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Literature summary extracted from
- Fungal lanosterol 14alpha-demethylase a target for next-generation antifungal design (2020), Biochim. Biophys. Acta, 1868, 140206.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 1.14.14.154 | agriculture | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of the azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Candida albicans |
| 1.14.14.154 | agriculture | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Nakaseomyces glabratus |
| 1.14.14.154 | agriculture | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Saccharomyces cerevisiae |
| 1.14.14.154 | agriculture | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Aspergillus fumigatus |
| 1.14.14.154 | agriculture | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Phanerodontia chrysosporium |
| 1.14.14.154 | agriculture | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Rhodonia placenta |
| 1.14.14.154 | agriculture | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Puccinia sp. |
| 1.14.14.154 | agriculture | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of the azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Zymoseptoria tritici |
| 1.14.14.154 | agriculture | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Pseudocercospora musae |
| 1.14.14.154 | agriculture | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Fusarium oxysporum |
| 1.14.14.154 | agriculture | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Pyricularia oryzae |
| 1.14.14.154 | agriculture | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Aspergillus flavus |
| 1.14.14.154 | agriculture | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Aspergillus parasiticus |
| 1.14.14.154 | agriculture | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Cryptococcus neoformans |
| 1.14.14.154 | analysis | DELTAERG11-DELTAERG3 mutants may be used to confirm the specificity of potential LDM inhibitors expressing LDMs from other species | Saccharomyces cerevisiae |
| 1.14.14.154 | medicine | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of the azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Candida albicans |
| 1.14.14.154 | medicine | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Nakaseomyces glabratus |
| 1.14.14.154 | medicine | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Saccharomyces cerevisiae |
| 1.14.14.154 | medicine | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Aspergillus fumigatus |
| 1.14.14.154 | medicine | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Phanerodontia chrysosporium |
| 1.14.14.154 | medicine | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Rhodonia placenta |
| 1.14.14.154 | medicine | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Puccinia sp. |
| 1.14.14.154 | medicine | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of the azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Zymoseptoria tritici |
| 1.14.14.154 | medicine | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Pseudocercospora musae |
| 1.14.14.154 | medicine | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Fusarium oxysporum |
| 1.14.14.154 | medicine | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Pyricularia oryzae |
| 1.14.14.154 | medicine | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Aspergillus flavus |
| 1.14.14.154 | medicine | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Aspergillus parasiticus |
| 1.14.14.154 | medicine | the cytochrome P450 enzyme lanosterol 14alpha-demethylase (LDM) is the target of azole antifungals used widely in medicine and agriculture as prophylaxis or treatments of infections or diseases caused by fungal pathogens. These drugs and agrochemicals contain an imidazole, triazole or tetrazole substituent, with one of the nitrogens in the azole ring coordinating as the sixth axial ligand to the LDM. Generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance | Cryptococcus neoformans |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.14.154 | gene CYP51, recombinant expression in Escherichia coli | Phanerodontia chrysosporium |
| 1.14.14.154 | gene CYP51, recombinant expression in Escherichia coli | Rhodonia placenta |
| 1.14.14.154 | gene ERG11, constitutive, functional overexpression of full-length, recombinant, C-terminally His6-tagged enzyme ScLDM from the PDR5 locus in Saccharomyces cerevisiae | Saccharomyces cerevisiae |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.14.14.154 | crystal structure of the LDM catalytic domain | Aspergillus fumigatus |
| 1.14.14.154 | crystal structures analysis | Saccharomyces cerevisiae |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.154 | clotrimazole | - |
Candida albicans |  |
| 1.14.14.154 | clotrimazole | - |
Nakaseomyces glabratus | |
| 1.14.14.154 | difenoconazole | - |
Aspergillus flavus | |
| 1.14.14.154 | difenoconazole | - |
Aspergillus fumigatus | |
| 1.14.14.154 | difenoconazole | - |
Aspergillus parasiticus | |
| 1.14.14.154 | difenoconazole | - |
Candida albicans | |
| 1.14.14.154 | difenoconazole | - |
Cryptococcus neoformans | |
| 1.14.14.154 | difenoconazole | - |
Fusarium oxysporum | |
| 1.14.14.154 | difenoconazole | - |
Nakaseomyces glabratus | |
| 1.14.14.154 | difenoconazole | - |
Phanerodontia chrysosporium | |
| 1.14.14.154 | difenoconazole | - |
Pseudocercospora musae | |
| 1.14.14.154 | difenoconazole | - |
Puccinia sp. | |
| 1.14.14.154 | difenoconazole | - |
Pyricularia oryzae | |
| 1.14.14.154 | difenoconazole | - |
Rhodonia placenta | |
| 1.14.14.154 | difenoconazole | - |
Saccharomyces cerevisiae | |
| 1.14.14.154 | difenoconazole | - |
Zymoseptoria tritici | |
| 1.14.14.154 | epoxiconazole | - |
Aspergillus flavus | |
| 1.14.14.154 | epoxiconazole | - |
Aspergillus parasiticus | |
| 1.14.14.154 | epoxiconazole | - |
Candida albicans | |
| 1.14.14.154 | epoxiconazole | - |
Fusarium oxysporum | |
| 1.14.14.154 | epoxiconazole | - |
Pseudocercospora musae | |
| 1.14.14.154 | epoxiconazole | - |
Puccinia sp. | |
| 1.14.14.154 | epoxiconazole | - |
Pyricularia oryzae | |
| 1.14.14.154 | epoxiconazole | - |
Zymoseptoria tritici | |
| 1.14.14.154 | fluconazole | - |
Aspergillus flavus | |
| 1.14.14.154 | fluconazole | - |
Aspergillus fumigatus | |
| 1.14.14.154 | fluconazole | - |
Aspergillus parasiticus | |
| 1.14.14.154 | fluconazole | - |
Candida albicans | |
| 1.14.14.154 | fluconazole | - |
Cryptococcus neoformans | |
| 1.14.14.154 | fluconazole | - |
Fusarium oxysporum | |
| 1.14.14.154 | fluconazole | - |
Nakaseomyces glabratus | |
| 1.14.14.154 | fluconazole | - |
Phanerodontia chrysosporium | |
| 1.14.14.154 | fluconazole | - |
Pseudocercospora musae | |
| 1.14.14.154 | fluconazole | - |
Puccinia sp. | |
| 1.14.14.154 | fluconazole | - |
Pyricularia oryzae | |
| 1.14.14.154 | fluconazole | - |
Rhodonia placenta | |
| 1.14.14.154 | fluconazole | - |
Saccharomyces cerevisiae | |
| 1.14.14.154 | fluconazole | - |
