Information on EC 1.14.13.70 - sterol 14alpha-demethylase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.14.13.70
-
RECOMMENDED NAME
GeneOntology No.
sterol 14alpha-demethylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 14alpha-methylsteroid + 3 O2 + 3 NADPH + 3 H+ = a Delta14-steroid + formate + 3 NADP+ + 4 H2O
show the reaction diagram
mechanism
-
a 14alpha-methylsteroid + 3 O2 + 3 NADPH + 3 H+ = a Delta14-steroid + formate + 3 NADP+ + 4 H2O
show the reaction diagram
mechanism
-
a 14alpha-methylsteroid + 3 O2 + 3 NADPH + 3 H+ = a Delta14-steroid + formate + 3 NADP+ + 4 H2O
show the reaction diagram
stoichiometry
-
a 14alpha-methylsteroid + 3 O2 + 3 NADPH + 3 H+ = a Delta14-steroid + formate + 3 NADP+ + 4 H2O
show the reaction diagram
regulation
Q64654
a 14alpha-methylsteroid + 3 O2 + 3 NADPH + 3 H+ = a Delta14-steroid + formate + 3 NADP+ + 4 H2O
show the reaction diagram
The heme-thiolate enzyme, P-450, catalyses successive hydroxylations of the 14alpha-methyl group and C-15, followed by elimination as formate leaving the 14(15) double bond. This enzyme acts on a range of steroids with a 14alpha-methyl group
-
-
-
a 14alpha-methylsteroid + 3 O2 + 3 NADPH + 3 H+ = a Delta14-steroid + formate + 3 NADP+ + 4 H2O
show the reaction diagram
active site structure, structure-function relationship
-
a 14alpha-methylsteroid + 3 O2 + 3 NADPH + 3 H+ = a Delta14-steroid + formate + 3 NADP+ + 4 H2O
show the reaction diagram
heme iron reduction as a rate-limiting step
-
a 14alpha-methylsteroid + 3 O2 + 3 NADPH + 3 H+ = a Delta14-steroid + formate + 3 NADP+ + 4 H2O
show the reaction diagram
reaction mechanism, phyla-specific residues in CYP51
-
a 14alpha-methylsteroid + 3 O2 + 3 NADPH + 3 H+ = a Delta14-steroid + formate + 3 NADP+ + 4 H2O
show the reaction diagram
mechanism
Zea mays LG11
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydroxylation
-
-
-
-
monooxygenation
-
-
-
-
oxidation
-
-
-
-
oxygenation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
cholesterol biosynthesis
-
-
Metabolic pathways
-
-
plant sterol biosynthesis
-
-
Steroid biosynthesis
-
-
zymosterol biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
sterol,NADPH:oxygen oxidoreductase (14-methyl cleaving)
This heme-thiolate (P-450) enzyme acts on a range of steroids with a 14alpha-methyl group, such as obtusifoliol and lanosterol. The enzyme catalyses two successive hydroxylations of the 14alpha-methyl group, followed by elimination as formate, leaving a 14(15) double bond.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14-demethylase
-
-
-
-
14alpha-demethylase
-
-
-
-
14alpha-methylsterol 14alpha-demethylase
-
-
-
-
14alpha-sterol demethylase
-
-
-
-
14DM
-
-
-
-
CYP51
-
-
-
-
CYPL1
-
-
-
-
cytochrome CYP51
-
-
-
-
cytochrome P 450 CYP51
-
-
-
-
cytochrome P-450 lanosterol 14alpha-demethylase
-
-
-
-
cytochrome P-450-dependent 14alpha-sterol demethylase
-
-
-
-
cytochrome P-450-dependent obtusifoliol 14alpha-demethylase
-
-
-
-
cytochrome P-450/14DM
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-
-
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cytochrome P-45014DM
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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
-
-
-
-
demethylase, methylsterol 14alpha-
-
-
-
-
eburicol 14 alpha-demethylase
-
-
-
-
eburicol 14alpha-demethylase
-
-
-
-
lanosterol 14 alpha-demethylase
-
-
-
-
lanosterol 14-demethylase
-
-
-
-
lanosterol 14alpha-demethylase
-
-
-
-
lanosterol 14alpha-methyldemethylase
-
-
-
-
lanosterol C-14 demethylase
-
-
-
-
lanosterol demethylase
-
-
-
-
LDM
-
-
-
-
methylsterol 14alpha-demethylase (P 450 CYP51)
-
-
-
-
Obtusifoliol 14-alpha demethylase
-
-
-
-
obtusifoliol 14-demethylase
-
-
-
-
obtusifoliol 14alpha-demethylase
-
-
-
-
obtusifoliol-metabolizing 14alpha-demethylase
-
-
-
-
obtusufoliol 14-demethylase
-
-
-
-
P 450 lanosterol C-14 demethylase
-
-
-
-
P-450 lanosterol demethylase
-
-
-
-
P-45014DM
-
-
-
-
P-45014DM-containing monooxygenase system
-
-
-
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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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-
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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-
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sterol 14alpha-demethylase (CYP51)
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sterol C14 demethylase
-
-
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-
CAS REGISTRY NUMBER
COMMENTARY
138674-19-8
deleted registry number
341989-59-1
deleted registry number
60063-87-8
-
90463-45-9
deleted registry number
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
voriconazole-resistant clinical isolates and voriconazole-susceptible parent strain X26728
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-
Manually annotated by BRENDA team
gene cyp51A, strain CM-237, and azole-insensitive clinical strains CNM-CM-1252 and CNM-CM-796
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-
Manually annotated by BRENDA team
isoenzymes CYP51A and CYP51B
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-
Manually annotated by BRENDA team
isozymes CYP51A and CYP51B, i.e. AF51A and AF51B
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-
Manually annotated by BRENDA team
isozymes CYP51A and CYP51B, i.e. AF51A and AF51B
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-
Manually annotated by BRENDA team
f. sp. hordei or f. sp. tritici, barley or wheat powdery mildew, gene CYP51
-
-
Manually annotated by BRENDA team
f.sp. hordei
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-
Manually annotated by BRENDA team
strain ATCC7661
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-
Manually annotated by BRENDA team
Candida albicans ATCC MYA.2876
-
Swissprot
Manually annotated by BRENDA team
Candida albicans ATCC7661
strain ATCC7661
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-
Manually annotated by BRENDA team
liver-type enzyme
SwissProt
Manually annotated by BRENDA team
testis-type enzyme
SwissProt
Manually annotated by BRENDA team
gene CYP51
-
-
Manually annotated by BRENDA team
Magnaporthe oryzae Guy11
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-
-
Manually annotated by BRENDA team
natural fusion protein of enzyme and ferredoxin
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-
Manually annotated by BRENDA team
fragment; field isolates from Georgia, which are demethylation inhibitor fungicides-sensitive or demethylation inhibitor fungicides-resistant, gene CYP51
UniProt
Manually annotated by BRENDA team
silencing of enzyme by potato virus X::Nt CYP51-1 transcripts, accumulation of obtusifoliol
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-
Manually annotated by BRENDA team
no activity in Escherichia coli
no endogenous sterol 14alpha-demethylase
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-
Manually annotated by BRENDA team
syn. Tapesia acuformis, cereal eyespot fungi, gene CYP51
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-
Manually annotated by BRENDA team
syn. Tapesia yallundae, cereal eyespot fungi, gene CYP51
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-
Manually annotated by BRENDA team
ram
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-
Manually annotated by BRENDA team
filamentous fungal plant pathogen
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-
Manually annotated by BRENDA team
filamentous fungi
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-
Manually annotated by BRENDA team
28 different species isolated from human lung
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-
Manually annotated by BRENDA team
male rat
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-
Manually annotated by BRENDA team
male sprague-dawley rats
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Manually annotated by BRENDA team
Sprague-Dawley rat
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-
Manually annotated by BRENDA team
strain BY4741
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-
Manually annotated by BRENDA team
strain FY1679
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-
Manually annotated by BRENDA team
Saccharomyces cerevisiae FY1679
strain FY1679
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-
Manually annotated by BRENDA team
Sinapis alba L.
L.
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-
Manually annotated by BRENDA team
gene CYP51
SwissProt
Manually annotated by BRENDA team
L., Moench
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Manually annotated by BRENDA team
expression in Escherichia coli with tetrahistidine tag
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Manually annotated by BRENDA team
i.e. Antrodia camphorata, gene CYP51
UniProt
Manually annotated by BRENDA team
Taiwanofungus camphoratus TFRIB 470
i.e. Antrodia camphorata, gene CYP51
UniProt
Manually annotated by BRENDA team
gene CYP51
SwissProt
Manually annotated by BRENDA team
strains Tulahuen, Peru, Y, EP, CL, SC-28, Colombiana, Bertoldo, YuYu and VL-10
SwissProt
Manually annotated by BRENDA team
LG11; maize
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-
Manually annotated by BRENDA team
maize
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Manually annotated by BRENDA team
Zea mays LG11
LG11
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Manually annotated by BRENDA team
gene CYP51
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-
Manually annotated by BRENDA team
septoria leaf blotch fungus
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
deletion mutants of CYP51A are morphologically indistinguishable from the isogenic wild type strain in vegetative culture, but are impaired in both conidiation and virulence. The deletion of isoform CYP51B does not result in any obvious phenotypic changes. The deletion mutant DELTAcyp51A is also highly sensitive to sterol demethylation inhibitor fungicides, while DELTAcyp51B mutants are unchanged in their sensitivity to these fungicides.
malfunction
Magnaporthe oryzae Guy11
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deletion mutants of CYP51A are morphologically indistinguishable from the isogenic wild type strain in vegetative culture, but are impaired in both conidiation and virulence. The deletion of isoform CYP51B does not result in any obvious phenotypic changes. The deletion mutant DELTAcyp51A is also highly sensitive to sterol demethylation inhibitor fungicides, while DELTAcyp51B mutants are unchanged in their sensitivity to these fungicides.
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metabolism
A8DBU6
sterol 14alpha-demethylase is one of the key enzymes for sterol biosynthesis in fungi
metabolism
-
CYP51A1 is involved in the cholesterol biosynthesis pathway
physiological function
-
cholesterol levels link-modulation system between cholesterol synthetic pathway through CYP51 and cholesterol transport pathway through low-density lipoprotein receptor in vivo
physiological function
Q68HC3
complementation of a conditional knock-down mutant of yeast CYP51. The CYP51 protein exhibits high affinity for azole antifungal compounds
physiological function
-
LDM is closely related to mouse embryo implantation and can be upregulated by oestrogen
physiological function
-
truncated CYP51 is successfully expressed in Escherichia coli, whereas the full-length CYP51 is not
physiological function
-
two distinct hydrogen-bond networks with the propensity to shuttle protons to the peroxo species in the CYP51 catalytic cycle. The first network is characterized by hydrogen-bonding between the His259, Thr260OH, and distal O2 atom. This hydrogen-bond network can catalyze the formation of compound 0 with a slightly higher barrier and comparable exothermicity to that of the Asp251-H2O-Thr252 shuttle of CYP101. Pursuit of a heterolytic O-O cleavage mechanism for the subsequent formation of compound I is unsuccessful, and exploration of a mechanism initiated by Op-Od bond homolysis realizes an endothermic reaction. Disruption of the His259H+-Thr260OH hydrogen bond followed by the influx of water into the active site and the evolution of an apparent second proton-transfer network, connecting the distal O2 atom to His259H+ and Glu173 via four water molecules. In this configuration of the active site, the peroxo intermediate has an unprecedented triradicaloid electronic structure with either two parallel or antiparallel electrons localized to the FeO2 unit, while a third resides on the protonated Glu173 side chain. This electronic structure is a direct result of the local hydrogen bond and electrostatic environment contributed by the enzyme interior, illustrating an important role for the protein environment to tune the electronic structure of the peroxo intermediate. Protonation of this residue gives rise to a peroxo intermediate with an electronic structure reflecting a potentially less reactive oxyferrous species in the catalytic core
physiological function
-
isoform CYP51A is required for conidiation, virulence and for mediating sensitivity to sterol demethylation inhibitors by Magnaporthe oryzae. Isoform CYP51A is expressed at low levels during vegetative growth, conidiation and appressorium formation
physiological function
Magnaporthe oryzae Guy11
-
isoform CYP51A is required for conidiation, virulence and for mediating sensitivity to sterol demethylation inhibitors by Magnaporthe oryzae. Isoform CYP51A is expressed at low levels during vegetative growth, conidiation and appressorium formation
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metabolism
Taiwanofungus camphoratus TFRIB 470
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sterol 14alpha-demethylase is one of the key enzymes for sterol biosynthesis in fungi
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additional information
-
an intrinsic azole fluconazole resistance is observed in Aspergillus fumigatus
additional information
-
an intrinsic azole fluconazole resistance is observed in Aspergillus fumigatus
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SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3b,4a,5a)-4,14-dimethylcholest-8-en-3-ol + O2 + NADPH
? + formate + NADP+ + H2O
show the reaction diagram
-
good substrate, 67% of activity compared to obtusifoliol
-
-
?
14alpha-methyl-24,28-dihydrofecosterol + O2 + NADPH
? + formate + NADP+ + H2O
show the reaction diagram
-
50% of activity compared to obtusifoliol
-
-
?
14alpha-methylzymosterol + O2 + NADPH + H+
?
show the reaction diagram
A2TEF2
-
-
-
?
2-phenylimidazole + NADPH + O2
?
show the reaction diagram
-
2-phenylimidazole binding causes thermally induced alterations in CYP51 active site structure and/or binding modes for the small ligand
-
-
?
24(28)-methylene-24,25-dihydrolanosterol + NADPH + O2
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
Q870D1
-
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
DHL
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
DHL
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
DHL
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
DHL
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
not the natural substrate
-
-
?
24,25-dihydrolanosterol + 3 O2 + 3 NADPH + 3 H+
(3beta,5alpha)-4,4-dimethylcholesta-8,14-dien-3-ol + formate + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
24,25-dihydrolanosterol + 3 O2 + 3 NADPH + 3 H+
(3beta,5alpha)-4,4-dimethylcholesta-8,14-dien-3-ol + formate + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
24,25-dihydrolanosterol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
24,25-dihydrolanosterol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
24,25-dihydrolanosterol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
24,25-dihydrolanosterol + NADPH + O2
?
show the reaction diagram
Q7Z1V1
-
-
-
?
