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Literature summary for 1.14.14.154 extracted from

  • Taton, M.; Rahier, A.
    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.
    View publication on PubMedView publication on EuropePMC

Application

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 Zea mays
agriculture target of important agrochemicals such as fungicides, plant growth regulators and herbicides Zea mays
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
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

General Stability Organism
plant demethylase is remarkably stable Zea mays

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic parameters Zea mays
0.116
-
(3beta,4alpha,5alpha)-4,14-dimethylcholest-8-en-3-ol
-
Zea mays
0.16
-
obtusifoliol
-
Zea mays

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
Zea mays 5783
-
endoplasmic reticulum light membrane fraction of endoplasmic reticulum, not in plasma membrane Zea mays 5783
-
membrane membrane-bound Zea mays 16020
-
microsome microsomal-bound Zea mays
-
-
additional information not in plasma membrane Zea mays
-
-
additional information subcellular localization, distribution Zea mays
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Zea mays enzyme of sterol biosynthetic pathway ?
-
?
additional information Zea mays enzyme of plant sterol, phytosterol, biosynthesis ?
-
?
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
-
?
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

Organism UniProt Comment Textmining
Zea mays
-
maize
-
Zea mays
-
LG11
-
Zea mays LG11
-
LG11
-

Reaction

Reaction Comment Organism Reaction ID
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

Source Tissue Comment Organism Textmining
seedling
-
Zea mays
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(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
-
?
(3beta,4alpha,5alpha)-4,14-dimethylcholest-8-en-3-ol + [reduced NADPH-hemoprotein reductase] + O2
-
Zea mays ?
-
r
14alpha-methyl-24,28-dihydrofecosterol + [reduced NADPH-hemoprotein reductase] + O2 50% of activity compared to obtusifoliol Zea mays ? + formate + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
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
-
?
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
-
?
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
-
?
additional information substrate specificity Zea mays ?
-
?
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 ?
-
?
additional information biosynthetic enzyme with very narrow substrate specificity Zea mays ?
-
?
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 ?
-
?
additional information enzyme with high degree of substrate and product specificity Zea mays ?
-
?
additional information plant sterol 14alpha-demethylase have high substrate specificity Zea mays ?
-
?
additional information narrow substrate selectivity Zea mays ?
-
?
additional information enzyme of sterol biosynthetic pathway Zea mays ?
-
?
additional information enzyme of plant sterol, phytosterol, biosynthesis Zea mays ?
-
?
additional information substrate specificity Zea mays LG11 ?
-
?
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 ?
-
?
additional information biosynthetic enzyme with very narrow substrate specificity Zea mays LG11 ?
-
?
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 ?
-
?
additional information enzyme with high degree of substrate and product specificity Zea mays LG11 ?
-
?
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
-
?
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
-
?
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
-
?
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]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Zea mays
30
-
aerobic conditions Zea mays

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8.5
-
Zea mays

pH Range

pH Minimum pH Maximum Comment Organism
6.5 9.5
-
Zea mays

Cofactor

Cofactor Comment Organism Structure
cytochrome P450
-
Zea mays
heme heme-thiolate enzyme Zea mays