Zymoseptoria tritici | |
| 1.14.14.154 | itraconazole | - |
Aspergillus flavus | |
| 1.14.14.154 | itraconazole | - |
Aspergillus fumigatus | |
| 1.14.14.154 | itraconazole | - |
Aspergillus parasiticus | |
| 1.14.14.154 | itraconazole | - |
Candida albicans | |
| 1.14.14.154 | itraconazole | - |
Cryptococcus neoformans | |
| 1.14.14.154 | itraconazole | - |
Fusarium oxysporum | |
| 1.14.14.154 | itraconazole | - |
Nakaseomyces glabratus | |
| 1.14.14.154 | itraconazole | - |
Phanerodontia chrysosporium | |
| 1.14.14.154 | itraconazole | - |
Pseudocercospora musae | |
| 1.14.14.154 | itraconazole | - |
Puccinia sp. | |
| 1.14.14.154 | itraconazole | - |
Pyricularia oryzae | |
| 1.14.14.154 | itraconazole | - |
Rhodonia placenta | |
| 1.14.14.154 | itraconazole | - |
Saccharomyces cerevisiae | |
| 1.14.14.154 | itraconazole | - |
Zymoseptoria tritici | |
| 1.14.14.154 | ketoconazole | - |
Candida albicans | |
| 1.14.14.154 | ketoconazole | - |
Cryptococcus neoformans | |
| 1.14.14.154 | ketoconazole | - |
Nakaseomyces glabratus | |
| 1.14.14.154 | miconazole | not effective against moulds | Candida albicans | |
| 1.14.14.154 | miconazole | not effective against moulds | Nakaseomyces glabratus | |
| 1.14.14.154 | additional information | generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance. Structure-directed drug discovery, overview. Measurements of type I and type II binding of substrates and azole drugs. Measurement of on and off rates for ligands using surface plasmon resonance (SPR) biosensors with purified LDM covalently tethered to the optical surface allows the measurement of affinity constants unaffected by the protein concentration of the target enzyme, at least for the larger azole drugs such as difenconazole and itraconazole but not for fluconazole or voriconazole | Aspergillus flavus | |
| 1.14.14.154 | additional information | generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance. Structure-directed drug discovery, overview. Measurements of type I and type II binding of substrates and azole drugs. Measurement of on and off rates for ligands using surface plasmon resonance (SPR) biosensors with purified LDM covalently tethered to the optical surface allows the measurement of affinity constants unaffected by the protein concentration of the target enzyme, at least for the larger azole drugs such as difenconazole and itraconazole but not for fluconazole or voriconazole; generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance. Structure-directed drug discovery, overview. Measurements of type I and type II binding of substrates and azole drugs. Measurement of on and off rates for ligands using surface plasmon resonance (SPR) biosensors with purified LDM covalently tethered to the optical surface allows the measurement of affinity constants unaffected by the protein concentration of the target enzyme, at least for the larger azole drugs such as difenconazole and itraconazole but not for fluconazole or voriconazole | Aspergillus fumigatus | |
| 1.14.14.154 | additional information | generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance. Structure-directed drug discovery, overview. Measurements of type I and type II binding of substrates and azole drugs. Measurement of on and off rates for ligands using surface plasmon resonance (SPR) biosensors with purified LDM covalently tethered to the optical surface allows the measurement of affinity constants unaffected by the protein concentration of the target enzyme, at least for the larger azole drugs such as difenconazole and itraconazole but not for fluconazole or voriconazole | Aspergillus parasiticus | |
| 1.14.14.154 | additional information | generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance. Structure-directed drug discovery, overview. Measurements of type I and type II binding of substrates and azole drugs. Measurement of on and off rates for ligands using surface plasmon resonance (SPR) biosensors with purified LDM covalently tethered to the optical surface allows the measurement of affinity constants unaffected by the protein concentration of the target enzyme, at least for the larger azole drugs such as difenconazole and itraconazole but not for fluconazole or voriconazole | Candida albicans | |
| 1.14.14.154 | additional information | generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance. Structure-directed drug discovery, overview. Measurements of type I and type II binding of substrates and azole drugs. Measurement of on and off rates for ligands using surface plasmon resonance (SPR) biosensors with purified LDM covalently tethered to the optical surface allows the measurement of affinity constants unaffected by the protein concentration of the target enzyme, at least for the larger azole drugs such as difenconazole and itraconazole but not for fluconazole or voriconazole | Cryptococcus neoformans | |
| 1.14.14.154 | additional information | generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance. Structure-directed drug discovery, overview. Measurements of type I and type II binding of substrates and azole drugs. Measurement of on and off rates for ligands using surface plasmon resonance (SPR) biosensors with purified LDM covalently tethered to the optical surface allows the measurement of affinity constants unaffected by the protein concentration of the target enzyme, at least for the larger azole drugs such as difenconazole and itraconazole but not for fluconazole or voriconazole | Fusarium oxysporum | |
| 1.14.14.154 | additional information | generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance. Structure-directed drug discovery, overview. Measurements of type I and type II binding of substrates and azole drugs. Measurement of on and off rates for ligands using surface plasmon resonance (SPR) biosensors with purified LDM covalently tethered to the optical surface allows the measurement of affinity constants unaffected by the protein concentration of the target enzyme, at least for the larger azole drugs such as difenconazole and itraconazole but not for fluconazole or voriconazole | Nakaseomyces glabratus | |
| 1.14.14.154 | additional information | generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance. Structure-directed drug discovery, overview. Measurements of type I and type II binding of substrates and azole drugs. Measurement of on and off rates for ligands using surface plasmon resonance (SPR) biosensors with purified LDM covalently tethered to the optical surface allows the measurement of affinity constants unaffected by the protein concentration of the target enzyme, at least for the larger azole drugs such as difenconazole and itraconazole but not for fluconazole or voriconazole | Phanerodontia chrysosporium | |
