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Information on EC 1.14.14.154 - sterol 14alpha-demethylase and Organism(s) Trypanosoma cruzi and UniProt Accession Q7Z1V1

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IUBMB Comments
This cytochrome P-450 (heme-thiolate) enzyme acts on a range of steroids with a 14alpha-methyl group, such as obtusifoliol and lanosterol. The enzyme catalyses a hydroxylation and a reduction of the 14alpha-methyl group, followed by a second hydroxylation, resulting in the elimination of formate and formation of a 14(15) double bond.
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This record set is specific for:
Trypanosoma cruzi
UNIPROT: Q7Z1V1
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The taxonomic range for the selected organisms is: Trypanosoma cruzi
The enzyme appears in selected viruses and cellular organisms
Synonyms
cyp51, erg11, cyp51a, cyp51a1, erg11p, cyp51b, lanosterol 14alpha-demethylase, lanosterol 14 alpha-demethylase, lanosterol demethylase, sterol 14alpha-demethylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sterol 14alpha-demethylase
-
14-demethylase
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14alpha-demethylase
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14alpha-methylsterol 14alpha-demethylase
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14alpha-sterol demethylase
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14DM
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CYP51
CYPL1
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cytochrome CYP51
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-
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cytochrome P 450 CYP51
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cytochrome P-450 lanosterol 14alpha-demethylase
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cytochrome P-450-dependent 14alpha-sterol demethylase
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cytochrome P-450-dependent obtusifoliol 14alpha-demethylase
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-
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cytochrome P-450/14DM
-
-
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cytochrome P-45014DM
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-
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cytochrome P450 14DM
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cytochrome P450 51
-
-
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cytochrome P450 CYP51
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-
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cytochrome-P450 14alpha-demethylase
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demethylase, methylsterol 14alpha-
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eburicol 14 alpha-demethylase
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eburicol 14alpha-demethylase
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lanosterol 14 alpha-demethylase
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lanosterol 14-demethylase
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lanosterol 14alpha-demethylase
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lanosterol 14alpha-methyldemethylase
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-
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lanosterol C-14 demethylase
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lanosterol demethylase
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LDM
-
-
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methylsterol 14alpha-demethylase (P 450 CYP51)
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Obtusifoliol 14-alpha demethylase
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obtusifoliol 14-demethylase
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obtusifoliol 14alpha-demethylase
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obtusifoliol-metabolizing 14alpha-demethylase
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-
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obtusufoliol 14-demethylase
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-
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P 450 lanosterol C-14 demethylase
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-
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P-450 lanosterol demethylase
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P-45014DM
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-
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P-45014DM-containing monooxygenase system
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-
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P-450OBT 14DM
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-
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P450(14DM)
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-
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P450-14DM
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-
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P450-L1A1
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P45014DM
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-
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sterol 14-demethylase
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sterol 14-demethylase P450
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sterol 14alpha-demethylase
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sterol 14alpha-demethylase (CYP51)
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sterol 14alpha-demethylase cytochrome P 450
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sterol C14 demethylase
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-
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sterol C14-demethylase
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additional information
-
the enzyme belongs to the CYP51 family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a 14alpha-methylsteroid + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = a DELTA14-steroid + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
show the reaction diagram
reaction mechanism, phyla-specific residues in CYP51
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxygenation
-
-
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redox reaction
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oxidation
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reduction
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hydroxylation
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monooxygenation
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-
-
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PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
sterol,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (14-methyl cleaving)
This cytochrome P-450 (heme-thiolate) enzyme acts on a range of steroids with a 14alpha-methyl group, such as obtusifoliol and lanosterol. The enzyme catalyses a hydroxylation and a reduction of the 14alpha-methyl group, followed by a second hydroxylation, resulting in the elimination of formate and formation of a 14(15) double bond.
CAS REGISTRY NUMBER
COMMENTARY hide
138674-19-8
deleted registry number
341989-59-1
deleted registry number
60063-87-8
-
90463-45-9
deleted registry number
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
active site contains an isoleucine, lanosterol is the preferred substrate
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
i.e. 4alpha,4alpha-dimethylcholesta-8,24-dien-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
preferred substrate
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
preferred substrate
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
i.e. 4alpha,4alpha-dimethylcholesta-8,24-dien-3beta-ol
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
preferred substrate
-
-
?
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
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-
?
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
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the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
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-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
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the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
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-
?
additional information
?
