Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Lepesheva, G.I.; Waterman, M.R.
    Sterol 14alpha-demethylase cytochrome P 450 (CYP51), a P450 in all biological kingdoms (2007), Biochim. Biophys. Acta, 1770, 467-477.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.154 sequence comparison, phylogenetic analysis, heterologous overexpression Homo sapiens
1.14.14.154 sequence comparison, phylogenetic analysis, heterologous overexpression Rattus norvegicus
1.14.14.154 sequence comparison, phylogenetic analysis, heterologous overexpression Saccharomyces cerevisiae
1.14.14.154 sequence comparison, phylogenetic analysis, heterologous overexpression Mycolicibacterium smegmatis
1.14.14.154 sequence comparison, phylogenetic analysis, heterologous overexpression Trypanosoma brucei
1.14.14.154 sequence comparison, phylogenetic analysis, heterologous overexpression Mycobacterium tuberculosis
1.14.14.154 sequence comparison, phylogenetic analysis, heterologous overexpression Trypanosoma cruzi
1.14.14.154 sequence comparison, phylogenetic analysis, heterologous overexpression Candida albicans
1.14.14.154 sequence comparison, phylogenetic analysis, heterologous overexpression Sorghum bicolor
1.14.14.154 sequence comparison, phylogenetic analysis, heterologous overexpression Methylococcus capsulatus
1.14.14.154 sequence comparison, phylogenetic analysis, heterologous overexpression Ustilago maydis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.154 14alpha-amino-lanosterol
-
Candida albicans
1.14.14.154 14alpha-amino-lanosterol
-
Trypanosoma cruzi
1.14.14.154 15-hydroxy-lanosterol
-
Homo sapiens
1.14.14.154 15-keto-lanosterol
-
Homo sapiens
1.14.14.154 26-oxo-lanosterol
-
Homo sapiens
1.14.14.154 7-oxo-lanosterol
-
Homo sapiens
1.14.14.154 imidazole inhibitors
-
Candida albicans
1.14.14.154 imidazole inhibitors
-
Homo sapiens
1.14.14.154 imidazole inhibitors
-
Methylococcus capsulatus
1.14.14.154 imidazole inhibitors
-
Mycobacterium tuberculosis
1.14.14.154 imidazole inhibitors
-
Mycolicibacterium smegmatis
1.14.14.154 imidazole inhibitors
-
Rattus norvegicus
1.14.14.154 imidazole inhibitors
-
Saccharomyces cerevisiae
1.14.14.154 imidazole inhibitors
-
Sorghum bicolor
1.14.14.154 imidazole inhibitors
-
Trypanosoma brucei
1.14.14.154 imidazole inhibitors
-
Trypanosoma cruzi
1.14.14.154 imidazole inhibitors
-
Ustilago maydis
1.14.14.154 additional information 14alpha-carboaldehyde reaction intermediates are effective in competitive enzyme inhibition and as hypocholesterolemic agents Homo sapiens
1.14.14.154 triazole inhibitors
-
Candida albicans
1.14.14.154 triazole inhibitors
-
Homo sapiens
1.14.14.154 triazole inhibitors
-
Methylococcus capsulatus
1.14.14.154 triazole inhibitors
-
Mycobacterium tuberculosis
1.14.14.154 triazole inhibitors
-
Mycolicibacterium smegmatis
1.14.14.154 triazole inhibitors
-
Rattus norvegicus
1.14.14.154 triazole inhibitors
-
Saccharomyces cerevisiae
1.14.14.154 triazole inhibitors
-
Sorghum bicolor
1.14.14.154 triazole inhibitors
-
Trypanosoma brucei
1.14.14.154 triazole inhibitors
-
Trypanosoma cruzi
1.14.14.154 triazole inhibitors
-
Ustilago maydis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.14.154 microsome
-
Homo sapiens
-
-
1.14.14.154 microsome
-
Rattus norvegicus
-
-
1.14.14.154 microsome
-
Saccharomyces cerevisiae
-
-
1.14.14.154 microsome
-
Trypanosoma brucei
-
-
1.14.14.154 microsome
-
Trypanosoma cruzi
-
-
1.14.14.154 microsome
-
Candida albicans
-
-
1.14.14.154 microsome
-
Sorghum bicolor
-
-
1.14.14.154 microsome
-
Ustilago maydis
-
-
1.14.14.154 soluble
-
Mycolicibacterium smegmatis
-
-
1.14.14.154 soluble
-
Mycobacterium tuberculosis
-
-
1.14.14.154 soluble
-
Methylococcus capsulatus
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.154 24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 Homo sapiens the enzyme is involved in ergosterol and cholesterol biosynthesis ?