| 1.14.14.154 | additional information | generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance. Structure-directed drug discovery, overview. Measurements of type I and type II binding of substrates and azole drugs. Measurement of on and off rates for ligands using surface plasmon resonance (SPR) biosensors with purified LDM covalently tethered to the optical surface allows the measurement of affinity constants unaffected by the protein concentration of the target enzyme, at least for the larger azole drugs such as difenconazole and itraconazole but not for fluconazole or voriconazole | Pseudocercospora musae | |
| 1.14.14.154 | additional information | generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance. Structure-directed drug discovery, overview. Measurements of type I and type II binding of substrates and azole drugs. Measurement of on and off rates for ligands using surface plasmon resonance (SPR) biosensors with purified LDM covalently tethered to the optical surface allows the measurement of affinity constants unaffected by the protein concentration of the target enzyme, at least for the larger azole drugs such as difenconazole and itraconazole but not for fluconazole or voriconazole | Puccinia sp. | |
| 1.14.14.154 | additional information | generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance. Structure-directed drug discovery, overview. Measurements of type I and type II binding of substrates and azole drugs. Measurement of on and off rates for ligands using surface plasmon resonance (SPR) biosensors with purified LDM covalently tethered to the optical surface allows the measurement of affinity constants unaffected by the protein concentration of the target enzyme, at least for the larger azole drugs such as difenconazole and itraconazole but not for fluconazole or voriconazole | Pyricularia oryzae | |
| 1.14.14.154 | additional information | generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance. Structure-directed drug discovery, overview. Measurements of type I and type II binding of substrates and azole drugs. Measurement of on and off rates for ligands using surface plasmon resonance (SPR) biosensors with purified LDM covalently tethered to the optical surface allows the measurement of affinity constants unaffected by the protein concentration of the target enzyme, at least for the larger azole drugs such as difenconazole and itraconazole but not for fluconazole or voriconazole | Rhodonia placenta | |
| 1.14.14.154 | additional information | generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance. Structure-directed drug discovery, overview. Measurements of type I and type II binding of substrates and azole drugs. Measurement of on and off rates for ligands using surface plasmon resonance (SPR) biosensors with purified LDM covalently tethered to the optical surface allows the measurement of affinity constants unaffected by the protein concentration of the target enzyme, at least for the larger azole drugs such as difenconazole and itraconazole but not for fluconazole or voriconazole | Saccharomyces cerevisiae | |
| 1.14.14.154 | additional information | generation of antifungals targeting LDM, with the goal of obtaining highly potent broad-spectrum fungicides that will be able to avoid target- and drug-efflux mediated antifungal resistance. Structure-directed drug discovery, overview. Measurements of type I and type II binding of substrates and azole drugs. Measurement of on and off rates for ligands using surface plasmon resonance (SPR) biosensors with purified LDM covalently tethered to the optical surface allows the measurement of affinity constants unaffected by the protein concentration of the target enzyme, at least for the larger azole drugs such as difenconazole and itraconazole but not for fluconazole or voriconazole | Zymoseptoria tritici | |
| 1.14.14.154 | prothioconazole | is a prodrug, its conversion to the desthio form results in the active compound that inhibits LDM | Aspergillus flavus | |
| 1.14.14.154 | prothioconazole | is a prodrug, its conversion to the desthio form results in the active compound that inhibits LDM | Aspergillus parasiticus | |
| 1.14.14.154 | prothioconazole | is a prodrug, its conversion to the desthio form results in the active compound that inhibits LDM, acquisition of azole resistance in Candida albicans | Candida albicans | |
| 1.14.14.154 | prothioconazole | is a prodrug, its conversion to the desthio form results in the active compound that inhibits LDM | Cryptococcus neoformans | |
| 1.14.14.154 | prothioconazole | is a prodrug, its conversion to the desthio form results in the active compound that inhibits LDM | Fusarium oxysporum | |
| 1.14.14.154 | prothioconazole | is a prodrug, its conversion to the desthio form results in the active compound that inhibits LDM | Pseudocercospora musae | |
| 1.14.14.154 | prothioconazole | is a prodrug, its conversion to the desthio form results in the active compound that inhibits LDM | Puccinia sp. | |
| 1.14.14.154 | prothioconazole | is a prodrug, its conversion to the desthio form results in the active compound that inhibits LDM | Pyricularia oryzae | |
| 1.14.14.154 | prothioconazole | is a prodrug, its conversion to the desthio form results in the active compound that inhibits LDM | Saccharomyces cerevisiae | |
| 1.14.14.154 | prothioconazole | is a prodrug, its conversion to the desthio form results in the active compound that inhibits LDM | Zymoseptoria tritici | |
| 1.14.14.154 | tebuconazole | - |
Aspergillus flavus | |
| 1.14.14.154 | tebuconazole | - |
Aspergillus parasiticus | |
| 1.14.14.154 | tebuconazole | - |
Candida albicans | |
| 1.14.14.154 | tebuconazole | - |
Fusarium oxysporum | |
| 1.14.14.154 | tebuconazole | - |
Pseudocercospora musae | |
| 1.14.14.154 | tebuconazole | - |
Puccinia sp. | |
| 1.14.14.154 | tebuconazole | - |
Pyricularia oryzae | |
| 1.14.14.154 | tebuconazole | - |
Zymoseptoria tritici | |
| 1.14.14.154 | voriconazole | - |
Aspergillus flavus | |
| 1.14.14.154 | voriconazole | - |
Aspergillus fumigatus | |
| 1.14.14.154 | voriconazole | - |
Aspergillus parasiticus | |
| 1.14.14.154 | voriconazole | - |
Candida albicans | |
| 1.14.14.154 | voriconazole | - |
Cryptococcus neoformans | |
| 1.14.14.154 | voriconazole | - |
Fusarium oxysporum | |
| 1.14.14.154 | voriconazole | - |
Nakaseomyces glabratus | |
| 1.14.14.154 | voriconazole | - |
Phanerodontia chrysosporium | |
| 1.14.14.154 | voriconazole | - |
Pseudocercospora musae | |
| 1.14.14.154 | voriconazole | - |
Puccinia sp. | |
| 1.14.14.154 | voriconazole | - |
Pyricularia oryzae | |
| 1.14.14.154 | voriconazole | - |
Rhodonia placenta | |
| 1.14.14.154 | voriconazole | - |
Saccharomyces cerevisiae | |
| 1.14.14.154 | voriconazole | - |
Zymoseptoria tritici | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.14.14.154 | membrane | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane | Candida albicans | 16020 | - |
| 1.14.14.154 | membrane | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane | Nakaseomyces glabratus | 16020 | - |
