Cloned (Comment) | Organism |
---|---|
sequence comparison, phylogenetic analysis, heterologous overexpression | Homo sapiens |
sequence comparison, phylogenetic analysis, heterologous overexpression | Rattus norvegicus |
sequence comparison, phylogenetic analysis, heterologous overexpression | Saccharomyces cerevisiae |
sequence comparison, phylogenetic analysis, heterologous overexpression | Mycolicibacterium smegmatis |
sequence comparison, phylogenetic analysis, heterologous overexpression | Trypanosoma brucei |
sequence comparison, phylogenetic analysis, heterologous overexpression | Mycobacterium tuberculosis |
sequence comparison, phylogenetic analysis, heterologous overexpression | Trypanosoma cruzi |
sequence comparison, phylogenetic analysis, heterologous overexpression | Candida albicans |
sequence comparison, phylogenetic analysis, heterologous overexpression | Sorghum bicolor |
sequence comparison, phylogenetic analysis, heterologous overexpression | Methylococcus capsulatus |
sequence comparison, phylogenetic analysis, heterologous overexpression | Ustilago maydis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
14alpha-amino-lanosterol | - |
Candida albicans | |
14alpha-amino-lanosterol | - |
Trypanosoma cruzi | |
15-hydroxy-lanosterol | - |
Homo sapiens | |
15-keto-lanosterol | - |
Homo sapiens | |
26-oxo-lanosterol | - |
Homo sapiens | |
7-oxo-lanosterol | - |
Homo sapiens | |
imidazole inhibitors | - |
Candida albicans | |
imidazole inhibitors | - |
Homo sapiens | |
imidazole inhibitors | - |
Methylococcus capsulatus | |
imidazole inhibitors | - |
Mycobacterium tuberculosis | |
imidazole inhibitors | - |
Mycolicibacterium smegmatis | |
imidazole inhibitors | - |
Rattus norvegicus | |
imidazole inhibitors | - |
Saccharomyces cerevisiae | |
imidazole inhibitors | - |
Sorghum bicolor | |
imidazole inhibitors | - |
Trypanosoma brucei | |
imidazole inhibitors | - |
Trypanosoma cruzi | |
imidazole inhibitors | - |
Ustilago maydis | |
additional information | 14alpha-carboaldehyde reaction intermediates are effective in competitive enzyme inhibition and as hypocholesterolemic agents | Homo sapiens | |
triazole inhibitors | - |
Candida albicans | |
triazole inhibitors | - |
Homo sapiens | |
triazole inhibitors | - |
Methylococcus capsulatus | |
triazole inhibitors | - |
Mycobacterium tuberculosis | |
triazole inhibitors | - |
Mycolicibacterium smegmatis | |
triazole inhibitors | - |
Rattus norvegicus | |
triazole inhibitors | - |
Saccharomyces cerevisiae | |
triazole inhibitors | - |
Sorghum bicolor | |
triazole inhibitors | - |
Trypanosoma brucei | |
triazole inhibitors | - |
Trypanosoma cruzi | |
triazole inhibitors | - |
Ustilago maydis |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
microsome | - |
Homo sapiens | - |
- |
microsome | - |
Rattus norvegicus | - |
- |
microsome | - |
Saccharomyces cerevisiae | - |
- |
microsome | - |
Trypanosoma brucei | - |
- |
microsome | - |
Trypanosoma cruzi | - |
- |
microsome | - |
Candida albicans | - |
- |
microsome | - |
Sorghum bicolor | - |
- |
microsome | - |
Ustilago maydis | - |
- |
soluble | - |
Mycolicibacterium smegmatis | - |
- |
soluble | - |
Mycobacterium tuberculosis | - |
- |
soluble | - |
Methylococcus capsulatus | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Homo sapiens | the enzyme is involved in ergosterol and cholesterol biosynthesis | ? | - |
? | |
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Rattus norvegicus | the enzyme is involved in ergosterol and cholesterol biosynthesis | ? | - |
? | |
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Saccharomyces cerevisiae | the enzyme is involved in ergosterol and cholesterol biosynthesis | ? | - |
? | |
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Mycobacterium tuberculosis | the enzyme is involved in ergosterol and cholesterol biosynthesis | ? | - |
? | |
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Candida albicans | the enzyme is involved in ergosterol and cholesterol biosynthesis | ? | - |
? | |
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Mycobacterium tuberculosis | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | ? | - |
? | |
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Trypanosoma cruzi | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | ? | - |
? | |
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Ustilago maydis | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Saccharomyces cerevisiae | - |
? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Homo sapiens | the enzyme is involved in ergosterol and cholesterol biosynthesis | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Rattus norvegicus | the enzyme is involved in ergosterol and cholesterol biosynthesis | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Mycolicibacterium smegmatis | the enzyme is involved in ergosterol and cholesterol biosynthesis | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Mycobacterium tuberculosis | the enzyme is involved in ergosterol and cholesterol biosynthesis | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Candida albicans | the enzyme is involved in ergosterol and cholesterol biosynthesis | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Methylococcus capsulatus | the enzyme is involved in ergosterol and cholesterol biosynthesis | ? | - |
? | |
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Trypanosoma brucei | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | ? | - |
? | |
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Mycobacterium tuberculosis | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | ? | - |
? | |