24,25-dihydrolanosterol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
24,25-dihydrolanosterol + NADPH + O2
?
show the reaction diagram
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
24,25-dihydrolanosterol + O2 + NADPH + H+
24,25-dihydro-4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
24,25-dihydrolanosterol + O2 + NADPH + H+
?
show the reaction diagram
A2TEF2
i.e. anosta-8-en-3ebta-ol
-
-
?
24,28-dihydroobtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
good substrate, 75% of activity to obtusifoliol
-
-
?
24,28-dihydroobtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
good substrate, 75% of activity to obtusifoliol
-
-
?
24,28-dihydroobtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
very poor substrate, about 10% of obtusifoliol demethylation, activity disappears in the presence of same concentration of lanosterol, 24-methylene-24,25-dihydrolanosterol, obtusifoliol or 24,25-dihydrolanosterol, DHO
-
-
?
24,28-dihydroobtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
DHO
-
-
?
24,28-dihydroobtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
DHO
-
-
?
24,28-dihydroobtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8-en-3beta-ol
-
-
?
24,28-dihydroobtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8-en-3beta-ol
-
-
?
24,28-dihydroobtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14-dien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8-en-3beta-ol
-
-
?
24-methylene-24,25-dihydrolanosterol + O2 + NADPH
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
good substrate
-
-
?
24-methylene-24,25-dihydrolanosterol + O2 + NADPH
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
poorest substrate, catalyzes 14alpha-demethylation of 24-methylene-DHL, but activity is considerably lower than that for lanosterol and for 24,25-dihydrolanosterol, DHL, 4,4,14alpha-trimethylergosta-8,24(28)-dien-3beta-ol
-
-
?
24-methylene-24,25-dihydrolanosterol + O2 + NADPH
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
4,4,14alpha-trimethylergosta-8,24(28)-dien-3beta-ol
-
-
?
24-methylene-24,25-dihydrolanosterol + O2 + NADPH
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
activity for 24-methylene-DHL is considerably higher, 4fold, than that for 24,25-dihydrolanosterol, DHL
-
-
?
24-methylene-24,25-dihydrolanosterol + O2 + NADPH
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
24-methylenelanost-8-en-3beta-ol, 24-methylene-DHL
-
-
?
24-methylene-24,25-dihydrolanosterol + O2 + NADPH
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
24-methylenelanost-8-en-3beta-ol, 24-methylene-DHL
-
-
?
24-methylene-24,25-dihydrolanosterol + O2 + NADPH
4,4-dimethyl-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
about 60% activity to that of lanosterol
-
-
?
24-methylene-24,25-dihydrolanosterol + O2 + NADPH + H+
14alpha-demethyl-24-methylene-4alpha-methyl-5alpha-ergosta-8,14,24-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
24-methylenedihydrolanosterol + NADPH + O2
?
show the reaction diagram
Q7Z1V1
-
-
-
?
24-methylenedihydrolanosterol + NADPH + O2
?
show the reaction diagram
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
24-methylenedihydrolanosterol + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
preferred substrate
-
-
?
7-lanosten-3beta-ol + O2 + NADPH
4,4-dimethylcholesta-7,14-dien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
very low activity
-
-
?
7-lanostene-3beta,32-diol + O2 + NADPH
4,4-dimethylcholesta-7,14-dien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
very low activity
-
-
?
8-lanostene-3beta,32-diol + O2 + NADPH
4,4-dimethylcholesta-8,14-dien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
eburicol + 3 O2 + 3 NADPH + 3 H+
?
show the reaction diagram
-
isozymes CYP51A and CYP51B
-
-
?
eburicol + O2 + NADPH
? + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
eburicol + O2 + NADPH + H+
2-(3-hydroxy-4,4,10,13-tetramethyl-2,3,4,5,6,7,10,11,12,13,16,17-dodecahydro-1H-cyclopenta[a]phenanthren-17-yl)-6-methyl-5-methylene-heptanoic acid + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
eburicol + O2 + NADPH + H+
?
show the reaction diagram
-
-
-
-
?
eburicol + O2 + NADPH + H+
?
show the reaction diagram
A2TEF2
i.e. 24-methylenelanosta-8-en-3beta-ol
-
-
?
estriol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
estriol + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + 2 NADPH + 2 H+ + 2 O2
4,4-dimethylzymosterol + formate + 2 NADP+ + 2 H2O
show the reaction diagram
Q673E9
-
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
-
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
-
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
best substrate
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
best substrate
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
natural substrate
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
natural substrate
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
Q64654
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
Q64654
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
P-45014DM catalyzes all three oxygenation steps from lanosterol to dimethylcholestratrienol, ergosterol synthesis in yeast involves oxidative removal of the 14alpha-methyl group, C-32, of lanosterol
-
-
?
lanosterol + 3 O2 + 3 NADPH + 3 H+
?
show the reaction diagram
-
-
-
-
?
lanosterol + 3 O2 + 3 NADPH + 3 H+
?
show the reaction diagram
-
isozymes CYP51A and CYP51B
-
-
?
lanosterol + 3 O2 + 3 NADPH + 3 H+
4,4-dimethylcholesta-8,14,24-trienol + formate + NADP+ + H2O
show the reaction diagram
Taiwanofungus camphoratus, Taiwanofungus camphoratus TFRIB 470
A8DBU6
-
-
-
?
lanosterol + NADP+ + H2O
?
show the reaction diagram
-
-
production of follicular fluid-meiosis activating steroid by lanosterol demethylation
-
?
lanosterol + NADPH + H+ + 2 O2
4,4-dimethylcholesta-8,14,24-trienol + formate + NADP+ + 2 H2O
show the reaction diagram
-
deletion of the enzyme is lethal
-
-
?
lanosterol + NADPH + H+ + 2 O2
4,4-dimethylcholesta-8,14,24-trienol + formate + NADP+ + 2 H2O
show the reaction diagram
Saccharomyces cerevisiae FY1679
-
deletion of the enzyme is lethal
-
-
?
lanosterol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
lanosterol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
lanosterol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
lanosterol + NADPH + O2
?
show the reaction diagram
Q7Z1V1
-
-
-
?
lanosterol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
lanosterol + NADPH + O2
?
show the reaction diagram
Q3HTM1
-
-
-
?
lanosterol + NADPH + O2
?
show the reaction diagram
-
CYP51 responds to cholesterol feedback regulation, being upregulated in sterol limiting conditions and downregulated in cholesterol rich conditions, regulation involves the sterol regulatory elements SRE in the promoter of the gene which bind sterol regulatory element binding protein, SREBP, the CYP51 promoter also contains a cAMP regulatory element, CRE, binding cAMP regulatory proteins CREB/CREM, overview
-
-
?
lanosterol + NADPH + O2
?
show the reaction diagram
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + NADPH + O2
?
show the reaction diagram
-
the enzyme is regulated by cholesterol feedback regulation through sterol regulatory element binding proteins, i.e. SREBPs, regulation mechanisms of enzyme expression, overview
-
-
?
lanosterol + NADPH + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + NADP+ + H2O
show the reaction diagram
Q16850
artificial fused enzymes have comparable activity to the reconstituted system. Reduction of CYP51 both in the fused enzyme and the reconstituted system is biphasic and consisted of an initial fast phase followed by a slow phase
-
-
?
lanosterol + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
Q16850
-
-
-
?
lanosterol + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
Q7Z1V1
active site contains an isoleucine, lanosterol is the preferred substrate
-
-
?
lanosterol + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + O2 + NADPH
? + formate + NADP+ + H2O
show the reaction diagram
-
activity depends on presence of natural fusion protein ferredoxin
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
Q4PJW3
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-triene-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethylcholesta-8,14,24-trien-3-ol + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethylcholesta-8,14,24-trien-3-ol + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethylcholesta-8,14,24-trien-3-ol + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethylcholesta-8,14,24-trien-3-ol + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethylcholesta-8,14,24-trien-3-ol + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethylcholesta-8,14,24-trien-3-ol + NADP+ + H2O
show the reaction diagram
A2TEF2
i.e. lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethylcholesta-8,14,24-trien-3-ol + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethylcholesta-8,14,24-trien-3-ol + NADP+ + H2O
show the reaction diagram
Magnaporthe oryzae Guy11
-
-
-
-
?
norlanosterol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
norlanosterol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
norlanosterol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
norlanosterol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
norlanosterol + NADPH + O2
?
show the reaction diagram
-
low activity
-
-
?
norlanosterol + NADPH + O2
?
show the reaction diagram
Q7Z1V1
i.e. 4alpha,4alpha-dimethylcholesta-8,24-dien-3beta-ol
-
-
?
norlanosterol + NADPH + O2
?
show the reaction diagram
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
norlanosterol + O2 + NADPH + H+
?
show the reaction diagram
A2TEF2
i.e. 4alpha,14alpha-dimethylcholesta-8,24-dien-3beta-ol
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
Q673E9
-
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
low activity
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
low activity
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
preferred substrate
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
Q7Z1V1
preferred substrate
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
Q3HTM1
preferred substrate
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
Q673E9
the enzyme is involved in biosynthesis of sitosterol and brassinosteroids, pathways overview
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
best substrate
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
catalyzes 14alpha-demethylation of obtusifoliol
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
catalyzes 14alpha-demethylation of obtusifoliol
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
catalyzes 14alpha-demethylation of obtusifoliol
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
catalyzes 14alpha-demethylation of obtusifoliol
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
presence of the large phenylalanine side chain in the active site seems to lead to preferred processing of obtusifoliol
-
-
?
obtusifoliol + O2 + NADPH + H+
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
obtusifoliol + O2 + NADPH + H+
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
obtusifoliol + O2 + NADPH + H+
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
A2TEF2
i.e. 4alpha,14alpha-dimethyl-5'-ergosta-8,24(24')-dien-3beta-ol
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethylcholesta-8,14,24-trien-3-ol + NADP+ + H2O
show the reaction diagram
Candida albicans ATCC MYA.2876
P10613
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
4beta-methyl group, C31, does not affect the activity of yeast P-45014DM, although removal reduces affinity for enzyme in some extent
-
-
-
additional information
?
-
-
no activity with 31-norlanosterol, cycloeucalenol, 4alpha,14alpha-dimethyl-5alpha-ergost-9(11)-en-3beta-ol, 4alpha,14alpha-dimethyl-5alpha-ergost-7-en-3beta-ol, 8(9),24(25)-tetrahydro-31-norlanosterol, 24-methylenelanosterol, 24,28-dihydro-4beta-methyl-30-norobtusifoliol, 24,25-dihydrolanosterol, lanosterol, obtusifoliyl-3beta-methoxy, obtusifoliyl-3beta-acetoxy, obtusifoliyl-3beta-amino
-
-
-
additional information
?
-
-
can not catalyze demethylation of sterols having 4beta-methyl group, favorably interacts with sterols having saturated side chain
-
-
-
additional information
?
-
-
substrate binding spectra
-
-
-
additional information
?
-
-
biosynthetic enzyme with very narrow substrate specificity
-
-
-
additional information
?
-
-
biosynthetic enzyme with very narrow substrate specificity
-
-
-
additional information
?
-
-
8-double bond of lanosterol plays an important critical role in enzyme-substrate interaction of cytochrome P-45014DM
-
-
-
additional information
?
-
-
P-450OBT 14DM has probably a specific apolar binding site for the side chain. DELTA8-double bond is absolute required for substrate demethylation and the 3-hydroxy group plays a critical role in enzyme-substrate interaction
-
-
-
additional information
?
-
-
no activity with 6-lanostene-3beta,32-diol and lanostane-3beta,32-diol
-
-
-
additional information
?
-
-
no activity with lanosterol, campesterol, sitosterol, or stigmasterol
-
-
-
additional information
?
-
-
yeast enzyme poorly metabolizes sterols having saturated side chain, plant enzyme shows considerable activity for such sterols
-
-
-
additional information
?
-
-
enzyme is a multifunctional cytochrome P450, which as the same active site catalyze demethylation in three consecutive NADPH- and O2-dependent hydroxylation reactions, resulting in the elimination of the methyl group as formic acid and the introduction of a double bond at the DELTA14 position
-
-
-
additional information
?
-
-
enzyme recognizes 8-lanostene structure and favourably interacts with 8-lanostene derivatives, can act also with substrates having 7-lanostene structure, utilizes them with lower efficiency than 8-lanostene derivatives
-
-
-
additional information
?
-
-
enzyme with high degree of substrate and product specificity
-
-
-
additional information
?
-
-
cycloartenol: not or very poor substrate, 3-hydroxy group, the 8-lanostene conformation of sterol ring and the side-chain terminal, C25, C26, C27, are the essential structures of substrates for interacting with the yeast enzyme
-
-
-
additional information
?
-
-
substrate for 14alpha-demethylation reaction in plants is different from that in animals and fungi
-
-
-
additional information
?
-
-
plant sterol 14alpha-demethylase have high substrate specificity
-
-
-
additional information
?
-
-
plant sterol 14alpha-demethylase have high substrate specificity
-
-
-
additional information
?
-
-
narrow substrate selectivity
-
-
-
additional information
?
-
-
narrow substrate selectivity
-
-
-
additional information
?
-
-
narrow substrate selectivity
-
-
-
additional information
?
-
-
substrate recognition
-
-
-
additional information
?
-
-
reaction reqires molecular oxygen, does not occur anaerobically
-
-
-
additional information
?
-
-
housekeeping enzyme essential for viability of mammals, essential step in cholesterol biosynthesis
-
-
-
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
-
additional information
?
-
-
catalyzes an essential step in sterol biosynthesis as evidenced by the absence of a 14alpha-methyl group in all known functional sterols, removal of the 14alpha-methyl group is essential
-
-
-
additional information
?
-
-
key enzyme in plant sterol, phytosterol, biosynthesis
-
-
-
additional information
?
-
-
brain microsomes, existence of sterol biosynthetic pathway in brain, cholesterol is synthesized de novo in brain
-
-
-
additional information
?
-
-
removal of 14alpha-methyl group, C32, from 14alpha-methylated precursor sterols is an essential step of sterol biosynthesis in eukaryotes
-
-
-
additional information
?
-
-
enzyme of cholesterol biosynthesis
-
-
-
additional information
?
-
-
enzyme of cholesterol biosynthesis
-
-
-
additional information
?
-
Q64654
enzyme of cholesterol biosynthesis
-
-
-
additional information
?
-
-
enzyme of cholesterol biosynthesis
-
-
-
additional information
?