| 1.14.14.154 | membrane | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane | Saccharomyces cerevisiae | 16020 | - |
| 1.14.14.154 | membrane | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane | Aspergillus fumigatus | 16020 | - |
| 1.14.14.154 | membrane | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane | Homo sapiens | 16020 | - |
| 1.14.14.154 | membrane | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane | Phanerodontia chrysosporium | 16020 | - |
| 1.14.14.154 | membrane | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane | Rhodonia placenta | 16020 | - |
| 1.14.14.154 | membrane | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane | Puccinia sp. | 16020 | - |
| 1.14.14.154 | membrane | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane | Zymoseptoria tritici | 16020 | - |
| 1.14.14.154 | membrane | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane | Pseudocercospora musae | 16020 | - |
| 1.14.14.154 | membrane | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane | Fusarium oxysporum | 16020 | - |
| 1.14.14.154 | membrane | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane | Pyricularia oryzae | 16020 | - |
| 1.14.14.154 | membrane | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane | Aspergillus flavus | 16020 | - |
| 1.14.14.154 | membrane | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane | Aspergillus parasiticus | 16020 | - |
| 1.14.14.154 | membrane | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane | Cryptococcus neoformans | 16020 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.154 | Fe2+ | in the cytochrome P450 heme | Aspergillus flavus | |
| 1.14.14.154 | Fe2+ | in the cytochrome P450 heme | Aspergillus fumigatus | |
| 1.14.14.154 | Fe2+ | in the cytochrome P450 heme | Aspergillus parasiticus | |
| 1.14.14.154 | Fe2+ | in the cytochrome P450 heme | Candida albicans | |
| 1.14.14.154 | Fe2+ | in the cytochrome P450 heme | Cryptococcus neoformans | |
| 1.14.14.154 | Fe2+ | in the cytochrome P450 heme | Fusarium oxysporum | |
| 1.14.14.154 | Fe2+ | in the cytochrome P450 heme | Homo sapiens | |
| 1.14.14.154 | Fe2+ | in the cytochrome P450 heme | Nakaseomyces glabratus | |
| 1.14.14.154 | Fe2+ | in the cytochrome P450 heme | Phanerodontia chrysosporium | |
| 1.14.14.154 | Fe2+ | in the cytochrome P450 heme | Pseudocercospora musae | |
| 1.14.14.154 | Fe2+ | in the cytochrome P450 heme | Puccinia sp. | |
| 1.14.14.154 | Fe2+ | in the cytochrome P450 heme | Pyricularia oryzae | |
| 1.14.14.154 | Fe2+ | in the cytochrome P450 heme | Rhodonia placenta | |
| 1.14.14.154 | Fe2+ | in the cytochrome P450 heme | Saccharomyces cerevisiae | |
| 1.14.14.154 | Fe2+ | in the cytochrome P450 heme | Zymoseptoria tritici | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.154 | a 14alpha-methylsteroid + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Homo sapiens | - |
a DELTA14-steroid + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Candida albicans | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Nakaseomyces glabratus | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Saccharomyces cerevisiae | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Aspergillus fumigatus | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Homo sapiens | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Phanerodontia chrysosporium | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Rhodonia placenta | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Puccinia sp. | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Zymoseptoria tritici | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Pseudocercospora musae | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Fusarium oxysporum | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Pyricularia oryzae | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Aspergillus flavus | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Aspergillus parasiticus | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Cryptococcus neoformans | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Aspergillus fumigatus Af293 | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Candida albicans ATCC MYA-2876 | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Aspergillus fumigatus ATCC MYA-4609 | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Aspergillus fumigatus CBS 101355 | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | Aspergillus fumigatus FGSC A1100 | - |
4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.154 | Aspergillus flavus | A0A2I5YP19 | - |
- |
| 1.14.14.154 | Aspergillus fumigatus | E9QY26 | Aspergillus fumigatus | - |
| 1.14.14.154 | Aspergillus fumigatus | Q4WNT5 | Aspergillus fumigatus | - |
| 1.14.14.154 | Aspergillus fumigatus Af293 | E9QY26 | Aspergillus fumigatus | - |
| 1.14.14.154 | Aspergillus fumigatus Af293 | Q4WNT5 | Aspergillus fumigatus | - |
| 1.14.14.154 | Aspergillus fumigatus ATCC MYA-4609 | E9QY26 | Aspergillus fumigatus | - |
| 1.14.14.154 | Aspergillus fumigatus ATCC MYA-4609 | Q4WNT5 | Aspergillus fumigatus | - |
| 1.14.14.154 | Aspergillus fumigatus CBS 101355 | E9QY26 | Aspergillus fumigatus | - |
| 1.14.14.154 | Aspergillus fumigatus CBS 101355 | Q4WNT5 | Aspergillus fumigatus | - |
| 1.14.14.154 | Aspergillus fumigatus FGSC A1100 | E9QY26 | Aspergillus fumigatus | - |
| 1.14.14.154 | Aspergillus fumigatus FGSC A1100 | Q4WNT5 | Aspergillus fumigatus | - |
| 1.14.14.154 | Aspergillus parasiticus | - |
- |
- |
| 1.14.14.154 | Candida albicans | P10613 | - |
- |
| 1.14.14.154 | Candida albicans ATCC MYA-2876 | P10613 | - |
- |
| 1.14.14.154 | Cryptococcus neoformans | A0A1I7P313 | - |
- |
| 1.14.14.154 | Fusarium oxysporum | - |
- |
- |
| 1.14.14.154 | Homo sapiens | Q16850 | - |
- |
| 1.14.14.154 | Nakaseomyces glabratus | - |
- |
- |
| 1.14.14.154 | Phanerodontia chrysosporium | B6DX27 | - |
- |
| 1.14.14.154 | Pseudocercospora musae | - |
- |
- |
| 1.14.14.154 | Puccinia sp. | - |
- |
- |
| 1.14.14.154 | Pyricularia oryzae | - |
- |
- |
| 1.14.14.154 | Rhodonia placenta | - |
- |
- |
| 1.14.14.154 | Saccharomyces cerevisiae | P10614 | - |
- |