-
?
1.14.14.154 24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 Rattus norvegicus the enzyme is involved in ergosterol and cholesterol biosynthesis ?
-
?
1.14.14.154 24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 Saccharomyces cerevisiae the enzyme is involved in ergosterol and cholesterol biosynthesis ?
-
?
1.14.14.154 24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 Mycobacterium tuberculosis the enzyme is involved in ergosterol and cholesterol biosynthesis ?
-
?
1.14.14.154 24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 Candida albicans the enzyme is involved in ergosterol and cholesterol biosynthesis ?
-
?
1.14.14.154 24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 Mycobacterium tuberculosis the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis ?
-
?
1.14.14.154 24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 Trypanosoma cruzi the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis ?
-
?
1.14.14.154 24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 Ustilago maydis the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2 Saccharomyces cerevisiae
-
?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2 Homo sapiens the enzyme is involved in ergosterol and cholesterol biosynthesis ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2 Rattus norvegicus the enzyme is involved in ergosterol and cholesterol biosynthesis ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2 Mycolicibacterium smegmatis the enzyme is involved in ergosterol and cholesterol biosynthesis ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2 Mycobacterium tuberculosis the enzyme is involved in ergosterol and cholesterol biosynthesis ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2 Candida albicans the enzyme is involved in ergosterol and cholesterol biosynthesis ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2 Methylococcus capsulatus the enzyme is involved in ergosterol and cholesterol biosynthesis ?
-
?
1.14.14.154 norlanosterol + [reduced NADPH-hemoprotein reductase] + O2 Trypanosoma brucei the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis ?
-
?
1.14.14.154 norlanosterol + [reduced NADPH-hemoprotein reductase] + O2 Mycobacterium tuberculosis the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis ?
-
?
1.14.14.154 norlanosterol + [reduced NADPH-hemoprotein reductase] + O2 Trypanosoma cruzi the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis ?
-
?
1.14.14.154 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
-
?
1.14.14.154 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
-
?
1.14.14.154 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
-
?
1.14.14.154 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

EC Number Organism UniProt Comment Textmining
1.14.14.154 Candida albicans
-
-
-
1.14.14.154 Homo sapiens
-
-
-
1.14.14.154 Methylococcus capsulatus
-
-
-
1.14.14.154 Mycobacterium tuberculosis
-
-
-
1.14.14.154 Mycolicibacterium smegmatis
-
-
-
1.14.14.154 Rattus norvegicus
-
-
-
1.14.14.154 Saccharomyces cerevisiae
-
-
-
1.14.14.154 Sorghum bicolor
-
-
-
1.14.14.154 Trypanosoma brucei
-
-
-
1.14.14.154 Trypanosoma cruzi
-
-
-
1.14.14.154 Ustilago maydis
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.14.14.154 additional information
-
substrate specificity Homo sapiens
1.14.14.154 additional information
-
substrate specificity Rattus norvegicus
1.14.14.154 additional information
-
substrate specificity Saccharomyces cerevisiae
1.14.14.154 additional information
-
substrate specificity Mycolicibacterium smegmatis
1.14.14.154 additional information
-
substrate specificity Trypanosoma brucei
1.14.14.154 additional information
-
substrate specificity Mycobacterium tuberculosis
1.14.14.154 additional information
-
substrate specificity Trypanosoma cruzi
1.14.14.154 additional information
-
substrate specificity Candida albicans
1.14.14.154 additional information
-
substrate specificity Sorghum bicolor
1.14.14.154 additional information
-
substrate specificity Methylococcus capsulatus
1.14.14.154 additional information
-
substrate specificity Ustilago maydis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.154 24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Homo sapiens ?
-
?
1.14.14.154 24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Rattus norvegicus ?
-
?
1.14.14.154 24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Saccharomyces cerevisiae ?