-
-
lanosterol 14-demethylation is situated at the root of sterol-biosynthetic branch of mevalonic acid pathway
-
-
-
additional information
?
-
Q64654
enzyme for regulation of cholesterol biosynthesis
-
-
-
additional information
?
-
-
there is a possibility that P45014DM participates not only in sterol biogenesis but also in production of biosignal substance regulating meiosis of mammalian oocytes
-
-
-
additional information
?
-
-
enzyme of ergosterol biosynthesis
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
14alpha-demethylation is a key step of sterol biosynthesis in eukaryotes
-
-
-
additional information
?
-
-
enzyme of plant sterol, phytosterol, biosynthesis
-
-
-
additional information
?
-
-
enzyme of plant sterol, phytosterol, biosynthesis
-
-
-
additional information
?
-
-
enzyme of plant sterol, phytosterol, biosynthesis
-
-
-
additional information
?
-
-
involved in fertilization
-
-
-
additional information
?
-
P9WPP9
analysis of active site by spectroscopic titration, resonance Raman spectroscopy and EPR
-
-
-
additional information
?
-
-
analysis of active site by stectroscopic titration, resonance Raman spectroscopy and EPR
-
-
-
additional information
?
-
-
no substrate: lanosterol
-
-
-
additional information
?
-
-
CYP51 participates in biosynthesis of cholesterol
-
-
-
additional information
?
-
-
CYP51 plays a key role in fertilization by producing intermediates that could serve as ligands for nuclear receptors
-
-
-
additional information
?
-
-
enzyme inhibition may result in endocrine disruption since follicular fluid-meiosis activating steroid, the direct product of lanosterol demethylation, is involved in the control of meiosis
-
-
-
additional information
?
-
-
sterol composition of different species isolated from human lung, two distinct sterol compositional phenotypes occur, one, the wild-type, is characterized by DELTA7 C28- and C24 24-alkylsterols with only low proportions of higher molecular mass components, the other type, a mutant with 14alpha-demethylase deficiency, is dominated by high C31 and C32 24-alkylsterols, especially pneumocysterol, NMR sterol analysis, overview
-
-
-
additional information
?
-
-
the organism can specifically regulate gene expression, e.g. for the sterol C14-demethylase, in response to derangements in its cellular functions
-
-
-
additional information
?
-
-
P420 formation process with protonation of Cys394 and structure by binding of CO to P450, overview
-
-
-
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 oxgen 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
-
-
-
additional information
?
-
-
residues Ile381 and Leu321 are involved in substrate recognition
-
-
-
additional information
?
-
Q7Z1V1
substrate specificity, the Trypanosoma cruzi enzyme prefers C4-dimethylsterols substrates, overview
-
-
-
additional information
?
-
-
the regio- and stereospecific 14alpha-demethylation CYP51 reaction proceeds in three steps, each requiring one molecule of oxgen 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
-
-
-
additional information
?
-
-
CYP51 is a major checkpoint in membrane sterol biosynthesis, is a key target for fungal antibiotic therapy
-
-
-
additional information
?
-
A1XG20
CYP51 is one of the key enzymes of sterol biosynthesis in biological kingdoms and is a prime target of antifungal drugs
-
-
-
additional information
?
-
-
the enzyme catalyzes a step in the cholesterol biosynthesis via the mevalonate pathway, overview
-
-
-
additional information
?
-
A7LM25
the enzyme is a demethylation inhibitor fungicide resistance determinant in Monilinia fructicola field isolates
-
-
-
additional information
?
-
-
the enzyme is involved in follicle-stimulating hormone-induced mouse oocyte maturation and follicle-stimulating hormone-induced oocyte meiotic resumption, regulation, overview. The enzyme is involved in CREB phosphorylation
-
-
-
additional information
?
-
-
structure-activity relationship study of enzyme-ligand binding, pyridine binds within the heme binding pocket in an analogy with azoles, overview
-
-
-
additional information
?
-
-
azole binding properties of purified CYP51A and CYP51B, overview
-
-
-
additional information
?
-
-
CYP51b1 shows activity with coumarin derivatives as substrates, e.g. with 7-ethoxycoumarin, 4-methyl-7-hydroxycoumarin, 4-methyl-7-aminocoumarin, and 7-aminocoumarin-4-acetic acid, that are competitive to lanosterol. In the model system for assay of CYP51b1 activity, a flavin domain of the cytochrome P450BM-3, BMR, from Bacillus megaterium may serve as the electron donor, overview
-
-
-
additional information
?
-
Zea mays LG11
-
substrate specificity, no activity with 31-norlanosterol, cycloeucalenol, 4alpha,14alpha-dimethyl-5alpha-ergost-9(11)-en-3beta-ol, 4alpha,14alpha-dimethyl-5alpha-ergost-7-en-3beta-ol, 8(9),24(25)-tetrahydro-31-norlanosterol, 24-methylenelanosterol, 24,28-dihydro-4beta-methyl-30-norobtusifoliol, 24,25-dihydrolanosterol, lanosterol, obtusifoliyl-3beta-methoxy, obtusifoliyl-3beta-acetoxy, obtusifoliyl-3beta-amino, biosynthetic enzyme with very narrow substrate specificity, P-450OBT 14DM has probably a specific apolar binding site for the side chain. DELTA8-double bond is absolute required for substrate demethylation and the 3-hydroxy group plays a critical role in enzyme-substrate interaction, enzyme with high degree of substrate and product specificity
-
-
-
additional information
?
-
-
azole binding properties of purified CYP51A and CYP51B, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
14alpha-methylzymosterol + O2 + NADPH + H+
?
show the reaction diagram
A2TEF2
-
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
8-lanosta-3beta-ol
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
DHL
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
DHL
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
8-lanosten-3beta-ol
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol
-
-
?
24,25-dihydrolanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
not the natural substrate
-
-
?
24,25-dihydrolanosterol + 3 O2 + 3 NADPH + 3 H+
(3beta,5alpha)-4,4-dimethylcholesta-8,14-dien-3-ol + formate + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
24,25-dihydrolanosterol + 3 O2 + 3 NADPH + 3 H+
(3beta,5alpha)-4,4-dimethylcholesta-8,14-dien-3-ol + formate + 3 NADP+ + 4 H2O
show the reaction diagram
-
-
-
-
?
24,25-dihydrolanosterol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
24,25-dihydrolanosterol + NADPH + O2
?
show the reaction diagram
Q7Z1V1
-
-
-
?
24,25-dihydrolanosterol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
24,25-dihydrolanosterol + NADPH + O2
?
show the reaction diagram
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
24,25-dihydrolanosterol + O2 + NADPH + H+
24,25-dihydro-4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
24-methylenedihydrolanosterol + NADPH + O2
?
show the reaction diagram
Q7Z1V1
-
-
-
?
24-methylenedihydrolanosterol + NADPH + O2
?
show the reaction diagram
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
eburicol + O2 + NADPH
? + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
eburicol + O2 + NADPH + H+
?
show the reaction diagram
-
-
-
-
?
lanosterol + 2 NADPH + 2 H+ + 2 O2
4,4-dimethylzymosterol + formate + 2 NADP+ + 2 H2O
show the reaction diagram
Q673E9
-
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
natural substrate
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
natural substrate
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
Q64654
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
Q64654
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
4,4,14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
-
-
?
lanosterol + 2 O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + 2 H2O
show the reaction diagram
-
P-45014DM catalyzes all three oxygenation steps from lanosterol to dimethylcholestratrienol, ergosterol synthesis in yeast involves oxidative removal of the 14alpha-methyl group, C-32, of lanosterol
-
-
?
lanosterol + 3 O2 + 3 NADPH + 3 H+
?
show the reaction diagram
-
-
-
-
?
lanosterol + NADP+ + H2O
?
show the reaction diagram
-
-
production of follicular fluid-meiosis activating steroid by lanosterol demethylation
-
?
lanosterol + NADPH + H+ + 2 O2
4,4-dimethylcholesta-8,14,24-trienol + formate + NADP+ + 2 H2O
show the reaction diagram
Saccharomyces cerevisiae, Saccharomyces cerevisiae FY1679
-
deletion of the enzyme is lethal
-
-
?
lanosterol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
lanosterol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
lanosterol + NADPH + O2
?
show the reaction diagram
Q7Z1V1
-
-
-
?
lanosterol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
lanosterol + NADPH + O2
?
show the reaction diagram
Q3HTM1
-
-
-
?
lanosterol + NADPH + O2
?
show the reaction diagram
-
CYP51 responds to cholesterol feedback regulation, being upregulated in sterol limiting conditions and downregulated in cholesterol rich conditions, regulation involves the sterol regulatory elements SRE in the promoter of the gene which bind sterol regulatory element binding protein, SREBP, the CYP51 promoter also contains a cAMP regulatory element, CRE, binding cAMP regulatory proteins CREB/CREM, overview
-
-
?
lanosterol + NADPH + O2
?
show the reaction diagram
-
the enzyme is involved in ergosterol and cholesterol biosynthesis
-
-
?
lanosterol + NADPH + O2
?
show the reaction diagram
-
the enzyme is regulated by cholesterol feedback regulation through sterol regulatory element binding proteins, i.e. SREBPs, regulation mechanisms of enzyme expression, overview
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
Q4PJW3
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-triene-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethylcholesta-8,14,24-trien-3-ol + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethylcholesta-8,14,24-trien-3-ol + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethylcholesta-8,14,24-trien-3-ol + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethylcholesta-8,14,24-trien-3-ol + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethylcholesta-8,14,24-trien-3-ol + NADP+ + H2O
show the reaction diagram
A2TEF2
i.e. lanosta-8,24-dien-3beta-ol
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethylcholesta-8,14,24-trien-3-ol + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
norlanosterol + NADPH + O2
?
show the reaction diagram
-
-
-
-
?
norlanosterol + NADPH + O2
?
show the reaction diagram
Q7Z1V1
i.e. 4alpha,4alpha-dimethylcholesta-8,24-dien-3beta-ol
-
-
?
norlanosterol + NADPH + O2
?
show the reaction diagram
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
norlanosterol + O2 + NADPH + H+
?
show the reaction diagram
A2TEF2
i.e. 4alpha,14alpha-dimethylcholesta-8,24-dien-3beta-ol
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
low activity
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
Q7Z1V1
preferred substrate
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
Q3HTM1
preferred substrate
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
Q673E9
the enzyme is involved in biosynthesis of sitosterol and brassinosteroids, pathways overview
-
-
?
obtusifoliol + NADPH + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
4alpha,14alpha-dimethyl-24-methylene-5alpha-cholesta-8-en-3beta-ol
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol
-
-
?
obtusifoliol + O2 + NADPH
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
4alpha,14alpha-dimethyl-5alpha-ergosta-8,24(28)-dien-3beta-ol
-
-
?
obtusifoliol + O2 + NADPH + H+
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
obtusifoliol + O2 + NADPH + H+
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
obtusifoliol + O2 + NADPH + H+
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
A2TEF2
i.e. 4alpha,14alpha-dimethyl-5'-ergosta-8,24(24')-dien-3beta-ol
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethylcholesta-8,14,24-trien-3-ol + NADP+ + H2O
show the reaction diagram
Magnaporthe oryzae Guy11
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
biosynthetic enzyme with very narrow substrate specificity
-
-
-
additional information
?
-
-
enzyme is a multifunctional cytochrome P450, which as the same active site catalyze demethylation in three consecutive NADPH- and O2-dependent hydroxylation reactions, resulting in the elimination of the methyl group as formic acid and the introduction of a double bond at the DELTA14 position
-
-
-
additional information
?
-
-
housekeeping enzyme essential for viability of mammals, essential step in cholesterol biosynthesis
-
-
-
additional information
?
-
-
enzyme of sterol biosynthesis, sterol 14-demethylation occurs in all organism exhibiting de novo sterol biosynthesis
-
-
-
additional information
?
-
-
catalyzes an essential step in sterol biosynthesis as evidenced by the absence of a 14alpha-methyl group in all known functional sterols, removal of the 14alpha-methyl group is essential
-
-
-
additional information
?
-
-
key enzyme in plant sterol, phytosterol, biosynthesis
-
-
-
additional information
?
-
-
brain microsomes, existence of sterol biosynthetic pathway in brain, cholesterol is synthesized de novo in brain
-
-
-
additional information
?
-
-
removal of 14alpha-methyl group, C32, from 14alpha-methylated precursor sterols is an essential step of sterol biosynthesis in eukaryotes
-
-
-
additional information
?
-
-
enzyme of cholesterol biosynthesis
-
-
-
additional information
?
-
-
enzyme of cholesterol biosynthesis
-
-
-
additional information
?
-
Q64654
enzyme of cholesterol biosynthesis
-
-
-
additional information
?
-
-
enzyme of cholesterol biosynthesis
-
-
-
additional information
?
-
-
lanosterol 14-demethylation is situated at the root of sterol-biosynthetic branch of mevalonic acid pathway
-
-
-
additional information
?
-
Q64654
enzyme for regulation of cholesterol biosynthesis
-
-
-
additional information
?
-
-
there is a possibility that P45014DM participates not only in sterol biogenesis but also in production of biosignal substance regulating meiosis of mammalian oocytes
-
-
-
additional information
?
-
-
enzyme of ergosterol biosynthesis
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
enzyme of sterol biosynthetic pathway
-
-
-
additional information
?
-
-
14alpha-demethylation is a key step of sterol biosynthesis in eukaryotes
-
-
-
additional information
?
-
-
enzyme of plant sterol, phytosterol, biosynthesis
-
-
-
additional information
?
-
-
enzyme of plant sterol, phytosterol, biosynthesis
-
-
-
additional information
?
-
-
enzyme of plant sterol, phytosterol, biosynthesis
-
-
-
additional information
?
-
-
involved in fertilization
-
-
-
additional information
?
-
-
CYP51 participates in biosynthesis of cholesterol
-
-
-
additional information
?
-
-
CYP51 plays a key role in fertilization by producing intermediates that could serve as ligands for nuclear receptors
-
-
-
additional information
?
-
-
enzyme inhibition may result in endocrine disruption since follicular fluid-meiosis activating steroid, the direct product of lanosterol demethylation, is involved in the control of meiosis
-
-
-
additional information
?