| 1.14.14.154 | Zymoseptoria tritici | A0A0E3H4X7 | Mycosphaerella triticola | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.14.154 | recombinant C-terminally His6-tagged enzyme ScLDM from Saccharomyces cerevisiae by nickel affinity chromatography and gel filtration | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.154 | a 14alpha-methylsteroid + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Homo sapiens | a DELTA14-steroid + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Candida albicans | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Nakaseomyces glabratus | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Saccharomyces cerevisiae | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Aspergillus fumigatus | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Homo sapiens | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Phanerodontia chrysosporium | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Rhodonia placenta | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Puccinia sp. | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Zymoseptoria tritici | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Pseudocercospora musae | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Fusarium oxysporum | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Pyricularia oryzae | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Aspergillus flavus | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Aspergillus parasiticus | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Cryptococcus neoformans | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | the LDM enzyme reaction involves 3 cycles of reduction that removes a water molecule bound to the heme, and the formation activated heme-oxygen (FeIV=O) complexes that sequentially modify the lanosterol 14-methyl group to an alcohol, an aldehyde and then introduces a 14-15 double bond and releases formate. The reaction uses lanosterol as substrate, the electrons generated from 3 molecules of NADPH by NADPH-cytochrome P450 reductase, 3 protons, 3 O2 molecules and generates 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, formate and 4 water molecules | Candida albicans | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | the LDM enzyme reaction involves 3 cycles of reduction that removes a water molecule bound to the heme, and the formation activated heme-oxygen (FeIV=O) complexes that sequentially modify the lanosterol 14-methyl group to an alcohol, an aldehyde and then introduces a 14-15 double bond and releases formate. The reaction uses lanosterol as substrate, the electrons generated from 3 molecules of NADPH by NADPH-cytochrome P450 reductase, 3 protons, 3 O2 molecules and generates 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, formate and 4 water molecules | Nakaseomyces glabratus | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | the LDM enzyme reaction involves 3 cycles of reduction that removes a water molecule bound to the heme, and the formation activated heme-oxygen (FeIV=O) complexes that sequentially modify the lanosterol 14-methyl group to an alcohol, an aldehyde and then introduces a 14-15 double bond and releases formate. The reaction uses lanosterol as substrate, the electrons generated from 3 molecules of NADPH by NADPH-cytochrome P450 reductase, 3 protons, 3 O2 molecules and generates 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, formate and 4 water molecules | Saccharomyces cerevisiae | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | the LDM enzyme reaction involves 3 cycles of reduction that removes a water molecule bound to the heme, and the formation activated heme-oxygen (FeIV=O) complexes that sequentially modify the lanosterol 14-methyl group to an alcohol, an aldehyde and then introduces a 14-15 double bond and releases formate. The reaction uses lanosterol as substrate, the electrons generated from 3 molecules of NADPH by NADPH-cytochrome P450 reductase, 3 protons, 3 O2 molecules and generates 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, formate and 4 water molecules | Aspergillus fumigatus | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | the LDM enzyme reaction involves 3 cycles of reduction that removes a water molecule bound to the heme, and the formation activated heme-oxygen (FeIV=O) complexes that sequentially modify the lanosterol 14-methyl group to an alcohol, an aldehyde and then introduces a 14-15 double bond and releases formate. The reaction uses lanosterol as substrate, the electrons generated from 3 molecules of NADPH by NADPH-cytochrome P450 reductase, 3 protons, 3 O2 molecules and generates 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, formate and 4 water molecules | Phanerodontia chrysosporium | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | the LDM enzyme reaction involves 3 cycles of reduction that removes a water molecule bound to the heme, and the formation activated heme-oxygen (FeIV=O) complexes that sequentially modify the lanosterol 14-methyl group to an alcohol, an aldehyde and then introduces a 14-15 double bond and releases formate. The reaction uses lanosterol as substrate, the electrons generated from 3 molecules of NADPH by NADPH-cytochrome P450 reductase, 3 protons, 3 O2 molecules and generates 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, formate and 4 water molecules | Rhodonia placenta | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | the LDM enzyme reaction involves 3 cycles of reduction that removes a water molecule bound to the heme, and the formation activated heme-oxygen (FeIV=O) complexes that sequentially modify the lanosterol 14-methyl group to an alcohol, an aldehyde and then introduces a 14-15 double bond and releases formate. The reaction uses lanosterol as substrate, the electrons generated from 3 molecules of NADPH by NADPH-cytochrome P450 reductase, 3 protons, 3 O2 molecules and generates 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, formate and 4 water molecules | Puccinia sp. | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | the LDM enzyme reaction involves 3 cycles of reduction that removes a water molecule bound to the heme, and the formation activated heme-oxygen (FeIV=O) complexes that sequentially modify the lanosterol 14-methyl group to an alcohol, an aldehyde and then introduces a 14-15 double bond and releases formate. The reaction uses lanosterol as substrate, the electrons generated from 3 molecules of NADPH by NADPH-cytochrome P450 reductase, 3 protons, 3 O2 molecules and generates 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, formate and 4 water molecules | Zymoseptoria tritici | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | the LDM enzyme reaction involves 3 cycles of reduction that removes a water molecule bound to the heme, and the formation activated heme-oxygen (FeIV=O) complexes that sequentially modify the lanosterol 14-methyl group to an alcohol, an aldehyde and then introduces a 14-15 double bond and releases formate. The reaction uses lanosterol as substrate, the electrons generated from 3 molecules of NADPH by NADPH-cytochrome P450 reductase, 3 protons, 3 O2 molecules and generates 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, formate and 4 water molecules | Pseudocercospora musae | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | the LDM enzyme reaction involves 3 cycles of reduction that removes a water molecule bound to the heme, and the formation activated heme-oxygen (FeIV=O) complexes that sequentially modify the lanosterol 14-methyl group to an alcohol, an aldehyde and then introduces a 14-15 double bond and releases formate. The reaction uses lanosterol as substrate, the electrons generated from 3 molecules of NADPH by NADPH-cytochrome P450 reductase, 3 protons, 3 O2 