Any feedback?
Literature summary extracted from
- Properties and structural requirements for substrate specificity of cytochrome P-450-dependent obtusifoliol 14alpha-demethylase from maize (Zea mays) seedlings (1991), Biochem. J., 277, 483-492.
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 | Zea mays |
| 1.14.14.154 | agriculture | target of important agrochemicals such as fungicides, plant growth regulators and herbicides | Zea mays |
| 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 | Zea mays |
| 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 | Zea mays |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 1.14.14.154 | plant demethylase is remarkably stable | Zea mays |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.14.154 | additional information | - |
additional information | kinetic parameters | Zea mays | |
| 1.14.14.154 | 0.116 | - |
(3beta,4alpha,5alpha)-4,14-dimethylcholest-8-en-3-ol | - |
Zea mays |  |
| 1.14.14.154 | 0.16 | - |
obtusifoliol | - |
Zea mays | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.14.14.154 | endoplasmic reticulum | - |
Zea mays | 5783 | - |
| 1.14.14.154 | endoplasmic reticulum | light membrane fraction of endoplasmic reticulum, not in plasma membrane | Zea mays | 5783 | - |
| 1.14.14.154 | membrane | membrane-bound | Zea mays | 16020 | - |
| 1.14.14.154 | microsome | microsomal-bound | Zea mays | - |
- |
| 1.14.14.154 | additional information | not in plasma membrane | Zea mays | - |
- |
| 1.14.14.154 | additional information | subcellular localization, distribution | Zea mays | - |
- |
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 | Zea mays | enzyme of sterol biosynthetic pathway | ? | - |
? | |
| 1.14.14.154 | additional information | Zea mays | enzyme of plant sterol, phytosterol, biosynthesis | ? | - |
? | |
| 1.14.14.154 | obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | Zea mays | 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 | Zea mays | 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 | Zea mays | - |
maize | - |
| 1.14.14.154 | Zea mays | - |
LG11 | - |
| 1.14.14.154 | Zea mays LG11 | - |
LG11 | - |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.14.14.154 | a 14alpha-methylsteroid + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = a DELTA14-steroid + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | mechanism | Zea mays |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.14.14.154 | seedling | - |
Zea mays | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.154 | (3b,4a,5a)-4,14-dimethylcholest-8-en-3-ol + [reduced NADPH-hemoprotein reductase] + O2 | good substrate, 67% of activity compared to obtusifoliol | Zea mays | ? + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
| 1.14.14.154 | (3beta,4alpha,5alpha)-4,14-dimethylcholest-8-en-3-ol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Zea mays | ? | - |
r | |
| 1.14.14.154 | 14alpha-methyl-24,28-dihydrofecosterol + [reduced NADPH-hemoprotein reductase] + O2 | 50% of activity compared to obtusifoliol | Zea mays | ? + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
| 1.14.14.154 | 24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | good substrate, 75% of activity to obtusifoliol | Zea mays | 4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
| 1.14.14.154 | 24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | DHO | Zea mays | 4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
| 1.14.14.154 | 24,28-dihydroobtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | 4alpha,14alpha-dimethyl-5alpha-ergosta-8-en-3beta-ol | Zea mays | 4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
| 1.14.14.154 | additional information | substrate specificity | Zea mays | ? | - |
? | |
| 1.14.14.154 | additional information | no activity with 31-norlanosterol, cycloeucalenol, 4alpha,14alpha-dimethyl-5alpha-ergost-9(11)-en-3beta-ol, 4alpha,14alpha-dimethyl-5alpha-ergost-7-en-3beta-ol, 8(9),24(25)-tetrahydro-31-norlanosterol, 24-methylenelanosterol, 24,28-dihydro-4beta-methyl-30-norobtusifoliol, 24,25-dihydrolanosterol, lanosterol, obtusifoliyl-3beta-methoxy, obtusifoliyl-3beta-acetoxy, obtusifoliyl-3beta-amino | Zea mays | ? | - |
? | |
| 1.14.14.154 | additional information | biosynthetic enzyme with very narrow substrate specificity | Zea mays | ? | - |
? | |
| 1.14.14.154 | additional information | P-450OBT 14DM has probably a specific apolar binding site for the side chain. DELTA8-double bond is absolute required for substrate demethylation and the 3-hydroxy group plays a critical role in enzyme-substrate interaction | Zea mays | ? | - |
? | |
| 1.14.14.154 | additional information | enzyme with high degree of substrate and product specificity | Zea mays | ? | - |
? | |
| 1.14.14.154 | additional information | plant sterol 14alpha-demethylase have high substrate specificity | Zea mays | ? | - |
? | |
| 1.14.14.154 | additional information | narrow substrate selectivity | Zea mays | ? | - |
? | |
| 1.14.14.154 | additional information | enzyme of sterol biosynthetic pathway | Zea mays | ? | - |
? | |
| 1.14.14.154 | additional information | enzyme of plant sterol, phytosterol, biosynthesis | Zea mays | ? | - |
? | |
| 1.14.14.154 | additional information | substrate specificity | Zea mays LG11 | ? | - |
? | |
| 1.14.14.154 | additional information | no activity with 31-norlanosterol, cycloeucalenol, 4alpha,14alpha-dimethyl-5alpha-ergost-9(11)-en-3beta-ol, 4alpha,14alpha-dimethyl-5alpha-ergost-7-en-3beta-ol, 8(9),24(25)-tetrahydro-31-norlanosterol, 24-methylenelanosterol, 24,28-dihydro-4beta-methyl-30-norobtusifoliol, 24,25-dihydrolanosterol, lanosterol, obtusifoliyl-3beta-methoxy, obtusifoliyl-3beta-acetoxy, obtusifoliyl-3beta-amino | Zea mays LG11 | ? | - |
? | |
| 1.14.14.154 | additional information | biosynthetic enzyme with very narrow substrate specificity | Zea mays LG11 | ? | - |
? | |
| 1.14.14.154 | additional information | P-450OBT 14DM has probably a specific apolar binding site for the side chain. DELTA8-double bond is absolute required for substrate demethylation and the 3-hydroxy group plays a critical role in enzyme-substrate interaction | Zea mays LG11 | ? | - |
? | |
| 1.14.14.154 | additional information | enzyme with high degree of substrate and product specificity | Zea mays LG11 | ? | - |
? | |
| 1.14.14.154 | obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | best substrate | Zea mays | 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 | Zea mays | 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 | Zea mays | 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 | Zea mays | 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.154 | 30 | - |
assay at | Zea mays |
| 1.14.14.154 | 30 | - |
aerobic conditions | Zea mays |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.154 | 7.5 | 8.5 | - |
Zea mays |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.154 | 6.5 | 9.5 | - |
Zea mays |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.154 | cytochrome P450 | - |
Zea mays | |
| 1.14.14.154 | heme | heme-thiolate enzyme | Zea mays | |
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