-
-
sterol composition of different species isolated from human lung, two distinct sterol compositional phenotypes occur, one, the wild-type, is characterized by DELTA7 C28- and C24 24-alkylsterols with only low proportions of higher molecular mass components, the other type, a mutant with 14alpha-demethylase deficiency, is dominated by high C31 and C32 24-alkylsterols, especially pneumocysterol, NMR sterol analysis, overview
-
-
-
additional information
?
-
-
the organism can specifically regulate gene expression, e.g. for the sterol C14-demethylase, in response to derangements in its cellular functions
-
-
-
additional information
?
-
-
CYP51 is a major checkpoint in membrane sterol biosynthesis, is a key target for fungal antibiotic therapy
-
-
-
additional information
?
-
A1XG20
CYP51 is one of the key enzymes of sterol biosynthesis in biological kingdoms and is a prime target of antifungal drugs
-
-
-
additional information
?
-
-
the enzyme catalyzes a step in the cholesterol biosynthesis via the mevalonate pathway, overview
-
-
-
additional information
?
-
A7LM25
the enzyme is a demethylation inhibitor fungicide resistance determinant in Monilinia fructicola field isolates
-
-
-
additional information
?
-
-
the enzyme is involved in follicle-stimulating hormone-induced mouse oocyte maturation and follicle-stimulating hormone-induced oocyte meiotic resumption, regulation, overview. The enzyme is involved in CREB phosphorylation
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome
-
a cytochrome P450 enzyme
-
cytochrome P450
-
-
-
cytochrome P450
-
-
-
cytochrome P450
-
-
-
cytochrome P450
-
-
-
cytochrome P450
-
-
-
cytochrome P450
-
-
-
cytochrome P450
Q4PJW3
a cytochrome P450 enzyme
-
cytochrome P450
-
a cytochrome P450 enzyme
-
cytochrome P450
A1XG20
a cytochrome P450 enzyme
-
cytochrome P450
-
a cytochrome P450 enzyme
-
cytochrome P450
-
a cytochrome P450 enzyme
-
cytochrome P450
-
-
-
cytochrome P450
-
-
-
cytochrome P450
Q68HC3
-
-
cytochrome P450
-
-
-
Ferredoxin
-
enzyme-bound, the enzyme is a fusion protein with a 3Fe-4S ferredoxin
-
Ferredoxin
-
Fdx binds a [3Fe-4S] iron-sulfur cluster, encoded by gene RV0763c adejacent to the gene encoding the enzyme
-
Ferredoxin
-
a ferredoxin-bound enzyme
-
heme
-
heme-thiolate enzyme; hemoprotein
heme
-
heme-thiolate enzyme
heme
-
heme-thiolate enzyme
heme
-
heme-thiolate enzyme
heme
-
heme-thiolate enzyme
heme
-
heme-thiolate enzyme
heme
-
two distinct azole binding conformations within the heme prosthetic group of CYP51A
NADPH
-
required
NADPH
-
required
NADPH
-
totally dependent upon NADPH, NADH extremely poor reductant
NADPH
Q673E9
-
NADPH
Q4PJW3
-
NADPH
A1XG20
-
NADPH
-
-
NADPH
Q16850
electron transfer from P450 reductase to CYP51 in the fusion proteins is significantly faster than that in the reconstituted system
NADPH
A2TEF2
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
-
a cytochrome P450 enzyme, non-heme iron
Fe2+
Q4PJW3
a cytochrome P450 enzyme
Fe2+
-
a cytochrome P450 enzyme
Fe2+
-
a cytochrome P450 enzyme
Fe2+
A1XG20
a cytochrome P450 enzyme, heme iron
Fe2+
-
a cytochrome P450 enzyme
Fe2+
-
a cytochrome P450 enzyme
Fe2+
Q7Z1V1
heme-iron in the active site
Fe2+
-
heme protein
Iron
-
3.9 molecules per enzyme molecule, 3Fe-4S center of ferredoxin component, one iron molecule bound to heme
Iron
-
cysteinate- and aqua-ligated heme iron, P450 formation involves residue Cys394, Cys 394 thiol is deprotonated to thiolate in the ferric form, and ferredoxin-bound [3Fe-4S] iron-sulfur cluster
Iron
-
a heme iron, DELTA7–8 double bond location is more favorable for coordination of the amino nitrogen to the heme iron
Mg2+
-
-
Mg2+
Q4PJW3
-
additional information
-
divalent metal ion is required for the catalytic reaction
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,4S)-ketoconazole
Q68HC3
-
(R)-3-(1H-1,2,4-triazol-1-yl)butyl 2-chlorobenzoate
-
exhibits stronger binding activities than triadimefon but lower binding activities than diniconazole
(R)-3-(1H-1,2,4-triazol-1-yl)butyl 3-chlorobenzoate
-
affinity with purified CYP51 is very low, exhibits lower binding activities than triadimefon and diniconazole
(R)-3-(1H-1,2,4-triazol-1-yl)butyl 4-chlorobenzoate
-
exhibits stronger binding activities than triadimefon but lower binding activities than diniconazole
(R)-3-(1H-1,2,4-triazol-1-yl)butyl 4-methylbenzoate
-
affinity with purified CYP51 is very tight, shows the best binding activities, exhibits stronger binding activities than triadimefon but lower binding activities than diniconazole; no binding affinity with purified CYP51
(R)-3-(1H-1,2,4-triazol-1-yl)butyl benzoate
-
exhibits lower binding activities than triadimefon and diniconazole
(R)-4'-chloro-N-(1-(2,4-dichlorophenyl)-2-(1H-imidazol-1-yl)ethyl)biphenyl-4-carboxamide
-
VNF, complexes CYP51, binding structure, overview
(R,S)-3-(1H-1,2,4-triazol-1-yl)butyl 2,4-dichlorobenzoate
-
exhibits binding activities than triadimefon but lower binding activities than diniconazole
(R,S)-3-(1H-1,2,4-triazol-1-yl)butyl 2-chlorobenzoate
-
exhibits lower binding activities than triadimefon and diniconazole
(R,S)-3-(1H-1,2,4-triazol-1-yl)butyl 3-chlorobenzoate
-
exhibits stronger binding activities than triadimefon but lower binding activities than diniconazole
(R,S)-3-(1H-1,2,4-triazol-1-yl)butyl 4-chlorobenzoate
-
exhibits lower binding activities than triadimefon and diniconazole
(R,S)-3-(1H-1,2,4-triazol-1-yl)butyl 4-methylbenzoate
-
affinity with purified CYP51 is very low, exhibits lower binding activities than triadimefon and diniconazole
(R,S)-3-(1H-1,2,4-triazol-1-yl)butyl benzoate
-
exhibits lower binding activities than triadimefon and diniconazole
(S)-3-(1H-1,2,4-triazol-1-yl)butyl 2,4-dichlorobenzoate
-
affinity with purified CYP51 is very tight, exhibits stronger binding activities than triadimefon but lower binding activities than diniconazole
(S)-3-(1H-1,2,4-triazol-1-yl)butyl 2-chlorobenzoate
-
exhibits stronger binding activities than triadimefon but lower binding activities than diniconazole
(S)-3-(1H-1,2,4-triazol-1-yl)butyl 3-chlorobenzoate
-
affinity with purified CYP51 is very tight, exhibits stronger binding activities than triadimefon but lower binding activities than diniconazole
(S)-3-(1H-1,2,4-triazol-1-yl)butyl 4-chlorobenzoate
-
exhibits binding activities than triadimefon but lower binding activities than diniconazole
(S)-3-(1H-1,2,4-triazol-1-yl)butyl benzoate
-
exhibits lower binding activities than triadimefon and diniconazole
(Z)-2,3-dihydro-3-(1H-imidazol-1-yl)-2-(1-butyl)-4H-1-benzopyran-4-one oxime
-
-
(Z)-trans-2,3-dihydro-3-(1H-imidazol-1-yl)-2-(1-pentyl)-4H-1-benzopyran-4-one oxime
-
-
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-amino-phenyl)-piperazin-1-yl]-propan-2-ol
-
-
1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[4-(2-fluoro-4-nitrophenyl)-piperazin-1-yl]-propan-2-ol
-
-
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2,4-dichlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-bromobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-methylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-bromobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-chlorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-ethylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-fluorobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-methylbenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-nitrobenzyl)-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-benzyl-amino]-2-propanol
-
exhibits higher activity than fluconazole
1-(phenethyl(propyl)amino)-3-(pyridin-3-yloxy)propan-2-ol
-
-
1-phenylimidazole
-
heme iron-coordinating inhibitor
11-ketoestrone
-
type I binding mechanism
14alpha-amino-lanosterol
-
-
14alpha-aminomethyl-lanosterol derivatives
-
competitive
-
15-hydroxy-lanosterol
-
-
15-keto-lanosterol
-
-
2,4-dichloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2,7-dihydroxy-9-fluorenone
-
type I binding mechanism
2-(2-(naphthalen-2-yl)ethyl](propyl)amino]-1-(pyridin-3-yl)ethanol dihydrobromide
-
-
2-(2-chlorophenethyl(propyl)amino)-1-(pyridin-4-yl)ethanol dihydrobromide
-
-
2-(3,4-dichlorophenethyl(methyl)amino)-1-(pyridin-3-yl)ethanol dihydrobromide
-
-
-
2-(3,4-dichlorophenethyl(methyl)amino)-1-(pyridin-4-yl)ethanol dihydrobromide
-
-
2-(3,4-dichlorophenethyl(propyl)amino)-1-(4-methylpyridin-2-yl)ethanol dihydrobromide
-
-
2-(3,4-dichlorophenethyl(propyl)amino)-1-(pyridin-3-yl)ethanol dihydrobromide
-
-
2-(3,4-dichlorophenethyl(propyl)amino)-1-phenylethanol
-
-
2-(3,4-difluorophenethyl(propyl)amino)-1-(pyridin-3-yl)ethanol dihydrobromide
-
-
2-(3,4-dimethoxyphenethyl(propyl)amino)-1-(pyridin-3-yl)ethanol dihydrobromide
-
-
2-(4-chlorophenethyl(propyl)amino)-1-(pyridin-4-yl)ethanol dihydrobromide
-
-
2-(4-nitrophenethyl(propyl)amino)-1-(pyridin-3-yl)ethanol dihydrobromide
-
-
2-(benzo[d]-2,1,3-thiadiazole-4-sulfonyl)-2-amino-2-phenyl-N-(pyridinyl-4)-acetamide
-
binding structure, overview
2-(phenethyl(propyl)amino)-1-(pyridin-3-yl) ethanol dihydrobromide
-
-
2-(propyl(2-(trifluoromethyl)phenethyl)amino)-1-(pyridin-3-yl)ethanol dihydrobromide
-
-
2-(propyl(4-(trifluoromethyl)phenethyl)amino)-1-(pyridin-3-yl)ethanol dihydrobromide
-
-
-
2-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
2-phenyl-N-pyridin-4-ylbutanamide
-
-
2-phenylimidazole
-
Kd-value 9.1 mM, comparison of affinity and binding to human and Mycobacterium tuberculosis enzyme
2-phenylimidazole
-
Kd-value 2.1 mM, comparison of affinity and binding to human and Mycobacterium tuberculosis enzyme
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-(1-pyridin-4-ylethyl)acetamide
-
-
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
-
-
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-(pyridin-2-ylmethyl)acetamide
-
-
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-(pyridin-4-ylmethyl)acetamide
-
-
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-pyridin-2-ylacetamide
-
-
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-pyridin-3-ylacetamide
-
-
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-pyrimidin-2-ylacetamide
-
-
2-[1-[(4-chlorophenyl)carbonyl]-5-methoxy-2-methyl-1H-indol-3-yl]-N-[(6-chloropyridin-3-yl)methyl]acetamide
-
-
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
-
-
2-{propyl[2-(pyridin-3-yl)ethyl]amino}-1-(pyridin-3-yl)ethanol
-
-
24,25-dihydrolanosterol
-
8.3% inhibition of 24-methylene-24,25-dihydrolanosterol demethylation, no inhibition of lanosterol demethylation
24,25-dihydrolanosterol
-
16.4% inhibition of obtusifoliol 14alpha-demethylation
24-methylene-24,25-dihydrolanosterol
-
21.6% inhibition of lanosterol demethylation, 55.3% inhibition of 24,25-dihydrolanosterol demethylation
24-methylene-24,25-dihydrolanosterol
-
47.4% inhibition of obtusifoliol 14alpha-demethylation
26-oxo-lanosterol
-
-
3-(1H-1,2,4-triazol-1-yl)butyl 4-fluorobenzoate
-
-
3-(1H-1,2,4-triazol-1-yl)butyl 4-methoxybenzoate
-
-
3-(2-furyl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole
-
most potent inhibitor
3-benzyl-1-pyridin-4-ylpyrrolidine-2,5-dione
-
-
3-bromo-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
3-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
3-methyl-4-nitro-N-pyridin-4-ylbenzamide
-
-
3-nitrophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
3-nitrophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate
-
-
3-oxo-N-pyridin-4-yl-3H-benzo[f]chromene-2-carboxamide
-
-
3-thien-2-yl-5,6-dihydroimidazo[2,1-b][1,3]thiazole
-
-
4,4'-dihydroxybenzophenone
-
binds at the active site via a type I mechanism targeting the flexible region, binding structure and kinetics, overview
4-(2-(2-hydroxy-2-(pyridin-3-yl)ethyl)(propyl)amino)ethylbenzene-1,2-diol dihydrobromide
-
-
-
4-(propoxycarbonyl)-phenyl-[4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)propyl]amino)methyl)]benzoate
-
exhibits higher activity than fluconazole
4-(propoxycarbonyl)-phenyl-[4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)propyl]amino)methyl)]benzoate
-
-
4-butyl-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-chloro-N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-chlorophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits activity than fluconazole
4-nitrophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
4-nitrophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits activity than fluconazole
4-nitrophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
4-phenylimidazole
-
Kd-value 0.19 mM, comparison of affinity and binding to human and Mycobacterium tuberculosis enzyme
4-phenylimidazole
-
Kd-value 0.29 mM, comparison of affinity and binding to human and Mycobacterium tuberculosis enzyme
4-phenylimidazole
-
heme iron-coordinating inhibitor
4-tert-butyl-N-(4-[4-[2-(2,4-difluorophenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-benzamide
-
-
4-[5-(2,4-difluoro-phenyl)-5-imidazol-1-ylmethyl-tetrahydro-furan-3-yl]-1-isopropyl-butylamine
-
0.0001 mM, wild-type, 10% residual activity, mutant F145L, 35% residual activity, mutant Y132H, 60% residual activity
4-[5-(2,4-difluoro-phenyl)-5-[1,2,4]triazol-1-ylmethyl-tetrahydro-furan-3-yl]-1-isopropyl-butylamine
-
0.0001 mM, wild-type, 25% residual activity, mutant F145L, 75% residual activity, mutant Y132H, 75% residual activity
6-[5-(2,4-difluoro-phenyl)-5-imidazol-1-ylmethyl-tetrahydro-furan-3-yl]-2-methyl-hexan-3-one
-
0.0001 mM, wild-type, no residual activity, mutant F145L, 5% residual activity, mutant Y132H, 25% residual activity
6-[5-(2,4-difluoro-phenyl)-5-[1,2,4]triazol-1-ylmethyl-tetrahydro-furan-3-yl]-2-methyl-hexan-3-one
-
0.0001 mM, wild-type, no residual activity, mutant F145L, 15% residual activity, mutant Y132H, 55% residual activity
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
Q7Z1V1
-
7-oxo-lanosterol
-
-
albaconazole
Q870D1
lower interaction energies with CYP51 than those of voriconazole
alpha-ethyl-N-4-pyridinyl-benzeneacetamide
-
binds to the non-heme iron, binding structure involving residues H259 and Y76, overview
Amphotericin B
-
-
Amphotericin B
-
-
anti-P-45014DM antibodies
-
complete inhibition
-
azalanstat
Q64654
specific inhibitor, IC50 less than 0.000002 mM
azole
-
the organism shows reduced azole-sensitivity
azole antifungal agents
-
specific inhibitors
-
