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Information on EC 1.14.14.154 - sterol 14alpha-demethylase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WPP9

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IUBMB Comments
This cytochrome P-450 (heme-thiolate) enzyme acts on a range of steroids with a 14alpha-methyl group, such as obtusifoliol and lanosterol. The enzyme catalyses a hydroxylation and a reduction of the 14alpha-methyl group, followed by a second hydroxylation, resulting in the elimination of formate and formation of a 14(15) double bond.
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Mycobacterium tuberculosis
UNIPROT: P9WPP9
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The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
Synonyms
cyp51, erg11, cyp51a, cyp51a1, erg11p, cyp51b, lanosterol 14alpha-demethylase, lanosterol 14 alpha-demethylase, lanosterol demethylase, sterol 14alpha-demethylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14alpha-lanosterol demethylase
-
lanosterol 14alpha-demethylase
-
sterol 14alpha-demethylase
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14-demethylase
-
-
-
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14alpha-demethylase
-
-
-
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14alpha-methylsterol 14alpha-demethylase
-
-
-
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14alpha-sterol demethylase
-
-
-
-
14DM
-
-
-
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CYP51
CYPL1
-
-
-
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cytochrome CYP51
-
-
-
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cytochrome P 450 CYP51
-
-
-
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cytochrome P-450 lanosterol 14alpha-demethylase
-
-
-
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cytochrome P-450-dependent 14alpha-sterol demethylase
-
-
-
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cytochrome P-450-dependent obtusifoliol 14alpha-demethylase
-
-
-
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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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cytochrome-P450 14alpha-demethylase
-
-
-
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demethylase, methylsterol 14alpha-
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-
-
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eburicol 14 alpha-demethylase
-
-
-
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eburicol 14alpha-demethylase
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-
-
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lanosterol 14 alpha-demethylase
-
-
-
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lanosterol 14-demethylase
-
-
-
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lanosterol 14alpha-demethylase
-
-
-
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lanosterol 14alpha-methyldemethylase
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-
-
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lanosterol C-14 demethylase
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-
-
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lanosterol demethylase
-
-
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LDM
-
-
-
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methylsterol 14alpha-demethylase (P 450 CYP51)
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Obtusifoliol 14-alpha demethylase
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obtusifoliol 14-demethylase
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-
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obtusifoliol 14alpha-demethylase
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-
-
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obtusifoliol-metabolizing 14alpha-demethylase
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-
-
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obtusufoliol 14-demethylase
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-
-
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P 450 lanosterol C-14 demethylase
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P-450 lanosterol demethylase
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-
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P-45014DM
-
-
-
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P-45014DM-containing monooxygenase system
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-
-
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P-450OBT 14DM
-
-
-
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P450(14DM)
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-
-
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P450-14DM
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-
-
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P450-L1A1
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-
-
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P45014DM
-
-
-
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sterol 14-demethylase
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-
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sterol 14-demethylase P450
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-
-
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sterol 14alpha-demethylase
sterol 14alpha-demethylase (CYP51)
-
-
-
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sterol 14alpha-demethylase cytochrome P 450
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sterol C14 demethylase
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-
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sterol demethylase P450
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sterol-14alpha-demethylase
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a 14alpha-methylsteroid + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = a DELTA14-steroid + formate + 3 [oxidized NADPH-hemoprotein reductase] + 4 H2O
show the reaction diagram
heme iron reduction as a rate-limiting step
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxygenation
-
-
-
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redox reaction
-
-
-
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oxidation
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-
-
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reduction
-
-
-
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hydroxylation
-
-
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monooxygenation
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
sterol,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (14-methyl cleaving)
This cytochrome P-450 (heme-thiolate) enzyme acts on a range of steroids with a 14alpha-methyl group, such as obtusifoliol and lanosterol. The enzyme catalyses a hydroxylation and a reduction of the 14alpha-methyl group, followed by a second hydroxylation, resulting in the elimination of formate and formation of a 14(15) double bond.
CAS REGISTRY NUMBER
COMMENTARY hide
138674-19-8
deleted registry number
341989-59-1
deleted registry number
60063-87-8
-
90463-45-9
deleted registry number
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
(3beta,5alpha)-4,4-dimethylcholesta-8,14-dien-3-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
?
estriol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + 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 + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
? + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
2-phenylimidazole + [reduced NADPH-hemoprotein reductase] + 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
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
estriol + [reduced NADPH-hemoprotein reductase] + O2
?
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 + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
(3beta,5alpha)-4,4-dimethylcholesta-8,14-dien-3-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
eburicol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
4,4-dimethylcholesta-8,14,24-trien-3-ol + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
24,25-dihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
24-methylenedihydrolanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
the enzyme is involved in functional sterol, ergosterol, and sitosterol biosynthesis
-
-
?