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the organism can specifically regulate gene expression, e.g. for the sterol C14-demethylase, in response to derangements in its cellular functions
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
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cytochrome P450
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-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
heme-iron in the active site
Iron
a heme iron, DELTA7–8 double bond location is more favorable for coordination of the amino nitrogen to the heme iron
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-4'-chloro-N-(1-(2,4-dichlorophenyl)-2-(1H-imidazol-1-yl)ethyl)biphenyl-4-carboxamide
VNF, complexes CYP51, binding structure, overview
(R)-N-(1-(2,4-dichlorophenyl)-2-(1H-imidazol-1-yl)ethyl)-4-(5-phenyl-1,3,4-oxadiazol-2-yl)-benzamide
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(R)-N-(2-(1H-imidazol-1-yl)-1-phenylethyl)-4'-chlorobiphenyl-4-carboxamide
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14alpha-aminomethyl-lanosterol derivatives
competitive
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7-chloro-3-[(2R,3R)-3-(2,4-difluorophenyl)-3-hydroxy-4-(1H-1,2,4-triazol-1-yl)butan-2-yl]-4a,8a-dihydroquinazolin-4(3H)-one
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fluconazole
posaconazole
14alpha-amino-lanosterol
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2-phenyl-N-pyridin-4-ylbutanamide
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2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-(1-pyridin-4-ylethyl)acetamide
-
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2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-(2-phenylpropyl)acetamide
-
most potent inhibitor, antiparasitic activities at concentrations less than 0.01 mM
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-(2-pyridin-3-ylethyl)acetamide
-
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2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-(pyridin-2-ylmethyl)acetamide
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2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-(pyridin-4-ylmethyl)acetamide
-
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2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-pyridin-2-ylacetamide
-
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2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-pyridin-3-ylacetamide
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2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-pyrimidin-2-ylacetamide
-
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2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-[(6-chloropyridin-3-yl)methyl]acetamide
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2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-[2-(3-chlorophenyl)ethyl]acetamide
-
most potent inhibitor, antiparasitic activities at concentrations less than 0.01 mM
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-[[6-(trifluoromethyl)pyridin-3-yl]methyl]acetamide
-
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3-(2-furyl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole
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most potent inhibitor
3-benzyl-1-pyridin-4-ylpyrrolidine-2,5-dione
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3-methyl-4-nitro-N-pyridin-4-ylbenzamide
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3-oxo-N-pyridin-4-yl-3H-benzo[f]chromene-2-carboxamide
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3-thien-2-yl-5,6-dihydroimidazo[2,1-b][1,3]thiazole
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imidazole inhibitors
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N-pyridin-4-yl-9H-xanthene-9-carboxamide
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strongest binding compound
Nalpha-[(4-methylcyclohexyl)carbonyl]-N-pyridin-4-yltryptophanamide
-
strongest binding compound
triazole inhibitors
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-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
the lanosterol synthase inhibitor terbinafine and inhibition of squalene epoxidase and lanosterol synthase induce the transcription and translation of the enzyme about 7-12fold, upregulation is mediated through the 3'-untranslated region of the gene
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000001
7-chloro-3-[(2R,3R)-3-(2,4-difluorophenyl)-3-hydroxy-4-(1H-1,2,4-triazol-1-yl)butan-2-yl]-4a,8a-dihydroquinazolin-4(3H)-one
Trypanosoma cruzi
strain EP or Y, intracellular amastigote, Vero cell as host cell
0.0015 - 0.02
benznidazole
0.00001 - 0.0001
D0870
0.02
econazole
Trypanosoma cruzi
strain Tulahuen, epimastigote
0.008 - 0.1
fluconazole
0.000001 - 0.001
itraconazole
0.000001 - 0.03
ketoconazole
0.00002 - 0.02
miconazole
0.00000025 - 0.0005
posaconazole
0.0000001 - 0.0001
ravuconazole
0.0000003
TAK-187
Trypanosoma cruzi
strain EP or Y, intracellular amastigote, Vero cell as host cell
0.000004 - 0.03
voriconazole
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
-
x * 52000, SDS-PAGE, recombinant enzyme
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 52000, SDS-PAGE, recombinant enzyme
additional information
-
comparison of CYP51 family enzyme structures, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
for crystallization purposes, an N-terminal truncated construct is used where the membrane anchor sequence is replaced with the 5-amino acid sequence fragment MAKKT-. Crystals are grown at 23°C using the hanging-drop vapor diffusion method
purified recombinant C-terminally His-tagged enzyme, for crystallization purposes, the N-terminal transmembrane domain upstream of Pro32 is replaced with MAKKTSSKGKL- in the construct used for co-crystallization with fluconazole and (R)-4'-chloro-N-(1-(2,4-dichlorophenyl)-2-(1H-imid-azol-1-yl)ethyl)biphenyl-4-carboxamide, and with MAKKT-(5'-ATGGTCAAGAAAACG-3') in the complex with posaconazole, hanging drop vapour diffusion method, 25°C, from 0.260 mM cytochrome P450 solution in 20 mM potassium phosphate buffer, pH 7.2, containing 200 mM NaCl, 0.1 mM EDTA,10% glycerol, and 0.048mMn-tridecyl-beta-D-maltoside preincubated with 1.2fold molar excess of posaconazole, or (R)-4'-chloro-N-(1-(2,4-dichlorophenyl)-2-(1H-imid-azol-1-yl)ethyl)biphenyl-4-carboxamide, and 2-fold molar excess of fluconazole against an equal volume of well solution containing 0.2 M potassium formate, pH 7.2, or 0.2 M sodium formate, pH 7.4, in the case of (R)-4'-chloro-N-(1-(2,4-dichlorophenyl)-2-(1H-imid-azol-1-yl)ethyl)biphenyl-4-carboxamide, and 15% w/v PEG 3550, X-ray diffraction structure determination and analysis, modelling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I105F
sited-directed mutagenesis, exchange of the animal/fungi-like I105 B' helix residue for the F105 found in this position in all plant and the other six CYP51 sequences from Trypanosomatidae dramatically alters the mutant substrate specificity, activity with C4-methylsterol substrate is 3.5fold reduced and activity with norlanosterol and obtusifoliol is increased 150fold and 60fold, respectively, overview
additional information
-
enzyme is able to complement the function of the homologous gene in yeast
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His-tagged wild-type and mutant enzymes by nickel affinity chromatography and gel filtration
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography, and anion and cation exchange chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain HMS174(DE3)
expression of C-terminally His-tagged wild-type and mutant enzymes
gene CYP51, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, expression of His-tagged enzyme in Escherichia coli
expression of gene during both insect and mammalian life-cycle stage
-
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), usage of the luciferase expression system
-
sequence comparison, phylogenetic analysis, heterologous overexpression
-
subcloned into the pCW vector (Nde I/Hind III cloning sites) and expressed in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
pharmacology
Chagas disease is caused by the protozoan parasite Trypanosoma cruzi, which depends on the production of endogenous sterols, and therefore can be blocked by sterol 14alpha-demethylase inhibitors
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Buckner, F.S.; Joubert, B.M.; Boyle, S.M.; Eastman, R.T.; Verlinde, C.L.; Matsuda, S.P.