azole antifungal agents
-
specific inhibitors
-
azoxystrobin
-
-
benznidazole
Q7Z1V1
-
bifonazole
-
IC50: 300 nM
bifonazole
-
IC50: 0.0008 mM
bitertanol
-
IC50: 59 nM
bitertanol
-
IC50: 0.0013 mM
butyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
clomiphene
-
interacts with heme, is less potent than azoles
clotrimazole
-
IC50: 91 nM
clotrimazole
-
IC50: 0.0009 mM
clotrimazole
Q68HC3
-
CO
-
high partial pressure of CO, ratio CO:O2 of 95:5 causes 48% inhibition
CO
-
ratio CO:O2 of 90:10, 51.1% inhibition, ratio CO:O2 of 95:5, 100% inhibition
cyproconazole
-
IC50: 100 nM
cyproconazole
-
IC50: 0.0228 mM
D0870
Q7Z1V1
-
difenoconazole
-
an azole inhibitor
diniconazole
A1XG20
homology modeling and docking model
diniconazole
-
-
diniconazole
-
is the most sensitive fungicide for CYP51, has a stronger affinity for CYP51 than the other fungicides
econazole
Q7Z1V1
-
econazole
-
-
epoxiconazole
-
IC50: 220 nM
epoxiconazole
-
IC50: 0.0020 mM
epoxiconazole
-
-
estriol
-
a substrate analogue
ethyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
ethyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
-
ethyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits activity than fluconazole
ethyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
fadrozole
-
IC50: 0.0322 mM, above
fadrozole
-
IC50: 0.10 mM, above
fluconazole
-
Kd-value 0.12 mM, comparison of affinity and binding to human and Mycobacterium tuberculosis enzyme
fluconazole
-
Kd-value 0.02 mM, comparison of affinity and binding to human and Mycobacterium tuberculosis enzyme
fluconazole
-
-
fluconazole
-
and analogues
fluconazole
-
IC50: 51 nM, above
fluconazole
-
IC50: 0.030 mM, above
fluconazole
-
a clinical drug
fluconazole
Q7Z1V1
-
fluconazole
-
-
fluconazole
Q870D1
is bound to the active site of CYP51 through the formation of a coordination bond with the iron of the heme group (the P1 subsite). The difluorophenyl group of fluconazole points toward substrate access channel 1 (the BC loop) and forms a hydrophobic interaction with Met153 and the alkyl group of Lys157 (the P3 subsite). Another triazolyl ring of fluconazole attached to C-3 has a preferable orientation toward substrate access channel 2 (the FG loop) and forms indirect nonbonding interactions with the surrounding residues, lined with Leu134, Phe240, Met316, Ile386, and Ile529 (the P4 subsite). The hydroxyl group attached to C-2 is important for antifungal activity, but no interaction between this hydroxyl group and the active site of CYP51
fluconazole
-
binds to the active site of CYP51 via coordination of the N atom of the triazole nucleus with iron of the heme group
fluconazole
Q68HC3
-
fluconazole
-
complexes CYP51, binding structure, overview
fluconazole
A2TEF2
the inhibitor not only replaces the substrate in the enzyme active site but most likely displaces the CO from the iron coordination sphere
flusilazole
-
IC50: 85 nM
flusilazole
-
IC50: 0.0034 mM
fungicides
-
-
-
glafenine
-
interacts with heme, shows no potency which may arise from its hydrophilic nature which lower its up-take and capacity to reach the target enzyme
hexaconazole
-
IC50: 66 nM
hexaconazole
-
IC50: 0.0156 mM
imazalil
-
IC50: 82 nM
imazalil
-
IC50: 0.0361 mM
isobutyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
isopropyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
itraconazole
-
IC50: 39 nM
itraconazole
-
IC50: 0.030 mM
itraconazole
Q7Z1V1
-
itraconazole
-
-
itraconazole
-
-
itraconazole
Q870D1
lowest interaction energies with CYP51
itraconazole
-
-
itraconazole
Q68HC3
-
itraconazole
A8DBU6
a fungicide that targets CYP51 and as an inhibitor causes the accumulation of lanosterol and reduced ergosterol biosynthesis in fungi, also induces AcCYP51 expression after 24 h of treatment
ketoconazole
-
potent inhibitor, 0.015 mM: complete inhibition
ketoconazole
-
Kd-value 0.008 mM, comparison of affinity and binding to human and Mycobacterium tuberculosis enzyme
ketoconazole
-
Kd-value 0.019 mM, comparison of affinity and binding to human and Mycobacterium tuberculosis enzyme
ketoconazole
-
IC50: 64 nM
ketoconazole
-
IC50: 0.0004 mM
ketoconazole
Q4PJW3
-
ketoconazole
Q7Z1V1
-
ketoconazole
-
residues lining the ketoconazole pocket include Ala397 and Ala398, Arg389 and Arg393, Asp377, Glu308, Gly390, Ile401, Leu311 and Leu315, Lys312, Phe387, Pro386, Trp382 and Trp384
ketoconazole
-
-
KG-501
-
the enzyme can be rescued by progesterone
lanosterol
-
63% inhibition of 24-methylene-24,25-dihydrolanosterol demethylation, 74.9% inhibition of 24,25-dihydrolanosterol demethylation
lanosterol
-
53.1% inhibition of obtusifoliol 14alpha-demethylation
letrozole
-
IC50: 0.0133 mM, above
letrozole
-
IC50: 0.10 mM, above
menadione
-
0.125 mM: 62.1% inhibition
methyl-2-[4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoyloxy]-benzoate
-
exhibits higher activity than fluconazole
methyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
methyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
-
methyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
Metyrapone
-
strong inhibition, 0.1 mM: 57.3% inhibition
Miconazole
-
IC50: 72 nM
Miconazole
-
IC50: 0.00006 mM
Miconazole
Q7Z1V1
-
myclobutanil
-
IC50: 140 nM
myclobutanil
-
IC50: 0.0290 mM
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2,4-dimethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-2-nitro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4,5-trimethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3,4-dimethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-3-trifluoromethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-ethyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-isopropyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-nitro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-pentyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-propyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluoro-phenyl)-4-trifluoromethoxy-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-fluoro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-2-methyl-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-4-fluoro-benzamide
-
-
N-(4-[4-[2-(2,4-difluoro-phenyl)-2-hydroxy-3-[1H-1,2,4]triazol-1-yl-propyl]-piperazin-1-yl]-3-fluorophenyl)-benzamide
-
-
N-pyridin-4-yl-9H-xanthene-9-carboxamide
-
strongest binding compound
N-{2-[4-(acetylamino)phenyl]ethyl}-2-[1-(4-chlorobenzoyl)-5-methoxy-2-methyl-1H-indol-3-yl]acetamide
-
interacts with heme
Nalpha-[(4-methylcyclohexyl)carbonyl]-N-pyridin-4-yltryptophanamide
-
strongest binding compound
nitrogen
-
nitrogen atmosphere
obtusifoliol
-
24.4% inhibition of 24,25-dihydrolanosterol, DHL, demethylation, no inhibition of lanosterol and 24-methylene-24,25-dihydrolanosterol demethylation
penconazole
-
IC50: 76 nM
penconazole
-
IC50: 0.0193 mM
pentyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
phenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate
-
exhibits higher activity than fluconazole
posaconazole
Q7Z1V1
-
posaconazole
Q870D1
lowest interaction energies with CYP51
posaconazole
-
-
posaconazole
-
complexes CYP51, binding structure, overview
Prochloraz
-
-
Prochloraz
-
IC50: 98 nM
Prochloraz
-
IC50: 0.0050 mM
prochlorazole
-
-
Propiconazole
-
-
Propiconazole
-
IC50: 150 nM
Propiconazole
-
IC50: 0.0083 mM
Propiconazole
-
-
prothioconazole
-
-
ravuconazole
-
-
ravuconazole
Q7Z1V1
-
ravuconazole
Q870D1
thiazole ring interacts with the side chain of Tyr131, Leu134, and Ile389. Besides the hydrophobic interaction with Phe240, Met528, and Ile529, the 4-cyano-phenyl group of ravuconazole can also form a pi-pi stacking interaction with His133
ravuconazole
-
-
rottlerin
-
interacts with heme
RS21607
-
specific inhibition of CYP51, the enzyme can be rescued by progesterone
siRNA
-
administrated single dose of 10 microg CYP51-siRNAs for 48 h results in significantly depletion of CYP51 mRNA in liver of mice fed on normal diet (from 40 to 60%). Exerts inhibition in a dose dependent manner (from 26% in 5 microg to 40% in 20 microg). Most inhibitive effect from day 3 to day 6 (over 50%) after treatment. Six days after administration of 30 microg CYP51-siRNAs (20 microg on day 0 and 10 microg on day 3), CYP51 mRNA and protein levels are significantly knocked down in mice liver. Low-density lipoprotein receptor expression is significantly elevated compared with controls in hepatic cells after CYP51-siRNAs. As a consequence, about 50% of sera low-density lipoprotein cholesterol are significantly reduced. Effect on low-density lipoprotein receptor increase and low-density lipoprotein cholesterol reduction lasts 8 days after a single 20 microg CYP51-siRNAs injection. CYP51-siRNAs can not cause any fatty liver compared with buffer-group and do not interfere with mice ovulation
-
SKF-525A
-
potent inhibitor, 1.0 mM: 100% inhibition
SPSM1
-
interacts with heme
TAK-187
Q7Z1V1
-
tebuconazole
-
IC50: 350 nM
tebuconazole
-
IC50: 0.0036 mM
tebuconazole
-
an azole inhibitor
tebuconazole
-
-
trans-2,3-dihydro-3-(1H-imidazol-1-yl)-2-(1-heptyl)-4H-1-benzopyran-4-one nitrate
-
-
trans-2,3-dihydro-3-(1H-imidazol-1-yl)-2-(1-hexyl)-4H-1-benzopyran-4-one nitrate
-
-
trans-2,3-dihydro-3-(1H-imidazol-1-yl)-2-(1-pentyl)-4H-1-benzopyran-4-one nitrate
-
-
triadimefon
-
IC50: 130 nM
triadimefon
-
IC50: 0.010 mM
triadimefon
-
-
triadimefon
-
is the less sensitive fungicide for CYP51, affinity for CYP51 is the weakest
triadimenol
-
-
triadimenol
-
IC50: 330 nM
triadimenol
-
IC50: 0.0372 mM
triadimenol
-
hydrophobicity of triadimenol is reduced by the shortening of the carbon chain and the addition of a polar oxygen atom in comparison with tebuconazole, which may be the cause of the decrease in the affinity of triadimenol compared with tebuconazole
triadimenol
-
-
triazole
-
-
triazole
-
sensitive and resistant variants of CYP51A1, mutations lead to alterations in the enzyme as drug target, primary determinants of triazole resistance, overview
voriconazole
-
-
voriconazole
Q7Z1V1
-
voriconazole
-
displays the greatest specificity
voriconazole
Q870D1
shows higher affinity with CYP51 than fluconazole
voriconazole
-
-
voriconazole
-
-
voriconazole
Q68HC3
-
additional information
-
no inhibition by 24,28-dihydroobtusifoliol
-
additional information
-
in vivo inhibition study with different strains, overview
-
additional information
-
the enzyme is highly resistant to triadimenol
-
additional information
-
Oculimacula acuformis is intrinsically resistant to triazoles and sensitive to imidazoles
-
additional information
-
14alpha-carboaldehyde reaction intermediates are effective in competitive enzyme inhibition and as hypocholesterolemic agents
-
additional information
-
design of non-azole antifungal lead compounds based on the constructed three-dimensional model of CYP51by coupling structure-based de novo design, overview
-
additional information
-
inhibitory potency, antifungal activity in vivo, and structure-function analysis of 1-(1H-1,2,4-triazol-1-yl)-2-(2,4-difluorophenyl)-3-[(4-substituted phenyl)-piperazin-1-yl]-propan-2-ol derivatives, overview
-
additional information
-
inhibition kinetics and mechanism
-
additional information
-
inhibitory potency of fungicides, antifungal drugs, and cytostatic drugs, overview
-
additional information
-
specific inhibitor screening
-
additional information
-
structure–activity relationship study of enzyme-ligand binding, pyridine binds within the heme binding pocket in an analogy with azoles, overview
-
additional information
-
EC50 values, structure-function relationship of enzyme and inhibitor interactions, overview
-
additional information
-
yeast cells are more sensitive to azole drugs than mammalian cells, yeast cells have lower P450 enzyme content and a higher IC50 value
-
additional information
-
azole antifungals have higher IC50 values against the human CYP51 than against that of Candida albicans by a factor of ca. 30
-
additional information
-
the aromatic moieties of drugs where aligning to phenylalanine and tyrosine residues that lines the hydrophobic part of the binding pocket which is itself generally hydrophobic
-
additional information
-
humanized yeast strain as compared to the parental yeast strain shows up to 1000fold reduced susceptibility to the orally active azole drugs and reduced effectiveness for the topical drugs
-
additional information
-
the parental yeast strain as compared to humanized yeast strain shows up to 1000fold higher susceptibility to the orally active azole drugs
-
additional information
-
is not inhibited by fluconazole, amphotericin B, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-benzyl-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-fluorobenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-fluorobenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-fluorobenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-chlorobenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(3-chlorobenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-chlorobenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-bromobenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-bromobenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2-methylbenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-methylbenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-nitrobenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(4-ethylbenzyl)-amino]-2-propanol, 1-(1H-1,2,4-triazole-1-yl)-2-(2,4-difluorophenyl)-3-[N-allyl-N-(2,4-dichlorobenzyl)-amino]-2-propanol, methyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate, ethyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate, isopropyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate, isopropyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate, isobutyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate, pentyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate, phenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazole-1-yl)-propyl]-amino)-methyl)-benzoate, 3-nitrophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate, 4-nitrophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate, 4-chlorophenyl-4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoate, methyl-2-[4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)-propyl]-amino)-methyl)-benzoyloxy]-benzoate or 4-(propoxycarbonyl)-phenyl-[4-((allyl[2-(2,4-difluorophenyl)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)propyl]amino)methyl)]benzoate