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2 | Trypanosoma cruzi | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | ? | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | Trypanosoma brucei | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | 4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | Mycobacterium tuberculosis | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | 4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | Trypanosoma cruzi | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | 4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | Sorghum bicolor | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | 4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Candida albicans | - |
- |
- |
Homo sapiens | - |
- |
- |
Methylococcus capsulatus | - |
- |
- |
Mycobacterium tuberculosis | - |
- |
- |
Mycolicibacterium smegmatis | - |
- |
- |
Rattus norvegicus | - |
- |
- |
Saccharomyces cerevisiae | - |
- |
- |
Sorghum bicolor | - |
- |
- |
Trypanosoma brucei | - |
- |
- |
Trypanosoma cruzi | - |
- |
- |
Ustilago maydis | - |
- |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
substrate specificity | Homo sapiens |
additional information | - |
substrate specificity | Rattus norvegicus |
additional information | - |
substrate specificity | Saccharomyces cerevisiae |
additional information | - |
substrate specificity | Mycolicibacterium smegmatis |
additional information | - |
substrate specificity | Trypanosoma brucei |
additional information | - |
substrate specificity | Mycobacterium tuberculosis |
additional information | - |
substrate specificity | Trypanosoma cruzi |
additional information | - |
substrate specificity | Candida albicans |
additional information | - |
substrate specificity | Sorghum bicolor |
additional information | - |
substrate specificity | Methylococcus capsulatus |
additional information | - |
substrate specificity | Ustilago maydis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Homo sapiens | ? | - |
? | |
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Rattus norvegicus | ? | - |
? | |
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Saccharomyces cerevisiae | ? | - |
? | |
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Mycobacterium tuberculosis | ? | - |
? | |
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Trypanosoma cruzi | ? | - |
? | |
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Candida albicans | ? | - |
? | |
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in ergosterol and cholesterol biosynthesis | Homo sapiens | ? | - |
? | |
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in ergosterol and cholesterol biosynthesis | Rattus norvegicus | ? | - |
? | |
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in ergosterol and cholesterol biosynthesis | Saccharomyces cerevisiae | ? | - |
? | |
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in ergosterol and cholesterol biosynthesis | Mycobacterium tuberculosis | ? | - |
? | |
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in ergosterol and cholesterol biosynthesis | Candida albicans | ? | - |
? | |
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Homo sapiens | ? | - |
? | |
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Saccharomyces cerevisiae | ? | - |
? | |
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Mycobacterium tuberculosis | ? | - |
? | |
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Trypanosoma cruzi | ? | - |
? | |
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Candida albicans | ? | - |
? | |
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Ustilago maydis | ? | - |
? | |
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | Mycobacterium tuberculosis | ? | - |
? | |
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | Trypanosoma cruzi | ? | - |
? | |
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | Ustilago maydis | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Homo sapiens | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Rattus norvegicus | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Saccharomyces cerevisiae | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Mycolicibacterium smegmatis | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Mycobacterium tuberculosis | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Trypanosoma cruzi | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Candida albicans | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Methylococcus capsulatus | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in ergosterol and cholesterol biosynthesis | Homo sapiens | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in ergosterol and cholesterol biosynthesis | Rattus norvegicus | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in ergosterol and cholesterol biosynthesis | Mycolicibacterium smegmatis | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in ergosterol and cholesterol biosynthesis | Mycobacterium tuberculosis | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in ergosterol and cholesterol biosynthesis | Candida albicans | ? | - |
? | |
lanosterol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in ergosterol and cholesterol biosynthesis | Methylococcus capsulatus | ? | - |
? | |
additional information | poor activity with lanosterol, 24,25-dihydrolanosterol, and 24-methylenedihydrolanosterol, the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core | Trypanosoma brucei | ? | - |
? | |
additional information | poor activity with lanosterol, 24,25-dihydrolanosterol, and 24-methylenedihydrolanosterol, the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core | Sorghum bicolor | ? | - |
? | |
additional information | the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core | Homo sapiens | ? | - |
? | |
additional information | the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core | Rattus norvegicus | ? | - |
? | |
additional information | the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core | Saccharomyces cerevisiae | ? | - |
