron | a herbicide | Nicotiana tabacum | |
| chlorotoluron | chlorotoluron treatment of the transgenic plants could lead to inhibition of the germination of broomrape, overview | Phelipanche ramosa | |
| chlorotoluron | a herbicide | Solanum tuberosum | |
| Diuron | a herbicide | Nicotiana tabacum | |
| Diuron | a herbicide | Solanum tuberosum | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| microsome | membrane-bound | Homo sapiens | - |
- |
| microsome | membrane-bound | Rattus norvegicus | - |
- |
| microsome | membrane-bound | Triticum aestivum | - |
- |
| microsome | membrane-bound | Zea mays | - |
- |
| microsome | membrane-bound | Solanum tuberosum | - |
- |
| microsome | membrane-bound | Nicotiana tabacum | - |
- |
| microsome | membrane-bound | Sorghum sp. | - |
- |
| microsome | membrane-bound | Phelipanche ramosa | - |
- |
| microsome | membrane-bound | Lolium rigidum | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | heme iron | Homo sapiens | |
| Fe2+ | heme iron | Rattus norvegicus | |
| Fe2+ | heme iron | Triticum aestivum | |
| Fe2+ | heme iron | Zea mays | |
| Fe2+ | heme iron | Solanum tuberosum | |
| Fe2+ | heme iron | Nicotiana tabacum | |
| Fe2+ | heme iron | Sorghum sp. | |
| Fe2+ | heme iron | Phelipanche ramosa | |
| Fe2+ | heme iron | Lolium rigidum | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 + ? | - |
? | |
| 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 + ? | - |
? | |
| bentazon + [reduced NADPH-hemoprotein reductase] + O2 | Zea mays | ring-hydroxylation | ? | - |
? | |
| benzo-pyrene + [reduced NADPH-hemoprotein reductase] + O2 | Rattus norvegicus | recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants | ? | - |
? | |
| chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 | Triticum aestivum | a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group | ? | - |
? | |
| chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 | Solanum tuberosum | a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group | ? | - |
? | |
| chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 | Nicotiana tabacum | a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group | ? | - |
? | |
| 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 | ? | - |
? | |
| chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 | Homo sapiens | recombinant wild-type enzyme and enzyme mutant fused to yeast reductase expressed in transgenic potato plants | ? | - |
? | |
| chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 | Zea mays | ring methyl-hydroxylation | ? | - |
? | |
| chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 | Lolium rigidum | ring methyl-hydroxylation | ? | - |
? | |
| diclofop + [reduced NADPH-hemoprotein reductase] + O2 | Triticum aestivum | ring-hydroxylation | ? | - |
? | |
| metolachlor + [reduced NADPH-hemoprotein reductase] + O2 | Sorghum sp. | de-ethylation | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
| Lolium rigidum | - |
- |
- |
| Nicotiana tabacum | - |
- |
- |
| Phelipanche ramosa | - |
broomrape, a root parasitic weed often in tobacco plants | - |
| Rattus norvegicus | - |
- |
- |
| Solanum tuberosum | - |
- |
- |
| Sorghum sp. | - |
- |
- |
| Triticum aestivum | - |
- |
- |
| Zea mays | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| RH + [reduced NADPH-hemoprotein reductase] + O2 = ROH + [oxidized NADPH-hemoprotein reductase] + H2O | reaction mechanism | Triticum aestivum | |
| RH + [reduced NADPH-hemoprotein reductase] + O2 = ROH + [oxidized NADPH-hemoprotein reductase] + H2O | reaction mechanism | Zea mays | |
| RH + [reduced NADPH-hemoprotein reductase] + O2 = ROH + [oxidized NADPH-hemoprotein reductase] + H2O | reaction mechanism | Solanum tuberosum | |
| RH + [reduced NADPH-hemoprotein reductase] + O2 = ROH + [oxidized NADPH-hemoprotein reductase] + H2O | reaction mechanism | Nicotiana tabacum | |
| RH + [reduced NADPH-hemoprotein reductase] + O2 = ROH + [oxidized NADPH-hemoprotein reductase] + H2O | reaction mechanism | Sorghum sp. | |
| RH + [reduced NADPH-hemoprotein reductase] + O2 = ROH + [oxidized NADPH-hemoprotein reductase] + H2O | reaction mechanism | Phelipanche ramosa | |
| RH + [reduced NADPH-hemoprotein reductase] + O2 = ROH + [oxidized NADPH-hemoprotein reductase] + H2O | reaction mechanism | Lolium rigidum |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| seed | - |
Sorghum sp. | - |
| seed | - |
Phelipanche ramosa | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 + ? | - |
? | |
| 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 + ? | - |
? | |
| bentazon + [reduced NADPH-hemoprotein reductase] + O2 | ring-hydroxylation | Zea mays | ? | - |
? | |
| benzo-pyrene + [reduced NADPH-hemoprotein reductase] + O2 | recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants | Rattus norvegicus | ? | - |
? | |
| chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 | a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group | Triticum aestivum | ? | - |
? | |
| chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 | a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group | Solanum tuberosum | ? | - |
? | |
| chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 | a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group | Nicotiana tabacum | ? | - |
? | |
| 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 | ? | - |
? | |
| chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 | recombinant wild-type enzyme and enzyme mutant fused to yeast reductase expressed in transgenic potato plants | Homo sapiens | ? | - |
? | |
| chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 | ring methyl-hydroxylation | Zea mays | ? | - |
? | |
| chlorotoluron + [reduced NADPH-hemoprotein reductase] + O2 | ring methyl-hydroxylation | Lolium rigidum | ? | - |
? | |
| diclofop + [reduced NADPH-hemoprotein reductase] + O2 | ring-hydroxylation | Triticum aestivum | ? | - |
? | |
| metolachlor + [reduced NADPH-hemoprotein reductase] + O2 | de-ethylation | Sorghum sp. | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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. | ? | - |
? | |
| 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 | ? | - |
? | |
| 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
| Subunits | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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 |
| 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 |
| 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. |
| 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 |
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| Cyp | - |
Homo sapiens |
| CYP1A1 | - |
Rattus norvegicus |
| cytochrome P450 monooxygenase | - |
Homo sapiens |
| cytochrome P450 monooxygenase | - |
Rattus norvegicus |
| cytochrome P450 monooxygenase | - |
Triticum aestivum |
| cytochrome P450 monooxygenase | - |
Zea mays |
| cytochrome P450 monooxygenase | - |
Solanum tuberosum |
| cytochrome P450 monooxygenase | - |
Nicotiana tabacum |
| cytochrome P450 monooxygenase | - |
Sorghum sp. |
| cytochrome P450 monooxygenase | - |
Phelipanche ramosa |
| cytochrome P450 monooxygenase | - |
Lolium rigidum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
Homo sapiens | |
| FAD | - |
Rattus norvegicus | |
| FAD | - |
Triticum aestivum | |
| FAD | - |
Zea mays | |
| FAD | - |
Solanum tuberosum | |
| FAD | - |
Nicotiana tabacum | |
| FAD | - |
Sorghum sp. | |
| FAD | - |
Phelipanche ramosa | |
| FAD | - |
Lolium rigidum | |
| NADPH | - |
Homo sapiens | |
| NADPH | - |
Rattus norvegicus | |
| NADPH | - |
Triticum aestivum | |
| NADPH | - |
Zea mays | |
| NADPH | - |
Solanum tuberosum | |
| NADPH | - |
Nicotiana tabacum | |
| NADPH | - |
Sorghum sp. | |
| NADPH | - |
Phelipanche ramosa | |
| NADPH | - |
Lolium rigidum | |
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