-
additional information
-
inhibition of CYP51 involves a coordination bond with iron of the heme group, the hydrophilic H-bonding region, the hydrophobic region, and the narrow hydrophobic cleft
-
additional information
-
affinity of the azoles for CYP51 is positively correlated with their hydrophobicity. Amino acid residues Tyr112, Phe120, Phe220, His308 and Phe497 of CYP51, forming a large hydrophobic cavity, are the key residues interacting with azole fungicides
-
additional information
-
development of a simple, highly sensitive and accurate method for screening of sterol 14alpha-demethylase inhibitors, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7-lanostene-3beta,32-diol
-
activation
-
7-lanostene-3beta-ol
-
activation
8-lanostene-3beta,32-diol
-
activation
-
8-lanostene-3beta-ol
-
activation
Cycloartenol
-
activation of enzymatic reaction
cytosolic carrier
-
required for maximum activity
-
Iron
-
the enzyme is a fusion protein with a 3Fe-4S ferredoxin
oestrogen
-
induces a high level of LDM expression in the uterus of ovariectomised mice
-
lanosterol
-
induction and activation
additional information
-
enzyme mRNA is increased by forskolin, cAMP-dependent transactivation of CYP51
-
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
-
additional information
A7LM25
effects of demethylation inhibitor fungicides on enzyme gene expression, resistamce occurs, but some are inductive, overview
-
additional information
-
3,5-cyclic adenosine monophosphate response element binding protein and follicle stimulating hormone, FSH. Up-regulate the enzyme expression during or before oocyte meturation, respectively. FSH includes via MAPK activation, overview
-
additional information
Q870D1
active site with four functional regions
-
additional information
-
progesterone treatment does not induce expression in the uterus of ovariectomised mice
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.116
(3beta,4alpha,5alpha)-4,14-dimethylcholest-8-en-3-ol
-
-
0.00911
14alpha-Methylzymosterol
A2TEF2
at pH 7.4 and 37°C
0.017
24,25-dihydrolanosterol
-
-
0.02
24,25-dihydrolanosterol
-
8-lanosten-3beta-ol
0.0077
24-methylene-24,25-dihydrolanosterol
-
-
0.0087
24-methylene-24,25-dihydrolanosterol
-
-
0.003
7-lanostene-3beta,32-diol
-
-
-
0.0001
8-lanostene-3beta,32-diol
-
-
-
0.0041
eburicol
-
isozyme CYP51A, pH not specified in the publication, temperature not specified in the publication
0.0226
eburicol
-
isozyme CYP51B, pH not specified in the publication, temperature not specified in the publication
0.0017
lanosterol
-
pH 7.4, 37°C
0.0031
lanosterol
-
isozyme CYP51A, pH not specified in the publication, temperature not specified in the publication
0.004
lanosterol
Q16850
fusion protein CYP51 (F1) consisting of the ORF of modified CYP51, a linker region containing the amino acid sequence S-T, and DELTA41 P450 reductase
0.0044
lanosterol
Q16850
fusion protein CYP51 (F2) consisting of the ORF of modified CYP51, a linker region containing the amino acid sequence S-T-E-Q-S-A-K-K-V-R-K-K-A, and DELTA55 P450 reductase
0.005
lanosterol
-
-
0.005
lanosterol
Q16850
ORF of modified CYP51
0.0067
lanosterol
-
-
0.0074
lanosterol
-
pH 7.4, 37°C
0.0086
lanosterol
-
isozyme CYP51B, pH not specified in the publication, temperature not specified in the publication
0.01852
norlanosterol
A2TEF2
at pH 7.4 and 37°C
0.01131
obtusifoliol
A2TEF2
at pH 7.4 and 37°C
0.012
obtusifoliol
-
-
0.16
obtusifoliol
-
-
0.01204
lanosterol
A2TEF2
at pH 7.4 and 37°C
additional information
additional information
-
kinetic parameters
-
additional information
additional information
-
affinity and activity for 7-lanosten-3beta-ol is very low, no exact Km; enzyme shows higher affinity for 8-lanostene conformation, such as lanosterol and 24,25-dihydrolanosterol, than for 7-lanostene one; kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetic parameters
-
additional information
additional information
-
steady-state kinetic and thermodynamic analysis
-
additional information
additional information
-
kinetics, overview
-
additional information
additional information
-
the binding of azoles, with the exception of fluconazole, to CYP51B is tight, with the Kd values for clotrimazole, itraconazole, posaconazole, and voriconazole being 0.00021, 0.00006, 0.00012, and 0.00042 mM, respectively, and 0.004 m for fluconazole
-
additional information
additional information
-
the enzyme shows a Michaelis-Menten kinetic mechanism, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
Q7Z1V1
strain EP or Y, intracellular amastigote, Vero cell as host cell
0.000002
azalanstat
Q64654
specific inhibitor, IC50 less than 0.000002 mM
0.0015
benznidazole
Q7Z1V1
strain Tulahuen, intracellular amastigote
0.02
benznidazole
Q7Z1V1
strain Tulahuen, murine 3T3 fibroblast as host cell
0.0003
bifonazole
-
IC50: 300 nM
0.0008
bifonazole
-
IC50: 0.0008 mM
0.000059
bitertanol
-
IC50: 59 nM
0.0013
bitertanol
-
IC50: 0.0013 mM
0.0000091
clotrimazole
-
IC50: 91 nM
0.0009
clotrimazole
-
IC50: 0.0009 mM
0.0001
cyproconazole
-
IC50: 100 nM
0.0228
cyproconazole
-
IC50: 0.0228 mM
0.00001
D0870
Q7Z1V1
intracellular amastigote, Vero cell as host cell
0.0001
D0870
Q7Z1V1
epimastigote
0.02
econazole
Q7Z1V1
strain Tulahuen, epimastigote
0.00022
epoxiconazole
-
IC50: 220 nM
0.002
epoxiconazole
-
IC50: 0.0020 mM
0.0322
fadrozole
-
IC50: 0.0322 mM, above
0.1
fadrozole
-
IC50: 0.10 mM, above
0.000051
fluconazole
-
IC50: 51 nM, above
0.008
fluconazole
Q7Z1V1
strain Tulahuen, intracellular amastigote; strain Tulahuen, intracellular amastigote, murine 3T3 fibroblast as host cell
0.03
fluconazole
-
IC50: 0.030 mM, above
0.1
fluconazole
Q7Z1V1
strain Tulahuen, murine 3T3 fibroblast as host cell
0.000085
flusilazole
-
IC50: 85 nM
0.0034
flusilazole
-
IC50: 0.0034 mM
0.000066
hexaconazole
-
IC50: 66 nM
0.0156
hexaconazole
-
IC50: 0.0156 mM
0.000082
imazalil
-
IC50: 82 nM
0.0361
imazalil
-
IC50: 0.0361 mM
0.000001
itraconazole
Q7Z1V1
strain Tulahuen, intracellular amastigote
0.000002
itraconazole
Q7Z1V1
intracellular amastigote, macrophages as host cell
0.000039
itraconazole
-
IC50: 39 nM
0.001
itraconazole
Q7Z1V1
strain Tulahuen, murine 3T3 fibroblast as host cell
0.03
itraconazole
-
IC50: 0.030 mM
0.000001
ketoconazole
Q7Z1V1
strain Tulahuen, intracellular amastigote; strain Y, intracellular amastigote, macrophage as host cell
0.000002
ketoconazole
Q7Z1V1
strain Y, intracellular amastigote, Vero cell as host cell
0.00001
ketoconazole
Q7Z1V1
strain Peru, intracellular amastigote, macrophage as host cell
0.000064
ketoconazole
-
IC50: 64 nM
0.0001
ketoconazole
Q7Z1V1
strain Y, epimastigote
0.0002
ketoconazole
Q7Z1V1
strain Peru, epimastigote
0.0004
ketoconazole
-
IC50: 0.0004 mM
0.03
ketoconazole
Q7Z1V1
strain Tulahuen, murine 3T3 fibroblast as host cell
0.0133
letrozole
-
IC50: 0.0133 mM, above
0.1
letrozole
-
IC50: 0.10 mM, above
0.00002
Miconazole
Q7Z1V1
strain Tulahuen, intracellular amastigote
0.00006
Miconazole
-
IC50: 0.00006 mM
0.000072
Miconazole
-
IC50: 72 nM
0.01
Miconazole
Q7Z1V1
strain Tulahuen, murine 3T3 fibroblast as host cell
0.02
Miconazole
Q7Z1V1
strain Tulahuen, epimastigote
0.00014
myclobutanil
-
IC50: 140 nM
0.029
myclobutanil
-
IC50: 0.0290 mM
0.000076
penconazole
-
IC50: 76 nM
0.0193
penconazole
-
IC50: 0.0193 mM
0.00000025
posaconazole
Q7Z1V1
strain EP, intracellular amastigote, Vero cell as host cell
0.0000005
posaconazole
Q7Z1V1
strain Tulahuen, intracellular amastigote
0.000014
posaconazole
Q7Z1V1
strain EP, epimastigote
0.0005
posaconazole
Q7Z1V1
strain Tulahuen, murine 3T3 fibroblast as host cell
0.000098
Prochloraz
-
IC50: 98 nM
0.005
Prochloraz
-
IC50: 0.0050 mM
0.00015
Propiconazole
-
IC50: 150 nM
0.0083
Propiconazole
-
IC50: 0.0083 mM
0.0000001
ravuconazole
Q7Z1V1
strain EP or Y, intracellular amastigote, Vero cell as host cell
0.0001
ravuconazole
Q7Z1V1
strain EP or Y, epimastigote
0.0000003
TAK-187
Q7Z1V1
strain EP or Y, intracellular amastigote, Vero cell as host cell
0.00035
tebuconazole
-
IC50: 350 nM
0.0036
tebuconazole
-
IC50: 0.0036 mM
0.00013
triadimefon
-
IC50: 130 nM
0.01
triadimefon
-
IC50: 0.010 mM
0.00033
triadimenol
-
IC50: 330 nM
0.0372
triadimenol
-
IC50: 0.0372 mM
0.000004
voriconazole
Q7Z1V1
strain Tulahuen, intracellular amastigote
0.03
voriconazole
Q7Z1V1
strain Tulahuen, murine 3T3 fibroblast as host cell
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000084
-
brain microsomes, substrate: lanosterol
0.00756
Q4PJW3
purified recombinant truncated, soluble, monomeric enzyme
additional information
-
-
additional information
-
substrate specificities of recombinant wild-type and mutant I105F enzymes, overview
additional information
-
wild-type and enzyme-deficient mutant sterol composition, overview
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
A1XG20
assay at
7.4
-
assay at
7.4
Q4PJW3
assay at
7.4
A8DBU6
assay at
7.5 - 8.5
-
-
7.5
-
assay at
7.9
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
A1XG20
assay at
30
-
aerobic conditions; assay at
30
-
aerobic conditions; assay at
30
-
aerobic conditions; assay at
30
-
assay at
37
-
assay at
37
-
aerobic conditions; assay at
37
-
assay at
37
A8DBU6
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.12
A8DBU6
sequence calculation
6.27
Q68HC3
sequence analysis
7.7
A2TEF2
calculated from amino acid sequence
8.7
Q673E9
amino acid sequence caculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Magnaporthe oryzae Guy11
-
-
-
Manually annotated by BRENDA team
-
is selectively expressed in preimplantation embryos
Manually annotated by BRENDA team
-
of male and female, highest level of enzyme in Leydig cells and acrosomes
Manually annotated by BRENDA team
Magnaporthe oryzae Guy11
-
-
-
Manually annotated by BRENDA team
Q673E9
mature, weak enzyme expression
Manually annotated by BRENDA team
Q0KKP4, Q0KKP5
-
Manually annotated by BRENDA team
Q0KKP4, Q0KKP5
the liver-type enzyme expression is constantly high in mature, 2-year-old male chicken compared to immature, 5-weak-old chickens, overview
Manually annotated by BRENDA team
-
primary oocytes
Manually annotated by BRENDA team
Q673E9
ovules and ovaries without pericarp, transient increase in enzyme expression around 72 h postpollination pistils, weak enzyme expression in unpollinated pistils on the day of anthesis
Manually annotated by BRENDA team
Q673E9
weak enzyme expression
Manually annotated by BRENDA team
-
etiolated Sorghum seedlings
Manually annotated by BRENDA team
Zea mays LG11
-
-
-
Manually annotated by BRENDA team
-
acrosomal membrane of elongated spermatids
Manually annotated by BRENDA team
-
acrosomal membrane of mature sperm
Manually annotated by BRENDA team
Q0KKP4, Q0KKP5
-
Manually annotated by BRENDA team
Q0KKP4, Q0KKP5
expression levels of the testis-specific exon-1-containing gene are highly increased in mature, 2-year-old male chicken compared to immature, 5-weak-old chickens, overview
Manually annotated by BRENDA team
-
during the peri-implantation period, is selectively expressed in the uterine subluminal stroma surrounding the implanting blastocyst on day 5 of pregnancy. High level of LDM expression in the uterus decidua on days 6-8 of pregnancy. Is absent in the uterus on day 5 of pseudopregnancy
Manually annotated by BRENDA team
additional information
Q673E9
tissue- and development-specific expression pattern, in situ hybridization, no enzyme expression in stems, petals, stamens, pollen, and in-vitro-grown pollen tubes, overview, enzyme expression is regulated both by pollination and by fertilization
Manually annotated by BRENDA team
additional information
A7LM25
CYP51 shows constitutive expression
Manually annotated by BRENDA team
additional information
A8DBU6
expression analysis at different developmental and growth stages, overview
Manually annotated by BRENDA team
additional information
Taiwanofungus camphoratus TFRIB 470
-
expression analysis at different developmental and growth stages, overview
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Magnaporthe oryzae Guy11
-
isoform Cyp51A
-
Manually annotated by BRENDA team
-
light membrane fraction of endoplasmic reticulum, not in plasma membrane
Manually annotated by BRENDA team
-
present during all phases of acrosome development
Manually annotated by BRENDA team
-
distribution of Erg proteins between endoplasmic reticulum and liquid particles in wild-type and DELTAerg11-DELTAerg3 mutant, overview
Manually annotated by BRENDA team
Zea mays LG11
-
light membrane fraction of endoplasmic reticulum, not in plasma membrane
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae FY1679
-
distribution of Erg proteins between endoplasmic reticulum and liquid particles in wild-type and DELTAerg11-DELTAerg3 mutant, overview
-
Manually annotated by BRENDA team
-
present during all phases of acrosome development, in liver, no detection in trans-Golgi
Manually annotated by BRENDA team
-
membrane-bound
Manually annotated by BRENDA team
Zea mays LG11
-
membrane-bound
-
Manually annotated by BRENDA team
Aspergillus fumigatus Af293, Saccharomyces cerevisiae FY1679
-
-
-
Manually annotated by BRENDA team
-
microsomal-bound
-
Manually annotated by BRENDA team
Zea mays LG11
-
microsomal-bound
-
-
Manually annotated by BRENDA team
additional information
-
not in plasma membrane, subcellular localization, distribution
-
Manually annotated by BRENDA team
additional information
Zea mays LG11
-
not in plasma membrane
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
44000
Q4PJW3
CYP51 mutant variant 1, gel filtration
684925
50000
Q4PJW3
CYP51 mutant variant 2, gel filtration
684925
51000
-
sequence analysis, truncated CYP51
706082
53000
-
SDS-PAGE and amino acid sequence analysis
285350
55050
Q64654
amino acid analysis
285353
57300
-
amino acid analysis
285352
62000
Q68HC3
sequence analysis
705462
706000
-
gel filtration
659189
additional information
-
enzyme consisting of 509 amino acids, amino acid sequencing
285354
additional information
-
protein consisting of 503 amino acids, amino acid sequencing
285354
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 53000, SDS-PAGE
?