Cloning and analysis of Trypanosoma cruzi lanosterol 14alpha-demethylase
Mol. Biochem. Parasitol.
132
75-81
2003
Trypanosoma cruzi
Manually annotated by BRENDA team
Lepesheva, G.I.; Waterman, M.R.
Sterol 14alpha-demethylase cytochrome P 450 (CYP51), a P450 in all biological kingdoms
Biochim. Biophys. Acta
1770
467-477
2007
Candida albicans, Homo sapiens, Methylococcus capsulatus, Mycobacterium tuberculosis, Mycolicibacterium smegmatis, Rattus norvegicus, Saccharomyces cerevisiae, Sorghum bicolor, Trypanosoma brucei, Trypanosoma cruzi, Ustilago maydis
Manually annotated by BRENDA team
Lepesheva, G.I.; Zaitseva, N.G.; Nes, W.D.; Zhou, W.; Arase, M.; Liu, J.; Hill, G.C.; Waterman, M.R.
CYP51 from Trypanosoma cruzi: a phyla-specific residue in the B helix defines substrate preferences of sterol 14alpha-demethylase
J. Biol. Chem.
281
3577-3585
2006
Trypanosoma cruzi (Q7Z1V1), Trypanosoma cruzi
Manually annotated by BRENDA team
Hankins, E.G.; Gillespie, J.R.; Aikenhead, K.; Buckner, F.S.
Upregulation of sterol C14-demethylase expression in Trypanosoma cruzi treated with sterol biosynthesis inhibitors
Mol. Biochem. Parasitol.
144
68-75
2005
Trypanosoma cruzi
Manually annotated by BRENDA team
Buckner, F.S.
Sterol 14-demethylase inhibitors for Trypanosoma cruzi infections
Adv. Exp. Med. Biol.
625
61-80
2008
Candida albicans, Homo sapiens, Mycobacterium tuberculosis, Trypanosoma brucei, Trypanosoma cruzi (Q7Z1V1), Trypanosoma cruzi
Manually annotated by BRENDA team
Konkle, M.E.; Hargrove, T.Y.; Kleshchenko, Y.Y.; von Kries, J.P.; Ridenour, W.; Uddin, M.J.; Caprioli, R.M.; Marnett, L.J.; Nes, W.D.; Villalta, F.; Waterman, M.R.; Lepesheva, G.I.
Indomethacin amides as a novel molecular scaffold for targeting Trypanosoma cruzi sterol 14alpha-demethylase
J. Med. Chem.
52
2846-2853
2009
Trypanosoma cruzi
Manually annotated by BRENDA team
Lepesheva, G.I.; Hargrove, T.Y.; Anderson, S.; Kleshchenko, Y.; Furtak, V.; Wawrzak, Z.; Villalta, F.; Waterman, M.R.
Structural insights into inhibition of sterol 14alpha-demethylase in the human pathogen Trypanosoma cruzi
J. Biol. Chem.
285
25582-25590
2010
Trypanosoma cruzi (Q7Z1V1), Trypanosoma cruzi
Manually annotated by BRENDA team
Friggeri, L.; Hargrove, T.Y.; Rachakonda, G.; Williams, A.D.; Wawrzak, Z.; Di Santo, R.; De Vita, D.; Waterman, M.R.; Tortorella, S.; Villalta, F.; Lepesheva, G.I.
Structural basis for rational design of inhibitors targeting Trypanosoma cruzi sterol 14alpha-demethylase two regions of the enzyme molecule potentiate its inhibition
J. Med. Chem.
57
6704-6717
2014
Trypanosoma cruzi (Q7Z1V1), Trypanosoma cruzi, Trypanosoma cruzi CL Brener (Q7Z1V1)
Manually annotated by BRENDA team