molecules and generates 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, formate and 4 water molecules | Fusarium oxysporum | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | the LDM enzyme reaction involves 3 cycles of reduction that removes a water molecule bound to the heme, and the formation activated heme-oxygen (FeIV=O) complexes that sequentially modify the lanosterol 14-methyl group to an alcohol, an aldehyde and then introduces a 14-15 double bond and releases formate. The reaction uses lanosterol as substrate, the electrons generated from 3 molecules of NADPH by NADPH-cytochrome P450 reductase, 3 protons, 3 O2 molecules and generates 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, formate and 4 water molecules | Pyricularia oryzae | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | the LDM enzyme reaction involves 3 cycles of reduction that removes a water molecule bound to the heme, and the formation activated heme-oxygen (FeIV=O) complexes that sequentially modify the lanosterol 14-methyl group to an alcohol, an aldehyde and then introduces a 14-15 double bond and releases formate. The reaction uses lanosterol as substrate, the electrons generated from 3 molecules of NADPH by NADPH-cytochrome P450 reductase, 3 protons, 3 O2 molecules and generates 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, formate and 4 water molecules | Aspergillus flavus | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | the LDM enzyme reaction involves 3 cycles of reduction that removes a water molecule bound to the heme, and the formation activated heme-oxygen (FeIV=O) complexes that sequentially modify the lanosterol 14-methyl group to an alcohol, an aldehyde and then introduces a 14-15 double bond and releases formate. The reaction uses lanosterol as substrate, the electrons generated from 3 molecules of NADPH by NADPH-cytochrome P450 reductase, 3 protons, 3 O2 molecules and generates 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, formate and 4 water molecules | Aspergillus parasiticus | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | the LDM enzyme reaction involves 3 cycles of reduction that removes a water molecule bound to the heme, and the formation activated heme-oxygen (FeIV=O) complexes that sequentially modify the lanosterol 14-methyl group to an alcohol, an aldehyde and then introduces a 14-15 double bond and releases formate. The reaction uses lanosterol as substrate, the electrons generated from 3 molecules of NADPH by NADPH-cytochrome P450 reductase, 3 protons, 3 O2 molecules and generates 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, formate and 4 water molecules | Cryptococcus neoformans | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Aspergillus fumigatus Af293 | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | the LDM enzyme reaction involves 3 cycles of reduction that removes a water molecule bound to the heme, and the formation activated heme-oxygen (FeIV=O) complexes that sequentially modify the lanosterol 14-methyl group to an alcohol, an aldehyde and then introduces a 14-15 double bond and releases formate. The reaction uses lanosterol as substrate, the electrons generated from 3 molecules of NADPH by NADPH-cytochrome P450 reductase, 3 protons, 3 O2 molecules and generates 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, formate and 4 water molecules | Aspergillus fumigatus Af293 | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Candida albicans ATCC MYA-2876 | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | the LDM enzyme reaction involves 3 cycles of reduction that removes a water molecule bound to the heme, and the formation activated heme-oxygen (FeIV=O) complexes that sequentially modify the lanosterol 14-methyl group to an alcohol, an aldehyde and then introduces a 14-15 double bond and releases formate. The reaction uses lanosterol as substrate, the electrons generated from 3 molecules of NADPH by NADPH-cytochrome P450 reductase, 3 protons, 3 O2 molecules and generates 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, formate and 4 water molecules | Candida albicans ATCC MYA-2876 | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Aspergillus fumigatus ATCC MYA-4609 | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | the LDM enzyme reaction involves 3 cycles of reduction that removes a water molecule bound to the heme, and the formation activated heme-oxygen (FeIV=O) complexes that sequentially modify the lanosterol 14-methyl group to an alcohol, an aldehyde and then introduces a 14-15 double bond and releases formate. The reaction uses lanosterol as substrate, the electrons generated from 3 molecules of NADPH by NADPH-cytochrome P450 reductase, 3 protons, 3 O2 molecules and generates 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, formate and 4 water molecules | Aspergillus fumigatus ATCC MYA-4609 | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Aspergillus fumigatus CBS 101355 | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | the LDM enzyme reaction involves 3 cycles of reduction that removes a water molecule bound to the heme, and the formation activated heme-oxygen (FeIV=O) complexes that sequentially modify the lanosterol 14-methyl group to an alcohol, an aldehyde and then introduces a 14-15 double bond and releases formate. The reaction uses lanosterol as substrate, the electrons generated from 3 molecules of NADPH by NADPH-cytochrome P450 reductase, 3 protons, 3 O2 molecules and generates 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, formate and 4 water molecules | Aspergillus fumigatus CBS 101355 | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | - |
Aspergillus fumigatus FGSC A1100 | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | lanosterol + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 | the LDM enzyme reaction involves 3 cycles of reduction that removes a water molecule bound to the heme, and the formation activated heme-oxygen (FeIV=O) complexes that sequentially modify the lanosterol 14-methyl group to an alcohol, an aldehyde and then introduces a 14-15 double bond and releases formate. The reaction uses lanosterol as substrate, the electrons generated from 3 molecules of NADPH by NADPH-cytochrome P450 reductase, 3 protons, 3 O2 molecules and generates 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol, formate and 4 water molecules | Aspergillus fumigatus FGSC A1100 | 4,4-dimethylcholesta-8(9),14,24-trien-3beta-ol + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | - |
? | |
| 1.14.14.154 | additional information | measurement of LDM catalytic activity uses radiolabelled lanosterol and GC-MS methodology together with amounts of enzyme in excess of ligand affinities | Candida albicans | ? | - |
? | |
| 1.14.14.154 | additional information | measurement of LDM catalytic activity uses radiolabelled lanosterol and GC-MS methodology together with amounts of enzyme in excess of ligand affinities | Nakaseomyces glabratus | ? | - |