-
x * 50000, SDS-PAGE
?
-
x * 56000, SDS-PAGE
?
Q68HC3
x * 63000, SDS-PAGE
?
-
x * 59000, SDS-PAGE
?
-
x * 52000, SDS-PAGE, recombinant enzyme
?
-
x * 61500, SDS-PAGE
?
Q673E9
x * 55200, amino acid sequence caculation
?
A1XG20
x * 59000, recombinant enzyme, SDS-PAGE
?
A8DBU6
x * 87900, full-length recombinant GST-tagged enzyme, SDS-PAGE, x * 84600, mature recombinant GST-tagged enzyme, SDS-PAGE, x * 61900, about, sequence calculation
?
A2TEF2
x * 54000, calculated from amino acid sequence
?
Taiwanofungus camphoratus TFRIB 470
-
x * 87900, full-length recombinant GST-tagged enzyme, SDS-PAGE, x * 84600, mature recombinant GST-tagged enzyme, SDS-PAGE, x * 61900, about, sequence calculation
-
?
Candida albicans ATCC MYA.2876
-
x * 61500, SDS-PAGE
-
dodecamer
-
x * 62000, SDS-PAGE, recombinant enzyme
monomer
-
1 * 53000, SDS-PAGE
monomer
Q4PJW3
1 * 44000, CYP51 mutant variant 1, 2 * 50000, CYP mutant variant 2
additional information
-
detailed spectroscopic structure analysis of enzyme with bound ligands, overview
additional information
-
three-dimensional structure analysis: the S1 subsite is the hydrophilic hydrogen-bonding region, the S2 subsite is the hydrophobic region, the S3 subsite is the narrow hydrophobic cleft formed by the residues in the helix B'-meander1 loop and the N-terminus of helix I, the S4 subsite adjacent to the beta6-1/beta1-4 sheet is another important hydrogen-bonding region in the active site, overview
additional information
A1XG20
structure homology modeling and docking model
additional information
-
three-dimensional modeling
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
building up of homology models based on crystal coordinates of enzyme in complex with inhibitors 4-phenylimidazole or fluconazole, modeling of substrate 24-methylene-24,25-dihydrolanosterol into active site
-
hanging drop vapor diffusion method, using 0.1 M Tris-HCl, pH 8.0, and 9% (w/v) PEG 6000
A2TEF2
CYP51 in complex with 4,4'-dihydroxybenzophenone, enzyme in 20 mM Tris-HCl, pH 7.5, 200 mM NaCl, and 0.5 mM EDTA, is mixed with 4,4'-dihydroxybenzophenone, which is dissolved in Me2SO at 100 mM stock concentration, to final concentrations of 0.2 mM for protein and ligand resulting in needle-like crystals, larger crystals are obtained by hanging drop vapor diffusion method from 1.2 M lithium sulfate, 0.1 M HEPES, pH 7.5, and 2% isopropyl alcohol, cryoprotection by 20% glycerol, X-ray diffraction structure determination and analysis at 1.95 A resolution
-
in complex with fluconazole
-
purified recombinant enzyme, crystal structure determination and analysis, overview
-
recombinant mutant C37L/C442A in complex with alpha-ethyl-N-4-pyridinyl-benzeneacetamide, protein is mixed with a ligand dissolved in DMSO at a 100 mM concentration to obtain a final protein concentration of 0.2 mM and a final ligand concentration of 1 to 5 mM, 15-30% PEG 4000, 2-12% isopropanol, 0.1 M HEPES, pH 7.5, X-ray diffraction at 1.53 A resolution
-
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
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
thermal inactivation kinetics
672195
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the dithionite-reduced CO-P450 complex for purified recombinant CYP51A is unstable, rapidly denaturing to inactive P420, in marked contrast to purified recombinant CYP51B, where the CO-P450 complex is stable
-
the P450 form is stabilized by estriol
-
plant demethylase is remarkably stable
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, frozen in liquid nitrogen
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant isozymes CYP51A and CYP51B from Escherichia coli, the dithionite-reduced CO-P450 complex for CYP51A is unstable, rapidly denaturing to inactive P420, in marked contrast to CYP51B, where the CO-P450 complex is stable
-
recombinant soluble, monomeric CYP51 truncation mutants from Escherichia coli in a procedure comprising several steps, overview
Q4PJW3
Ni-NTA column chromatography, and gel filtration
-
recombinant GST-tagged enzyme from Escherichia coli by glutathione affinity chromatography, cleavage of the tag by thrombin, and thrombin elimination by benzamidine affinity chromatography
Q3HTM1
recombinant enzyme from Escherichia coli strain HMS174 (DE3) by two different steps of anion exchange chromatography and hydroxyapaptite chromatography to homogeneity
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
A1XG20
by Ni2+-NTA affinity chromatography, more than 90% pure
Q68HC3
to homogeneity
Q16850
purification and reconstitution
-
recombinant sorghum CYP51
-
recombinant enzyme
-
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
CYP51A and CYP51B, sequence comparisons and phylogenetic tree of fungal CYP51 proteins, expression of isozymes CYP51A and CYP51B in Escherichia coli
-
expression of isoenzymes CYP51A and CYP51B in the Saccharomyces cerevisiae mutant strain YUG37-erg11, wherein native ERG11/CYP51 expression is controlled using a doxycycline-regulatable promoter. Aspergillus fumigatus CYP51A and CYP51B both complement Saccharomyces cerevisiae sterol 14alpha-demethylase function with comparable efficiency. In the presence of doxycycline, recombinant YUG37-pcyp51A and YUG37-pcyp51B yeasts are able to synthesize ergosterol and grow, a control strain harboring reverse-oriented cyp51A cannot. YUG37-pcyp51A and YUG37-pcyp51B constructs show identical sensitivity to itraconazole, posaconazole, clotrimazole, voriconazole, and fluconazole
-
gene cyp51A, DNA and amino acid sequence determination and analysis
-
expression of CYP51 mutant soluble, monomeric enzymes in Escherichia coli
Q4PJW3
expressed in Escherichia coli DH5alpha cells
-
expressed in Escherichia coli TOP10F cells and in Pichia pastoris cells
-
expression in Spodoptera frugiperda Sf9 cell membranes under control of the p10 promoter using the baculovirus transfection system
-
expression of wild-type and mutant enzymes in Saccharomyces cerevisiae
-
sequence comparison, phylogenetic analysis, heterologous overexpression
-
gene CYP51, DNA and amino acid sequence determination and analysis of the liver enzyme; gene CYP51, DNA and amino acid sequence determination and analysis, the gene contains a testis-specific exon 1, expression levels of the gene in testis are highly increased in mature, 2-year-old male chicken compared to immature, 5-weak-old chickens, overview
Q0KKP4, Q0KKP5
cDNA cloning
-
expressed in Saccharomyces cerevisiae BY4741 under the control of the yeast CYP51 promoter
-
gene CYP51, the proximal promoter of CYP51 contains a conserved region with clustered regulatory elements: GC box, CRE-like cAMP-response elements, and sterol regulatory element, i.e. SRE, overview, in lipid-rich, and SREBP-poor conditions, the CYP51 mRNA amount drops gradually, the promoter activity is diminished, expression in JEG-3 choriocarcinoma cells and in Hep-G2 hepatocarcinoma cells
-
sequence comparison, phylogenetic analysis, heterologous overexpression
-
the genes are located on chromosomes 3, 7, and 13, the gene on chromosome 7 is the functional one while those on chromosomes 3 and 13 are processed pseudogenes which arise from reverse transcription of mRNA in germ cells and illegitimate recombination into the genome, CYP51 responds to cholesterol feedback regulation, being upregulated in sterol limiting conditions and downregulated in cholesterol rich conditions, regulation involves the sterol regulatory elements SRE in the promoter of the gene which bind sterol regulatory element binding protein, SREBP, the CYP51 promoter also contains a cAMP regulatory element, CRE, binding cAMP regulatory proteins CREB/CREM
-
expressed in Escherichia coli
A2TEF2
full-length and truncated CYP51 fragments cloned into vector pET30 and expressed in Escherichia coli strain BL21 (DE3) pLysS
-
sequence comparison, phylogenetic analysis, heterologous overexpression
-
gene CYP51, DNA and amino acid sequence determination and analysis, gene copy numbers and silent nucleotide variations in the coding region of the MfCYP51 gene from different isolates, expression analysis, overview
A7LM25
expression in Escherichia coli as GST-tagged enzyme
Q3HTM1
sequence comparison, phylogenetic analysis, heterologous overexpression
-
expression in Escherichia coli
-
gene RV0764c, coexpression with ferredoxin in Escherichia coli strain HMS174 (DE3)
-
sequence comparison, phylogenetic analysis, heterologous overexpression
-
expressed in Escherichia coli
-
gene CYP51, DNA and amino acid sequence determination and analysis, sequence comparison, expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3)
A1XG20
cDNA, introduced into Aspergillus niger by transformation
-
cloned from a cDNA library into pGEMT-Easy vector. The pCWori+ vector transformed into Escherichia coli strain DH5alpha. Expressed in yeast YUG73 from pYES2.1 vector
Q68HC3
cDNA, cloning and functional expression
Q64654
cDNA, cloning and functional expression; cDNA expression in COS7 cells and cloning of pRT-9 cDNA; pRT-9 cDNA; pRT-9 clone, pRT-9 protein is P45014DM
-
pRT-9 cDNA; pRT-9 clone, pRT-9 protein is P45014DM
-
sequence comparison, phylogenetic analysis, heterologous overexpression
-
CYP51 cDNA cloned with pBluescript KS-. Self sufficient lanosterol 14-demethylase fusion proteins by using yeast CYP51 and P450 reductase, expressed in Escherichia coli
Q16850
expression of N-terminally GFP-tagged enzyme in strain FYN8 under control of the GAL1 promoter
-
sequence comparison, phylogenetic analysis, heterologous overexpression
-
gene CYP51, DNA and amino acid sequence determination and analysis, sequence comparison, expression in Saccharomyces cerevisiae, functional complementation of the DELTAerg11 enzyme deficient yeast mutant strain to 81% cell viability
Q673E9
cDNA cloning of Sorghum CYP51and functional expression in Escherichia coli JM109 in high levels
-
sequence comparison, phylogenetic analysis, heterologous overexpression
-
expression in Escherichia coli with tetrahistidine tag
-
gene CYP51, DNA and amino acid sequence determination and analysis, functional expression as GST-tagged enzyme in Escherichia coli
A8DBU6
sequence comparison, phylogenetic analysis, heterologous overexpression
-
expression of C-terminally His-tagged wild-type and mutant enzymes
-
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
-
gene CYP51, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, expression of His-tagged enzyme in Escherichia coli
-
sequence comparison, phylogenetic analysis, heterologous overexpression
-
subcloned into the pCW vector (Nde I/Hind III cloning sites) and expressed in Escherichia coli
-
sequence comparison, phylogenetic analysis, heterologous overexpression
-
expressed in Saccharomyces cerevisiae mutant strain YUG37::erg11
-
expression of wild-type and mutant MgCYP51 variants in a Saccharomyces cerevisiae mutant strain YUG37:erg11 carrying a doxycycline-regulatable tetO7-CYC promoter controlling native CYP51 expression. The wild-type MgCYP51 protein complements the function of the orthologous protein in the yeast, while mutants L50S, Y459D, and Y461H do not, only mutant I381V/Y459D/Y461H partially restores the activity of the yeast mutant
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of both isoform CYP51A and CYP51B is significantly induced by exposure to sterol demethylation inhibitor fungicides tebuconazole, propiconazole, and prochloraz
-
expression of both isoform CYP51A and CYP51B is significantly induced by exposure to sterol demethylation inhibitor fungicides tebuconazole, propiconazole, and prochloraz
Magnaporthe oryzae Guy11
-
-
LDM expression is induced in the uterine stroma under artificial decidualisation. Oestrogen, but not progesterone, treatment induces a high level of LDM expression in the uterus of ovariectomised mice
-
transcription of AcCYP51 increases in various culture conditions including adding squalene, lanosterol, itroconazole, and oleic acid as inducers. Itroconazol, a fungicide that targets CYP51 and as an inhibitor causes the accumulation of lanosterol and reduced ergosterol biosynthesis in fungi, also induces AcCYP51 expression after 24 h of treatment
A8DBU6
transcription of AcCYP51 increases in various culture conditions including adding squalene, lanosterol, itroconazole, and oleic acid as inducers. Itroconazol, a fungicide that targets CYP51 and as an inhibitor causes the accumulation of lanosterol and reduced ergosterol biosynthesis in fungi, also induces AcCYP51 expression after 24 h of treatment
Taiwanofungus camphoratus TFRIB 470
-
-
expressed in baculovirus and in Escherichia coli
Q7Z1V1
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H399P/D411N
-
CYP51Ap mutant of voriconazole-resistant clinical isolate, shows higher minimum inhibitory concentration of voriconazole compared with the drug-susceptible parent
K197N
-
CYP51Ap mutant of voriconazole-resistant clinical isolate, shows higher minimum inhibitory concentration of voriconazole compared with the drug-susceptible parent
K197N/D282E/M288L
-
CYP51Ap mutant of voriconazole-resistant clinical isolate, shows higher minimum inhibitory concentration of voriconazole compared with the drug-susceptible parent
T454P/T486P
-
CYP51Ap mutant of voriconazole-resistant clinical isolate, shows higher minimum inhibitory concentration of voriconazole compared with the drug-susceptible parent
K147Q
-
mutation found in strains expressing very high levels of resistance against sterol 14alpha-demethylase inhibiting fungicides
Y136F
-
a naturally occuring mutation in both wheat and barley powdery mildew that leads to resistance or low sensitivity against triazole
D116E
-
the azole Kd value of the mutant enzyme is little altered compared to the wild type enzyme
F105L
-
the azole Kd value of the mutant enzyme is little altered compared to the wild type enzyme
F145L
-
