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Literature summary for 1.14.14.154 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)

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

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

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/ Products (Substrates)

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

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 [micromol/min/mg]

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 and Products (Substrate)

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

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

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

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