? | |
| 1.14.14.154 | additional information | measurement of LDM catalytic activity uses radiolabelled lanosterol and GC-MS methodology together with amounts of enzyme in excess of ligand affinities | Saccharomyces cerevisiae | ? | - |
? | |
| 1.14.14.154 | additional information | measurement of LDM catalytic activity uses radiolabelled lanosterol and GC-MS methodology together with amounts of enzyme in excess of ligand affinities | Aspergillus fumigatus | ? | - |
? | |
| 1.14.14.154 | additional information | measurement of LDM catalytic activity uses radiolabelled lanosterol and GC-MS methodology together with amounts of enzyme in excess of ligand affinities | Phanerodontia chrysosporium | ? | - |
? | |
| 1.14.14.154 | additional information | measurement of LDM catalytic activity uses radiolabelled lanosterol and GC-MS methodology together with amounts of enzyme in excess of ligand affinities | Rhodonia placenta | ? | - |
? | |
| 1.14.14.154 | additional information | measurement of LDM catalytic activity uses radiolabelled lanosterol and GC-MS methodology together with amounts of enzyme in excess of ligand affinities | Aspergillus fumigatus Af293 | ? | - |
? | |
| 1.14.14.154 | additional information | measurement of LDM catalytic activity uses radiolabelled lanosterol and GC-MS methodology together with amounts of enzyme in excess of ligand affinities | Candida albicans ATCC MYA-2876 | ? | - |
? | |
| 1.14.14.154 | additional information | measurement of LDM catalytic activity uses radiolabelled lanosterol and GC-MS methodology together with amounts of enzyme in excess of ligand affinities | Aspergillus fumigatus ATCC MYA-4609 | ? | - |
? | |
| 1.14.14.154 | additional information | measurement of LDM catalytic activity uses radiolabelled lanosterol and GC-MS methodology together with amounts of enzyme in excess of ligand affinities | Aspergillus fumigatus CBS 101355 | ? | - |
? | |
| 1.14.14.154 | additional information | measurement of LDM catalytic activity uses radiolabelled lanosterol and GC-MS methodology together with amounts of enzyme in excess of ligand affinities | Aspergillus fumigatus FGSC A1100 | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.14.154 | CYP51 | - |
Candida albicans |
| 1.14.14.154 | CYP51 | - |
Nakaseomyces glabratus |
| 1.14.14.154 | CYP51 | - |
Saccharomyces cerevisiae |
| 1.14.14.154 | CYP51 | - |
Aspergillus fumigatus |
| 1.14.14.154 | CYP51 | - |
Homo sapiens |
| 1.14.14.154 | CYP51 | - |
Phanerodontia chrysosporium |
| 1.14.14.154 | CYP51 | - |
Rhodonia placenta |
| 1.14.14.154 | CYP51 | - |
Puccinia sp. |
| 1.14.14.154 | CYP51 | - |
Zymoseptoria tritici |
| 1.14.14.154 | CYP51 | - |
Pseudocercospora musae |
| 1.14.14.154 | CYP51 | - |
Fusarium oxysporum |
| 1.14.14.154 | CYP51 | - |
Pyricularia oryzae |
| 1.14.14.154 | CYP51 | - |
Aspergillus flavus |
| 1.14.14.154 | CYP51 | - |
Aspergillus parasiticus |
| 1.14.14.154 | CYP51 | - |
Cryptococcus neoformans |
| 1.14.14.154 | Cyp51A | - |
Aspergillus fumigatus |
| 1.14.14.154 | CYP51B | - |
Aspergillus fumigatus |
| 1.14.14.154 | cytochrome P450 51 | - |
Phanerodontia chrysosporium |
| 1.14.14.154 | cytochrome P450 51 | - |
Rhodonia placenta |
| 1.14.14.154 | ERG11 | - |
Cryptococcus neoformans |
| 1.14.14.154 | erg11A | - |
Aspergillus fumigatus |
| 1.14.14.154 | lanosterol 14alpha-demethylase | - |
Candida albicans |
| 1.14.14.154 | lanosterol 14alpha-demethylase | - |
Nakaseomyces glabratus |
| 1.14.14.154 | lanosterol 14alpha-demethylase | - |
Saccharomyces cerevisiae |
| 1.14.14.154 | lanosterol 14alpha-demethylase | - |
Aspergillus fumigatus |
| 1.14.14.154 | lanosterol 14alpha-demethylase | - |
Homo sapiens |
| 1.14.14.154 | lanosterol 14alpha-demethylase | - |
Phanerodontia chrysosporium |
| 1.14.14.154 | lanosterol 14alpha-demethylase | - |
Rhodonia placenta |
| 1.14.14.154 | lanosterol 14alpha-demethylase | - |
Puccinia sp. |
| 1.14.14.154 | lanosterol 14alpha-demethylase | - |
Zymoseptoria tritici |
| 1.14.14.154 | lanosterol 14alpha-demethylase | - |
Pseudocercospora musae |
| 1.14.14.154 | lanosterol 14alpha-demethylase | - |
Fusarium oxysporum |
| 1.14.14.154 | lanosterol 14alpha-demethylase | - |
Pyricularia oryzae |
| 1.14.14.154 | lanosterol 14alpha-demethylase | - |
Aspergillus flavus |
| 1.14.14.154 | lanosterol 14alpha-demethylase | - |
Aspergillus parasiticus |
| 1.14.14.154 | lanosterol 14alpha-demethylase | - |
Cryptococcus neoformans |
| 1.14.14.154 | LDM | - |
Candida albicans |
| 1.14.14.154 | LDM | - |
Nakaseomyces glabratus |
| 1.14.14.154 | LDM | - |
Saccharomyces cerevisiae |
| 1.14.14.154 | LDM | - |
Aspergillus fumigatus |
| 1.14.14.154 | LDM | - |
Homo sapiens |
| 1.14.14.154 | LDM | - |
Phanerodontia chrysosporium |
| 1.14.14.154 | LDM | - |
Rhodonia placenta |
| 1.14.14.154 | LDM | - |
Puccinia sp. |
| 1.14.14.154 | LDM | - |
Zymoseptoria tritici |
| 1.14.14.154 | LDM | - |
Pseudocercospora musae |
| 1.14.14.154 | LDM | - |
Fusarium oxysporum |
| 1.14.14.154 | LDM | - |
Pyricularia oryzae |
| 1.14.14.154 | LDM | - |
Aspergillus flavus |
| 1.14.14.154 | LDM | - |
Aspergillus parasiticus |
| 1.14.14.154 | LDM | - |
Cryptococcus neoformans |
| 1.14.14.154 | ScLDM | - |
Saccharomyces cerevisiae |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.154 | cytochrome P450 | - |
Candida albicans | |
| 1.14.14.154 | cytochrome P450 | - |
Nakaseomyces glabratus | |
| 1.14.14.154 | cytochrome P450 | - |
Saccharomyces cerevisiae | |
| 1.14.14.154 | cytochrome P450 | - |
Aspergillus fumigatus | |
| 1.14.14.154 | cytochrome P450 | - |
Homo sapiens | |
| 1.14.14.154 | cytochrome P450 | - |
Phanerodontia chrysosporium | |
| 1.14.14.154 | cytochrome P450 | - |
Rhodonia placenta | |
| 1.14.14.154 | cytochrome P450 | - |
Puccinia sp. | |
| 1.14.14.154 | cytochrome P450 | - |
Zymoseptoria tritici | |
| 1.14.14.154 | cytochrome P450 | - |
Pseudocercospora musae | |
| 1.14.14.154 | cytochrome P450 | - |
Fusarium oxysporum | |
| 1.14.14.154 | cytochrome P450 | - |
Pyricularia oryzae | |
| 1.14.14.154 | cytochrome P450 | - |
Aspergillus flavus | |
| 1.14.14.154 | cytochrome P450 | - |
Aspergillus parasiticus | |
| 1.14.14.154 | cytochrome P450 | - |
Cryptococcus neoformans | |
| 1.14.14.154 | heme | - |
Candida albicans | |
| 1.14.14.154 | heme | - |
Nakaseomyces glabratus | |
| 1.14.14.154 | heme | - |
Saccharomyces cerevisiae | |
| 1.14.14.154 | heme | - |
Aspergillus fumigatus | |
| 1.14.14.154 | heme | - |
Homo sapiens | |
| 1.14.14.154 | heme | - |
Phanerodontia chrysosporium | |
| 1.14.14.154 | heme | - |
Rhodonia placenta | |
| 1.14.14.154 | heme | - |
Puccinia sp. | |
| 1.14.14.154 | heme | - |
Zymoseptoria tritici | |
| 1.14.14.154 | heme | - |
Pseudocercospora musae | |
| 1.14.14.154 | heme | - |
Fusarium oxysporum | |
| 1.14.14.154 | heme | - |
Pyricularia oryzae | |
| 1.14.14.154 | heme | - |
Aspergillus flavus | |
| 1.14.14.154 | heme | - |
Aspergillus parasiticus | |