significant modification of heme environment as judged from spectral properties, about 45% of wild-type activity, resistant to azoles
K143R
-
the mutant shows a sustained capacity for producing ergosterol, even in the presence of fluconazole
R467K
-
the azole Kd value of the mutant enzyme is little altered compared to the wild type enzyme
V456I
-
the mutation leads to an 8fold increase in fluconazole minimal inhibitory concentrations of Pichia pastoris mutants compared to the wild type controls. The mutant shows a sustained capacity for producing ergosterol, even in the presence of fluconazole
Y118A
-
site-directed mutagenesis, the mutant shows reduced actalytic activity an reduced azole susceptibility compared to the wild-type enzyme
Y118F
-
site-directed mutagenesis, the mutant shows reduced actalytic activity an reduced azole susceptibility compared to the wild-type enzyme
Y118T
-
site-directed mutagenesis, the mutant shows reduced actalytic activity an reduced azole susceptibility compared to the wild-type enzyme
Y132H
-
significant modification of heme environment as judged from spectral properties, about 50% of wild-type activity, resistant to azoles
Y132H
-
the azole Kd value of the mutant enzyme is clearly altered compared to the wild type enzyme
Y447H
-
the mutation leads to an 8fold increase in fluconazole minimal inhibitory concentrations of Pichia pastoris mutants compared to the wild type controls. The mutant shows a sustained capacity for producing ergosterol, even in the presence of fluconazole
D116E
Candida albicans ATCC MYA.2876
-
the azole Kd value of the mutant enzyme is little altered compared to the wild type enzyme
-
F105L
Candida albicans ATCC MYA.2876
-
the azole Kd value of the mutant enzyme is little altered compared to the wild type enzyme
-
R467K
Candida albicans ATCC MYA.2876
-
the azole Kd value of the mutant enzyme is little altered compared to the wild type enzyme
-
Y132H
Candida albicans ATCC MYA.2876
-
the azole Kd value of the mutant enzyme is clearly altered compared to the wild type enzyme
-
G484S
Q870D1
azole resistance
F145A
-
the mutation leads to a serious weakening of steroid ligand binding
I383A
-
the mutation leads to a serious weakening of steroid ligand binding
R388A
-
the mutation leads to a serious weakening of steroid ligand binding
V149A
-
the mutation leads to a serious weakening of steroid ligand binding
Y137A
-
the mutation leads to a serious weakening of steroid ligand binding
E113D
-
increase in sensitivity to fluconazole, voriconazole, no difference in sensitivity to itraconazole
D134G
-
the mutation significantly impacts azole sensitivity
G143A
-
a cytochrome b substitution mutation
I381V
-
the naturally occuring mutation causes resistance against triazole inhibitors epoxiconazole and tebuconazole
I381V
-
naturally occuring mutation, the mutant shows reduced sensitivity to azole inhibitors
I381V
-
site-directed mutagenesis, the mutant enzyme does not complement the CYP-deficient Saccharomyces cerevisiae mutant strain YUG37:erg11
I381V/Y459D/Y461H
-
site-directed mutagenesis, the mutant enzyme does partially complement the CYP-deficient Saccharomyces cerevisiae mutant strain YUG37:erg11
S524T
-
the mutation confers decreased sensitivity to azole fungicides including epoxiconazole and prothioconazole, the mutation significantly impacts azole sensitivity
S524T/Y461S
-
the mutations confer decreased sensitivity to azole fungicides including epoxiconazole and prothioconazole
V136A
-
the mutation significantly impacts azole sensitivity
Y137F
-
the naturally occuring mutation does not affect triazole sensitivity
Y137F
-
the mutation confers greatest decrease in sensitivity to the azole fungicide triadimenol
Y137F/V136A
-
the mutation significantly impacts azole sensitivity
Y459D
-
site-directed mutagenesis, the mutant enzyme does not complement the CYP-deficient Saccharomyces cerevisiae mutant strain YUG37:erg11
Y461H
-
site-directed mutagenesis, the mutant enzyme does not complement the CYP-deficient Saccharomyces cerevisiae mutant strain YUG37:erg11
Y461S
-
the mutation significantly impacts azole sensitivity
I381V
-
site-directed mutagenesis, the mutant enzyme does not complement the CYP-deficient Saccharomyces cerevisiae mutant strain YUG37:erg11
-
Y459D
-
site-directed mutagenesis, the mutant enzyme does not complement the CYP-deficient Saccharomyces cerevisiae mutant strain YUG37:erg11
-
Y461H
-
site-directed mutagenesis, the mutant enzyme does not complement the CYP-deficient Saccharomyces cerevisiae mutant strain YUG37:erg11
-
Y132N/T469S
-
CYP51Ap mutant of voriconazole-resistant clinical isolate, shows higher minimum inhibitory concentration of voriconazole compared with the drug-susceptible parent
additional information
-
gene cyp51A knockout strains CM-A8, CM-A41, and CM-A83 show reduced sensitivity to azole in vivo, overview
Y136F/K147Q
-
a naturally occuring double mutation in barley powdery mildew that leads to high resistance against triazole
additional information
Q4PJW3
construction of a soluble, monomeric enzyme, two variants of bovine CYP51 with different truncations and modifications in their Nterminal membrane-spanning domains, overview
C37L/C442A
-
site-directed mutagenesis, structure determination
additional information
-
direct electron transfer is measured between CYP51 and graphite screen-printed electrodes modified with gold nanoparticles and with the membrane-like synthetic surfactant didodecyl dimethylammonium bromide, determination of the formal potential of the Fe3+/Fe2+ pair, detailed overview, lanosterol addition to the oxygenated solution causes a concentration-dependent increase in the reduction current in voltammetric and amperometric experiments
F180L
-
the naturally occuring mutation is responsible for the resistance to triazoles
additional information
-
the enzyme shows a number of polymorphisms at the amino acid level
additional information
A1XG20
determination of four naturally occuring polymorphisms or mutation in the CYP51 sequence, overview
T125K
-
increase in sensitivity to fluconazole, voriconazole, no difference in sensitivity to itraconazole
additional information
-
sterol composition of different species isolated from human lung, two distinct sterol compositional phenotypes occur, one, the wild-type, is characterized by DELTA7 C28- and C24 24-alkylsterols with only low proportions of higher molecular mass components, the other type, a mutant with 14alpha-demethylase deficiency, is dominated by high C31 and C32 24-alkylsterols, especially pneumocysterol, NMR sterol analysis, overview
additional information
-
construction of a deletion mutant strain DELTAerg11, the defect is lethal, but mutants survive in a DELTAerg3 background, erg11/erg3 mutant lacks ergosterol but compensates the lack, sterol distrubution is altered, mutant sterol composition and phenotype, overview
additional information
Saccharomyces cerevisiae FY1679
-
construction of a deletion mutant strain DELTAerg11, the defect is lethal, but mutants survive in a DELTAerg3 background, erg11/erg3 mutant lacks ergosterol but compensates the lack, sterol distrubution is altered, mutant sterol composition and phenotype, overview
-
additional information
-
mutant A3(2) containing a transposon insertion, no synthesis of functional hemoprotein, viable strain
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
L50S
-
site-directed mutagenesis, the mutant enzyme does not complement the CYP-deficient Saccharomyces cerevisiae mutant strain YUG37:erg11
additional information
-
construction of a deletion mutant by deletion of codons 459 and 460, the mutant shows a continuous distribution of EC50 values across isolates with either I381 or V381, and has no measurable effect on azole sensitivity
additional information
-
construction of the deletion mutant DELTAY459/G460
L50S
-
site-directed mutagenesis, the mutant enzyme does not complement the CYP-deficient Saccharomyces cerevisiae mutant strain YUG37:erg11
-
additional information
-
construction of the deletion mutant DELTAY459/G460
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
the enzyme is a target for antifungal inhibitors in protection of crops against fungal pathogens
medicine
-
fluconazole-resistant strain isolated from patients receiving long-term azole treatment shows Y132H and F145L substitutions
medicine
-
the enzyme is a target for antifungal inhibitors
drug development
Q870D1
structural model of CYP51 can be used in azole optimization, virtual screening, or de novo inhibitor design for the discovery of new antifungal agents
drug development
-
CYP51 is a potential anticholesterolemic drug target
drug development
-
the humanized yeast strain provides a useful tool for initial specificity testing for new drugs targeting CYP51 and clearly differentiates azole antifungals in a side-by-side comparison
drug development
-
non-conservative Phe497 and Phe220 of CYP51 may be key residues for design of potent specific fungicides for CYP51
medicine
Q3HTM1
the enzyme is a target in treatment of the chronic lung disease caused by Mycobacterium avium
drug development
-
CYP51 is a key target for fungal antibiotic therapy
drug development
-
the enzyme is a primary target in treatment of fungal infections in organisms ranging from humans to plants, and development of more potent and selective CYP51 inhibitors is an important biological objective
pharmacology
-
CYP51 is a key target for fungal antibiotic therapy
agriculture
-
silencing of enzyme by potato virus X::Nt CYP51-1 transcripts, accumulation of obtusifoliol and other 14alpha-methyl sterols
agriculture
-
the enzyme is a target for antifungal inhibitors in protection of crops against fungal pathogens
drug development
A1XG20
CYP51 is a prime target of antifungal drugs
medicine
Q64654
target for cholesterol-lowering drugs
pharmacology
-
-
pharmacology
Q64654
target for cholesterol-lowering drugs
agriculture
-
target enzyme for azole antifungal agents. These specific inhibitors are of great importance as plant growth regulators, fungicides and herbicides in the agricultural and medical fields
medicine
-
target enzyme for azole antifungal agents. These specific inhibitors are of great importance as plant growth regulators, fungicides and herbicides in the agricultural and medical fields
pharmacology
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target enzyme for azole antifungal agents. These specific inhibitors are of great importance as plant growth regulators, fungicides and herbicides in the agricultural and medical fields
agriculture
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target enzyme for azole antifungal agents. These specific inhibitors are of great importance as plant growth regulators, fungicides and herbicides in the agricultural and medical fields
agriculture
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all known functional sterols lack a 14alpha-methyl group, and therefore the 14alpha-demethylation reaction has received much attention from the pharmaceutical and agriculture-chemical industry as a possible means to specifically control and inhibit sterol biosynthesis in mammals, fungi, and plant
medicine
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target enzyme for azole antifungal agents. These specific inhibitors are of great importance as plant growth regulators, fungicides and herbicides in the agricultural and medical fields
pharmacology
-
target enzyme for azole antifungal agents. These specific inhibitors are of great importance as plant growth regulators, fungicides and herbicides in the agricultural and medical fields
pharmacology
-
all known functional sterols lack a 14alpha-methyl group, and therefore the 14alpha-demethylation reaction has received much attention from the pharmaceutical and agriculture-chemical industry as a possible means to specifically control and inhibit sterol biosynthesis in mammals, fungi, and plant, target enzyme for the design of phyla-specific sterol 14alpha-demethylase inhibitors
medicine
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the enzyme is a potential drug target for treatment of Chagas disease
agriculture
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target enzyme for azole antifungal agents. These specific inhibitors are of great importance as plant growth regulators, fungicides and herbicides in the agricultural and medical fields
agriculture
-
target of important agrochemicals such as fungicides, plant growth regulators and herbicides
medicine
-
target enzyme for azole antifungal agents. These specific inhibitors are of great importance as plant growth regulators, fungicides and herbicides in the agricultural and medical fields
pharmacology
-
target enzyme for azole antifungal agents. These specific inhibitors are of great importance as plant growth regulators, fungicides and herbicides in the agricultural and medical fields
agriculture
Zea mays LG11
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target enzyme for azole antifungal agents. These specific inhibitors are of great importance as plant growth regulators, fungicides and herbicides in the agricultural and medical fields, target of important agrochemicals such as fungicides, plant growth regulators and herbicides
-
medicine
Zea mays LG11
-
target enzyme for azole antifungal agents. These specific inhibitors are of great importance as plant growth regulators, fungicides and herbicides in the agricultural and medical fields
-
pharmacology
Zea mays LG11
-
target enzyme for azole antifungal agents. These specific inhibitors are of great importance as plant growth regulators, fungicides and herbicides in the agricultural and medical fields
-
agriculture
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the enzyme is a target for antifungal inhibitors in protection of crops against fungal pathogens