? | |
additional information | the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core | Mycolicibacterium smegmatis | ? | - |
? | |
additional information | the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core | Mycobacterium tuberculosis | ? | - |
? | |
additional information | the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core | Trypanosoma cruzi | ? | - |
? | |
additional information | the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core | Candida albicans | ? | - |
? | |
additional information | the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core | Methylococcus capsulatus | ? | - |
? | |
additional information | the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxygen and two NADPH-derived reducing equivalents, via 14alpha-carboxyalcohol and 14alpha-carboxyaldehyde intermediates, cleavage of the the C-C bond by radical or Bayer-Villiger mechanism, DELTA14,15 double bond introduction into the sterol core | Ustilago maydis | ? | - |
? | |
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Homo sapiens | ? | - |
? | |
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Trypanosoma brucei | ? | - |
? | |
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Mycobacterium tuberculosis | ? | - |
? | |
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Candida albicans | ? | - |
? | |
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Sorghum bicolor | ? | - |
? | |
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2 | low activity | Trypanosoma cruzi | ? | - |
? | |
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | Trypanosoma brucei | ? | - |
? | |
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | Mycobacterium tuberculosis | ? | - |
? | |
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | Trypanosoma cruzi | ? | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Homo sapiens | 4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Trypanosoma brucei | 4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | - |
Sorghum bicolor | 4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | low activity | Trypanosoma cruzi | 4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | preferred substrate | Mycobacterium tuberculosis | 4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | preferred substrate | Candida albicans | 4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | Trypanosoma brucei | 4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | Mycobacterium tuberculosis | 4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | Trypanosoma cruzi | 4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2 | the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis | Sorghum bicolor | 4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | comparison of CYP51 family enzyme structures, overview | Homo sapiens |
More | comparison of CYP51 family enzyme structures, overview | Rattus norvegicus |
More | comparison of CYP51 family enzyme structures, overview | Saccharomyces cerevisiae |
More | comparison of CYP51 family enzyme structures, overview | Mycolicibacterium smegmatis |
More | comparison of CYP51 family enzyme structures, overview | Trypanosoma brucei |
More | comparison of CYP51 family enzyme structures, overview | Mycobacterium tuberculosis |
More | comparison of CYP51 family enzyme structures, overview | Trypanosoma cruzi |
More | comparison of CYP51 family enzyme structures, overview | Candida albicans |
More | comparison of CYP51 family enzyme structures, overview | Sorghum bicolor |
More | comparison of CYP51 family enzyme structures, overview | Methylococcus capsulatus |
More | comparison of CYP51 family enzyme structures, overview | Ustilago maydis |
Synonyms | Comment | Organism |
---|---|---|
CYP51 | - |
Homo sapiens |
CYP51 | - |
Rattus norvegicus |
CYP51 | - |
Saccharomyces cerevisiae |
CYP51 | - |
Mycolicibacterium smegmatis |
CYP51 | - |
Trypanosoma brucei |
CYP51 | - |
Mycobacterium tuberculosis |
CYP51 | - |
Trypanosoma cruzi |
CYP51 | - |
Candida albicans |
CYP51 | - |
Sorghum bicolor |
CYP51 | - |
Methylococcus capsulatus |
CYP51 | - |
Ustilago maydis |
More | the enzyme belongs to the CYP51 family | Homo sapiens |
More | the enzyme belongs to the CYP51 family | Rattus norvegicus |
More | the enzyme belongs to the CYP51 family | Saccharomyces cerevisiae |
More | the enzyme belongs to the CYP51 family | Mycolicibacterium smegmatis |
More | the enzyme belongs to the CYP51 family | Trypanosoma brucei |
More | the enzyme belongs to the CYP51 family | Mycobacterium tuberculosis |
More | the enzyme belongs to the CYP51 family | Trypanosoma cruzi |
More | the enzyme belongs to the CYP51 family | Candida albicans |
More | the enzyme belongs to the CYP51 family | Sorghum bicolor |
More | the enzyme belongs to the CYP51 family | Methylococcus capsulatus |
More | the enzyme belongs to the CYP51 family | Ustilago maydis |
sterol 14alpha-demethylase cytochrome P 450 | - |
Homo sapiens |
sterol 14alpha-demethylase cytochrome P 450 | - |
Rattus norvegicus |
sterol 14alpha-demethylase cytochrome P 450 | - |
Saccharomyces cerevisiae |
sterol 14alpha-demethylase cytochrome P 450 | - |
Mycolicibacterium smegmatis |
sterol 14alpha-demethylase cytochrome P 450 | - |
Trypanosoma brucei |
sterol 14alpha-demethylase cytochrome P 450 | - |
Mycobacterium tuberculosis |
sterol 14alpha-demethylase cytochrome P 450 | - |
Trypanosoma cruzi |
sterol 14alpha-demethylase cytochrome P 450 | - |
Candida albicans |
sterol 14alpha-demethylase cytochrome P 450 | - |
Sorghum bicolor |
sterol 14alpha-demethylase cytochrome P 450 | - |
Methylococcus capsulatus |
sterol 14alpha-demethylase cytochrome P 450 | - |
Ustilago maydis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
Ferredoxin | a ferredoxin-bound enzyme | Methylococcus capsulatus |