| 1.14.14.154 | heme | - |
Cryptococcus neoformans | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.14.14.154 | additional information | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane. Within the ligand binding pocket the azole antifungals have additional affinity determining interactions with hydrophobic side-chains, the polypeptide backbone and via water-mediated hydrogen bond networks. Structure-function analysis | Candida albicans |
| 1.14.14.154 | additional information | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane. Within the ligand binding pocket the azole antifungals have additional affinity determining interactions with hydrophobic side-chains, the polypeptide backbone and via water-mediated hydrogen bond networks | Nakaseomyces glabratus |
| 1.14.14.154 | additional information | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane. Within the ligand binding pocket the azole antifungals have additional affinity determining interactions with hydrophobic side-chains, the polypeptide backbone and via water-mediated hydrogen bond networks. Structure-function analysis | Saccharomyces cerevisiae |
| 1.14.14.154 | additional information | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane. Within the ligand binding pocket the azole antifungals have additional affinity determining interactions with hydrophobic side-chains, the polypeptide backbone and via water-mediated hydrogen bond networks. Structure-function analysis | Aspergillus fumigatus |
| 1.14.14.154 | additional information | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane. Within the ligand binding pocket the azole antifungals have additional affinity determining interactions with hydrophobic side-chains, the polypeptide backbone and via water-mediated hydrogen bond networks. Structure-function analysis | Homo sapiens |
| 1.14.14.154 | additional information | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane. Within the ligand binding pocket the azole antifungals have additional affinity determining interactions with hydrophobic side-chains, the polypeptide backbone and via water-mediated hydrogen bond networks. Structure-function analysis | Phanerodontia chrysosporium |
| 1.14.14.154 | additional information | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane. Within the ligand binding pocket the azole antifungals have additional affinity determining interactions with hydrophobic side-chains, the polypeptide backbone and via water-mediated hydrogen bond networks. Structure-function analysis | Rhodonia placenta |
| 1.14.14.154 | additional information | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane. Within the ligand binding pocket the azole antifungals have additional affinity determining interactions with hydrophobic side-chains, the polypeptide backbone and via water-mediated hydrogen bond networks. Structure-function analysis | Puccinia sp. |
| 1.14.14.154 | additional information | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane. Within the ligand binding pocket the azole antifungals have additional affinity determining interactions with hydrophobic side-chains, the polypeptide backbone and via water-mediated hydrogen bond networks. Structure-function analysis | Zymoseptoria tritici |
| 1.14.14.154 | additional information | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane. Within the ligand binding pocket the azole antifungals have additional affinity determining interactions with hydrophobic side-chains, the polypeptide backbone and via water-mediated hydrogen bond networks. Structure-function analysis | Pseudocercospora musae |
| 1.14.14.154 | additional information | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane. Within the ligand binding pocket the azole antifungals have additional affinity determining interactions with hydrophobic side-chains, the polypeptide backbone and via water-mediated hydrogen bond networks. Structure-function analysis | Fusarium oxysporum |
| 1.14.14.154 | additional information | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane. Within the ligand binding pocket the azole antifungals have additional affinity determining interactions with hydrophobic side-chains, the polypeptide backbone and via water-mediated hydrogen bond networks. Structure-function analysis | Pyricularia oryzae |
| 1.14.14.154 | additional information | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane. Within the ligand binding pocket the azole antifungals have additional affinity determining interactions with hydrophobic side-chains, the polypeptide backbone and via water-mediated hydrogen bond networks. Structure-function analysis | Aspergillus flavus |
| 1.14.14.154 | additional information | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane. Within the ligand binding pocket the azole antifungals have additional affinity determining interactions with hydrophobic side-chains, the polypeptide backbone and via water-mediated hydrogen bond networks. Structure-function analysis | Aspergillus parasiticus |
| 1.14.14.154 | additional information | the membrane-bound enzyme contains a relatively rigid ligand binding pocket comprised of a deeply buried heme-containing active site together with a substrate entry channel and putative product exit channel that reach to the membrane. Within the ligand binding pocket the azole antifungals have additional affinity determining interactions with hydrophobic side-chains, the polypeptide backbone and via water-mediated hydrogen bond networks. Structure-function analysis | Cryptococcus neoformans |
| 1.14.14.154 | physiological function | azole inhibitors are used to inhibit the enzyme from Puccinia spp., which cause wheat rust as pathogens | Puccinia sp. |
| 1.14.14.154 | physiological function | azole inhibitors are used to inhibit the enzyme from Zymoseptoria tritici, which causes septoria leaf blotch in wheat as a pathogen | Zymoseptoria tritici |
| 1.14.14.154 | physiological function | azole inhibitors are used to inhibit the enzyme from Mycosphaerella musicola, which causes black sigatoka in bananas as a pathogen | Pseudocercospora musae |
| 1.14.14.154 | physiological function | azole inhibitors are used to inhibit the enzyme from Fusarium oxysporum, which causes panama disease or fusarium wilt in bananas as a pathogen | Fusarium oxysporum |
| 1.14.14.154 | physiological function | azole inhibitors are used to inhibit the enzyme from Magnaporthe oryzae, which causes rice blast disease as a pathogen | Pyricularia oryzae |
| 1.14.14.154 | physiological function | azole inhibitors are used to inhibit the enzyme from Aspergillus flavus, which produces mycotoxin as a pathogen | Aspergillus flavus |
| 1.14.14.154 | physiological function | azole inhibitors are used to inhibit the enzyme from Aspergillus parasiticus, which produces mycotoxin as a pathogen | Aspergillus parasiticus |
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