Application | Comment | Organism |
---|---|---|
agriculture | target enzyme for azole antifungal agents. These specific inhibitors are of great importance as plant growth regulators, fungicides and herbicides in the agricultural and medical fields | Sorghum bicolor |
agriculture | all known functional sterols lack a 14alpha-methyl group, and therefore the 14alpha-demethylation reaction has received much attention from the pharmaceutical and agriculture-chemical industry as a possible means to specifically control and inhibit sterol biosynthesis in mammals, fungi, and plant | Sorghum bicolor |
medicine | target enzyme for azole antifungal agents. These specific inhibitors are of great importance as plant growth regulators, fungicides and herbicides in the agricultural and medical fields | Sorghum bicolor |
pharmacology | target enzyme for azole antifungal agents. These specific inhibitors are of great importance as plant growth regulators, fungicides and herbicides in the agricultural and medical fields | Sorghum bicolor |
pharmacology | all known functional sterols lack a 14alpha-methyl group, and therefore the 14alpha-demethylation reaction has received much attention from the pharmaceutical and agriculture-chemical industry as a possible means to specifically control and inhibit sterol biosynthesis in mammals, fungi, and plant | Sorghum bicolor |
pharmacology | target enzyme for the design of phyla-specific sterol 14alpha-demethylase inhibitors | Sorghum bicolor |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
CO | - |
Sorghum bicolor |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Sorghum bicolor | 16020 | - |
microsome | - |
Embryophyta | - |
- |
microsome | - |
Sorghum bicolor | - |
- |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
53000 | - |
SDS-PAGE and amino acid sequence analysis | Sorghum bicolor |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Embryophyta | - |
? | - |
? | |
additional information | Sorghum bicolor | biosynthetic enzyme with very narrow substrate specificity | ? | - |
? | |
additional information | Sorghum bicolor | enzyme is a multifunctional cytochrome P450, which as the same active site catalyze demethylation in three consecutive NADPH- and O2-dependent hydroxylation reactions, resulting in the elimination of the methyl group as formic acid and the introduction of a double bond at the DELTA14 position | ? | - |
? | |
additional information | Sorghum bicolor | key enzyme in plant sterol, phytosterol, biosynthesis | ? | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | Embryophyta | 4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol | 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | Sorghum bicolor | 4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol | 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | Embryophyta | 4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol | 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | Sorghum bicolor | 4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol | 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Embryophyta | - |
higher plants | - |
Sorghum bicolor | - |
L., Moench | - |
Purification (Comment) | Organism |
---|---|
purification and reconstitution | Sorghum bicolor |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
seedling | etiolated Sorghum seedlings | Sorghum bicolor | - |
Storage Stability | Organism |
---|---|
-80°C, frozen in liquid nitrogen | Sorghum bicolor |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | - |
Embryophyta | ? | - |
? | |
additional information | substrate specificity | Embryophyta | ? | - |
? | |
additional information | substrate specificity | Sorghum bicolor | ? | - |
? | |
additional information | substrate binding spectra | Sorghum bicolor | ? | - |
? | |
additional information | biosynthetic enzyme with very narrow substrate specificity | Sorghum bicolor | ? | - |
? | |
additional information | no activity with lanosterol, campesterol, sitosterol, or stigmasterol | Sorghum bicolor | ? | - |
? | |
additional information | enzyme is a multifunctional cytochrome P450, which as the same active site catalyze demethylation in three consecutive NADPH- and O2-dependent hydroxylation reactions, resulting in the elimination of the methyl group as formic acid and the introduction of a double bond at the DELTA14 position | Sorghum bicolor | ? | - |
? | |
additional information | substrate for 14alpha-demethylation reaction in plants is different from that in animals and fungi | Embryophyta | ? | - |
? | |
additional information | substrate for 14alpha-demethylation reaction in plants is different from that in animals and fungi | Sorghum bicolor | ? | - |
? | |
additional information | plant sterol 14alpha-demethylase have high substrate specificity | Sorghum bicolor | ? | - |
? | |
additional information | key enzyme in plant sterol, phytosterol, biosynthesis | Sorghum bicolor | ? | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | 4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol | Embryophyta | 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | 4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol | Sorghum bicolor | 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | catalyzes 14alpha-demethylation of obtusifoliol | Embryophyta | 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | catalyzes 14alpha-demethylation of obtusifoliol | Sorghum bicolor | 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | 4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol | Embryophyta | 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | 4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol | Sorghum bicolor | 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 53000, SDS-PAGE | Sorghum bicolor |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
cytochrome P450 | - |
Embryophyta | |
cytochrome P450 | - |
Sorghum bicolor | |
heme | heme-thiolate enzyme | Embryophyta | |
heme | heme-thiolate enzyme | Sorghum bicolor |