-
?
1.14.14.154 24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Mycobacterium tuberculosis ?
-
?
1.14.14.154 24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Trypanosoma cruzi ?
-
?
1.14.14.154 24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Candida albicans ?
-
?
1.14.14.154 24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 the enzyme is involved in ergosterol and cholesterol biosynthesis Homo sapiens ?
-
?
1.14.14.154 24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 the enzyme is involved in ergosterol and cholesterol biosynthesis Rattus norvegicus ?
-
?
1.14.14.154 24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 the enzyme is involved in ergosterol and cholesterol biosynthesis Saccharomyces cerevisiae ?
-
?
1.14.14.154 24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 the enzyme is involved in ergosterol and cholesterol biosynthesis Mycobacterium tuberculosis ?
-
?
1.14.14.154 24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 the enzyme is involved in ergosterol and cholesterol biosynthesis Candida albicans ?
-
?
1.14.14.154 24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Homo sapiens ?
-
?
1.14.14.154 24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Saccharomyces cerevisiae ?
-
?
1.14.14.154 24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Mycobacterium tuberculosis ?
-
?
1.14.14.154 24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Trypanosoma cruzi ?
-
?
1.14.14.154 24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Candida albicans ?
-
?
1.14.14.154 24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Ustilago maydis ?
-
?
1.14.14.154 24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis Mycobacterium tuberculosis ?
-
?
1.14.14.154 24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis Trypanosoma cruzi ?
-
?
1.14.14.154 24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2 the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis Ustilago maydis ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Homo sapiens ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Rattus norvegicus ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Saccharomyces cerevisiae ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Mycolicibacterium smegmatis ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Mycobacterium tuberculosis ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Trypanosoma cruzi ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Candida albicans ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Methylococcus capsulatus ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2 the enzyme is involved in ergosterol and cholesterol biosynthesis Homo sapiens ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2 the enzyme is involved in ergosterol and cholesterol biosynthesis Rattus norvegicus ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2 the enzyme is involved in ergosterol and cholesterol biosynthesis Mycolicibacterium smegmatis ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2 the enzyme is involved in ergosterol and cholesterol biosynthesis Mycobacterium tuberculosis ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2 the enzyme is involved in ergosterol and cholesterol biosynthesis Candida albicans ?
-
?
1.14.14.154 lanosterol + [reduced NADPH-hemoprotein reductase] + O2 the enzyme is involved in ergosterol and cholesterol biosynthesis Methylococcus capsulatus ?
-
?
1.14.14.154 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 ?
-
?
1.14.14.154 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 ?
-
?
1.14.14.154 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 ?
-
?
1.14.14.154 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 ?
-
?
1.14.14.154 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 ?
-
?
1.14.14.154 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 ?
-
?
1.14.14.154 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 ?
-
?
1.14.14.154 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 ?
-
?
1.14.14.154 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 ?
-
?
1.14.14.154 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 ?
-
?
1.14.14.154 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 ?
-
?
1.14.14.154 norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Homo sapiens ?
-
?
1.14.14.154 norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Trypanosoma brucei ?
-
?
1.14.14.154 norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Mycobacterium tuberculosis ?
-
?
1.14.14.154 norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Candida albicans ?
-
?
1.14.14.154 norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Sorghum bicolor ?
-
?
1.14.14.154 norlanosterol + [reduced NADPH-hemoprotein reductase] + O2 low activity Trypanosoma cruzi ?
-
?
1.14.14.154 norlanosterol + [reduced NADPH-hemoprotein reductase] + O2 the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis Trypanosoma brucei ?
-
?
1.14.14.154 norlanosterol + [reduced NADPH-hemoprotein reductase] + O2 the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis Mycobacterium tuberculosis ?
-
?
1.14.14.154 norlanosterol + [reduced NADPH-hemoprotein reductase] + O2 the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis Trypanosoma cruzi ?
-
?
1.14.14.154 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
-
?
1.14.14.154 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
-
?
1.14.14.154 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
-
?
1.14.14.154 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
-
?
1.14.14.154 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
-
?
1.14.14.154 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
-
?
1.14.14.154 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
-
?
1.14.14.154 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
-
?
1.14.14.154 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
-
?
