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Literature summary for 1.14.14.154 extracted from

  • Kahn, R.A.; Bak, S.; Olsen, C.E.; Svendsen, I.; Moller, B.L.
    Isolation and reconstitution of the heme-thiolate protein obtusifoliol 14alpha-demethylase from Sorghum bicolor (L.) Moench (1996), J. Biol. Chem., 271, 32944-32950.
    View publication on PubMed

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 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

Inhibitors Comment Organism Structure
CO
-
Sorghum bicolor

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Sorghum bicolor 16020
-
microsome
-
Embryophyta
-
-
microsome
-
Sorghum bicolor
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
53000
-
SDS-PAGE and amino acid sequence analysis Sorghum bicolor

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Embryophyta
-
higher plants
-
Sorghum bicolor
-
L., Moench
-

Purification (Commentary)

Purification (Comment) Organism
purification and reconstitution Sorghum bicolor

Source Tissue

Source Tissue Comment Organism Textmining
seedling etiolated Sorghum seedlings Sorghum bicolor
-

Storage Stability

Storage Stability Organism
-80°C, frozen in liquid nitrogen Sorghum bicolor

Substrates and Products (Substrate)

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

Subunits Comment Organism
monomer 1 * 53000, SDS-PAGE Sorghum bicolor

Cofactor

Cofactor Comment Organism Structure
cytochrome P450
-
Embryophyta
cytochrome P450
-
Sorghum bicolor
heme heme-thiolate enzyme Embryophyta
heme heme-thiolate enzyme Sorghum bicolor