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Literature summary for 1.14.14.154 extracted from
- Yeast cytochrome P-450 catalyzing lanosterol 14alpha-demethylation. II. Lanosterol metabolism by purified P-45014DM and by intact microsomes (1984), J. Biol. Chem., 259, 1661-1666.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| lanosterol | induction and activation | Saccharomyces cerevisiae |  |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| anti-P-45014DM antibodies | complete inhibition | Saccharomyces cerevisiae | |
| CO | ratio CO:O2 of 90:10, 51.1% inhibition, ratio CO:O2 of 95:5, 100% inhibition | Saccharomyces cerevisiae | |
| menadione | 0.125 mM: 62.1% inhibition | Saccharomyces cerevisiae | |
| Metyrapone | strong inhibition, 0.1 mM: 57.3% inhibition | Saccharomyces cerevisiae | |
| nitrogen | nitrogen atmosphere | Saccharomyces cerevisiae | |
| SKF-525A | potent inhibitor, 1.0 mM: 100% inhibition | Saccharomyces cerevisiae | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics | Saccharomyces cerevisiae |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| microsome | - |
Saccharomyces cerevisiae | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Saccharomyces cerevisiae | natural substrate | 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
| lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Saccharomyces cerevisiae | lanosta-8,24-dien-3beta-ol | 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
| lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Saccharomyces cerevisiae | 4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol | 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
| lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Saccharomyces cerevisiae | P-45014DM catalyzes all three oxygenation steps from lanosterol to dimethylcholestratrienol | 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
| lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Saccharomyces cerevisiae | ergosterol synthesis in yeast involves oxidative removal of the 14alpha-methyl group, C-32, of lanosterol | 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Saccharomyces cerevisiae |
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 | Saccharomyces cerevisiae | |
| a 14alpha-methylsteroid + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = a DELTA14-steroid + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O | stoichiometry | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | natural substrate | Saccharomyces cerevisiae | 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
| lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | lanosta-8,24-dien-3beta-ol | Saccharomyces cerevisiae | 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
| lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | 4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol | Saccharomyces cerevisiae | 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
| lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | P-45014DM catalyzes all three oxygenation steps from lanosterol to dimethylcholestratrienol | Saccharomyces cerevisiae | 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
| lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | ergosterol synthesis in yeast involves oxidative removal of the 14alpha-methyl group, C-32, of lanosterol | Saccharomyces cerevisiae | 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
| additional information | reaction reqires molecular oxygen, does not occur anaerobically | Saccharomyces cerevisiae | ? | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Saccharomyces cerevisiae |
| 30 | - |
aerobic conditions | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Saccharomyces cerevisiae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| cytochrome P450 | - |
Saccharomyces cerevisiae | |
| heme | heme-thiolate enzyme | Saccharomyces cerevisiae | |
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