1.14.14.154 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

EC Number Subunits Comment Organism
1.14.14.154 More comparison of CYP51 family enzyme structures, overview Homo sapiens
1.14.14.154 More comparison of CYP51 family enzyme structures, overview Rattus norvegicus
1.14.14.154 More comparison of CYP51 family enzyme structures, overview Saccharomyces cerevisiae
1.14.14.154 More comparison of CYP51 family enzyme structures, overview Mycolicibacterium smegmatis
1.14.14.154 More comparison of CYP51 family enzyme structures, overview Trypanosoma brucei
1.14.14.154 More comparison of CYP51 family enzyme structures, overview Mycobacterium tuberculosis
1.14.14.154 More comparison of CYP51 family enzyme structures, overview Trypanosoma cruzi
1.14.14.154 More comparison of CYP51 family enzyme structures, overview Candida albicans
1.14.14.154 More comparison of CYP51 family enzyme structures, overview Sorghum bicolor
1.14.14.154 More comparison of CYP51 family enzyme structures, overview Methylococcus capsulatus
1.14.14.154 More comparison of CYP51 family enzyme structures, overview Ustilago maydis

Synonyms

EC Number Synonyms Comment Organism
1.14.14.154 CYP51
-
Homo sapiens
1.14.14.154 CYP51
-
Rattus norvegicus
1.14.14.154 CYP51
-
Saccharomyces cerevisiae
1.14.14.154 CYP51
-
Mycolicibacterium smegmatis
1.14.14.154 CYP51
-
Trypanosoma brucei
1.14.14.154 CYP51
-
Mycobacterium tuberculosis
1.14.14.154 CYP51
-
Trypanosoma cruzi
1.14.14.154 CYP51
-
Candida albicans
1.14.14.154 CYP51
-
Sorghum bicolor
1.14.14.154 CYP51
-
Methylococcus capsulatus
1.14.14.154 CYP51
-
Ustilago maydis
1.14.14.154 More the enzyme belongs to the CYP51 family Homo sapiens
1.14.14.154 More the enzyme belongs to the CYP51 family Rattus norvegicus
1.14.14.154 More the enzyme belongs to the CYP51 family Saccharomyces cerevisiae
1.14.14.154 More the enzyme belongs to the CYP51 family Mycolicibacterium smegmatis
1.14.14.154 More the enzyme belongs to the CYP51 family Trypanosoma brucei
1.14.14.154 More the enzyme belongs to the CYP51 family Mycobacterium tuberculosis
1.14.14.154 More the enzyme belongs to the CYP51 family Trypanosoma cruzi
1.14.14.154 More the enzyme belongs to the CYP51 family Candida albicans
1.14.14.154 More the enzyme belongs to the CYP51 family Sorghum bicolor
1.14.14.154 More the enzyme belongs to the CYP51 family Methylococcus capsulatus
1.14.14.154 More the enzyme belongs to the CYP51 family Ustilago maydis
1.14.14.154 sterol 14alpha-demethylase cytochrome P 450
-
Homo sapiens
1.14.14.154 sterol 14alpha-demethylase cytochrome P 450
-
Rattus norvegicus
1.14.14.154 sterol 14alpha-demethylase cytochrome P 450
-
Saccharomyces cerevisiae
1.14.14.154 sterol 14alpha-demethylase cytochrome P 450
-
Mycolicibacterium smegmatis
1.14.14.154 sterol 14alpha-demethylase cytochrome P 450
-
Trypanosoma brucei
1.14.14.154 sterol 14alpha-demethylase cytochrome P 450
-
Mycobacterium tuberculosis
1.14.14.154 sterol 14alpha-demethylase cytochrome P 450
-
Trypanosoma cruzi
1.14.14.154 sterol 14alpha-demethylase cytochrome P 450
-
Candida albicans
1.14.14.154 sterol 14alpha-demethylase cytochrome P 450
-
Sorghum bicolor
1.14.14.154 sterol 14alpha-demethylase cytochrome P 450
-
Methylococcus capsulatus
1.14.14.154 sterol 14alpha-demethylase cytochrome P 450
-
Ustilago maydis

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.154 Ferredoxin a ferredoxin-bound enzyme Methylococcus capsulatus