Any feedback?
Literature summary extracted from
- Isolation and reconstitution of the heme-thiolate protein obtusifoliol 14alpha-demethylase from Sorghum bicolor (L.) Moench (1996), J. Biol. Chem., 271, 32944-32950.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 1.14.14.154 | 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 |
| 1.14.14.154 | 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 |
| 1.14.14.154 | 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 |
| 1.14.14.154 | 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 |
| 1.14.14.154 | 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 |
| 1.14.14.154 | pharmacology | target enzyme for the design of phyla-specific sterol 14alpha-demethylase inhibitors | Sorghum bicolor |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.154 | CO | - |
Sorghum bicolor |  |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.14.14.154 | membrane | - |
Sorghum bicolor | 16020 | - |
| 1.14.14.154 | microsome | - |
Embryophyta | - |
- |
| 1.14.14.154 | microsome | - |
Sorghum bicolor | - |
- |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.154 | 53000 | - |
SDS-PAGE and amino acid sequence analysis | Sorghum bicolor |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.154 | additional information | Embryophyta | - |
? | - |
? | |
| 1.14.14.154 | additional information | Sorghum bicolor | biosynthetic enzyme with very narrow substrate specificity | ? | - |
? | |
| 1.14.14.154 | 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 | ? | - |
? | |
| 1.14.14.154 | additional information | Sorghum bicolor | key enzyme in plant sterol, phytosterol, biosynthesis | ? | - |
? | |
| 1.14.14.154 | 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 | - |
? | |
| 1.14.14.154 | 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 | - |
? | |
| 1.14.14.154 | 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 | - |
? | |
| 1.14.14.154 | 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
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.154 | Embryophyta | - |
higher plants | - |
| 1.14.14.154 | Sorghum bicolor | - |
L., Moench | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.14.154 | purification and reconstitution | Sorghum bicolor |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.14.14.154 | seedling | etiolated Sorghum seedlings | Sorghum bicolor | - |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 1.14.14.154 | -80°C, frozen in liquid nitrogen | Sorghum bicolor |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.154 | additional information | - |
Embryophyta | ? | - |
? | |
| 1.14.14.154 | additional information | substrate specificity | Embryophyta | ? | - |
? | |
| 1.14.14.154 | additional information | substrate specificity | Sorghum bicolor | ? | - |
? | |
| 1.14.14.154 | additional information | substrate binding spectra | Sorghum bicolor | ? | - |
? | |
| 1.14.14.154 | additional information | biosynthetic enzyme with very narrow substrate specificity | Sorghum bicolor | ? | - |
? | |
| 1.14.14.154 | additional information | no activity with lanosterol, campesterol, sitosterol, or stigmasterol | Sorghum bicolor | ? | - |
? | |
| 1.14.14.154 | 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 | ? | - |
? | |
| 1.14.14.154 | additional information | substrate for 14alpha-demethylation reaction in plants is different from that in animals and fungi | Embryophyta | ? | - |
? | |
| 1.14.14.154 | additional information | substrate for 14alpha-demethylation reaction in plants is different from that in animals and fungi | Sorghum bicolor | ? | - |
? | |
| 1.14.14.154 | additional information | plant sterol 14alpha-demethylase have high substrate specificity | Sorghum bicolor | ? | - |
? | |
| 1.14.14.154 | additional information | key enzyme in plant sterol, phytosterol, biosynthesis | Sorghum bicolor | ? | - |
? | |
| 1.14.14.154 | 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 | - |
? | |
| 1.14.14.154 | 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 | - |
? | |
| 1.14.14.154 | 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 | - |
? | |
| 1.14.14.154 | 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 | - |
? | |
| 1.14.14.154 | 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 | - |
? | |
| 1.14.14.154 | 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
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.14.14.154 | monomer | 1 * 53000, SDS-PAGE | Sorghum bicolor |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.154 | cytochrome P450 | - |
Embryophyta | |
| 1.14.14.154 | cytochrome P450 | - |
Sorghum bicolor | |
| 1.14.14.154 | heme | heme-thiolate enzyme | Embryophyta | |
| 1.14.14.154 | heme | heme-thiolate enzyme | Sorghum bicolor | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