lanosterol + O2 + NADPH + H+
4,4-dimethyl-5alpha-cholesta-8,14,24-triene-3beta-ol + formate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
norlanosterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
obtusifoliol + [reduced NADPH-hemoprotein reductase] + O2
4alpha-methyl-5alpha-ergost-8,14,24(28)-trien-3beta-ol + formate + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
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cytochrome P450
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a cytochrome P450 enzyme
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Ferredoxin
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Fdx binds a [3Fe-4S] iron-sulfur cluster, encoded by gene RV0763c adejacent to the gene encoding the enzyme
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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a cytochrome P450 enzyme
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
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(Z)-2,3-dihydro-3-(1H-imidazol-1-yl)-2-(1-butyl)-4H-1-benzopyran-4-one oxime
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(Z)-trans-2,3-dihydro-3-(1H-imidazol-1-yl)-2-(1-pentyl)-4H-1-benzopyran-4-one oxime
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11-ketoestrone
type I binding mechanism
2,7-dihydroxy-9-fluorenone
type I binding mechanism
2-(benzo[d]-2,1,3-thiadiazole-4-sulfonyl)-2-amino-2-phenyl-N-(pyridinyl-4)-acetamide
binding structure, overview
2-phenylimidazole
Kd-value 2.1 mM, comparison of affinity and binding to human and Mycobacterium tuberculosis enzyme
4,4'-dihydroxybenzophenone
binds at the active site via a type I mechanism targeting the flexible region, binding structure and kinetics, overview
4-phenylimidazole
Kd-value 0.29 mM, comparison of affinity and binding to human and Mycobacterium tuberculosis enzyme
alpha-ethyl-N-4-pyridinyl-benzeneacetamide
binds to the non-heme iron, binding structure involving residues H259 and Y76, overview
clomiphene
interacts with heme, is less potent than azoles
estriol
a substrate analogue
fluconazole
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
ketoconazole
N-{2-[4-(acetylamino)phenyl]ethyl}-2-[1-(4-chlorobenzoyl)-5-methoxy-2-methyl-1H-indol-3-yl]acetamide
interacts with heme
rottlerin
interacts with heme
SPSM1
interacts with heme
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
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trans-2,3-dihydro-3-(1H-imidazol-1-yl)-2-(1-pentyl)-4H-1-benzopyran-4-one nitrate
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1-phenylimidazole
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heme iron-coordinating inhibitor
4-phenylimidazole
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heme iron-coordinating inhibitor
imidazole inhibitors
-
-
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triazole inhibitors
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-
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additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
substrate specificity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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 enzyme, crystal structure determination and analysis, overview
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
thermal inactivation kinetics
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the P450 form is stabilized by estriol
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain HMS174 (DE3) by two different steps of anion exchange chromatography and hydroxyapaptite chromatography to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
gene RV0764c, coexpression with ferredoxin in Escherichia coli strain HMS174 (DE3)
-
sequence comparison, phylogenetic analysis, heterologous overexpression
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
pharmacology
CYP51 is a key target for fungal antibiotic therapy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Matsuura, K.; Yoshioka, S.; Tosha, T.; Hori, H.; Ishimori, K.; Kitagawa, T.; Morishima, I.; Kagawa, N.; Waterman, M.R.
Structural diversities of active site in clinical azole-bound forms between sterol 14alpha-demethylases (CYP51s) from human and Mycobacterium tuberculosis
J. Biol. Chem.
280
9088-9096
2005
Homo sapiens, Mycobacterium tuberculosis (P9WPP9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPP9)
Manually annotated by BRENDA team
Waterman, M.R.; Lepesheva, G.I.
Sterol 14alpha-demethylase, an abundant and essential mixed-function oxidase
Biochem. Biophys. Res. Commun.
338
418-422
2005
Homo sapiens, Methylococcus capsulatus, Mycobacterium tuberculosis, Trypanosoma brucei, Acanthamoeba polyphaga
Manually annotated by BRENDA team
McLean, K.J.; Warman, A.J.; Seward, H.E.; Marshall, K.R.; Girvan, H.M.; Cheesman, M.R.; Waterman, M.R.; Munro, A.W.
Biophysical characterization of the sterol demethylase P450 from Mycobacterium tuberculosis, its cognate ferredoxin, and their interactions
Biochemistry
45
8427-8443
2006
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Lepesheva, G.I.; Waterman, M.R.
Sterol 14alpha-demethylase cytochrome P 450 (CYP51), a P450 in all biological kingdoms
Biochim. Biophys. Acta
1770
467-477
2007
Candida albicans, Homo sapiens, Methylococcus capsulatus, Mycobacterium tuberculosis, Mycolicibacterium smegmatis, Rattus norvegicus, Saccharomyces cerevisiae, Sorghum bicolor, Trypanosoma brucei, Trypanosoma cruzi, Ustilago maydis
Manually annotated by BRENDA team
Podust, L.M.; von Kries, J.P.; Eddine, A.N.; Kim, Y.; Yermalitskaya, L.V.; Kuehne, R.; Ouellet, H.; Warrier, T.; Altekoester, M.; Lee, J.S.; Rademann, J.; Oschkinat, H.; Kaufmann, S.H.; Waterman, M.R.
Small-molecule scaffolds for CYP51 inhibitors identified by high-throughput screening and defined by X-ray crystallography
Antimicrob. Agents Chemother.
51
3915-3923
2007
Mycobacterium tuberculosis (P9WPP9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPP9)
Manually annotated by BRENDA team
Shumyantseva, V.V.; Bulko, T.V.; Kuznetsova, G.P.; Lisitsa, A.V.; Ponomarenko, E.A.; Karuzina, I.I.; Archakov, A.I.
Electrochemical reduction of sterol-14alpha-demethylase from Mycobacterium tuberculosis (CYP51b1)
Biochemistry (Moscow)
72
658-663
2007
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Eddine, A.N.; von Kries, J.P.; Podust, M.V.; Warrier, T.; Kaufmann, S.H.; Podust, L.M.
X-ray structure of 4,4-dihydroxybenzophenone mimicking sterol substrate in the active site of sterol 14alpha-demethylase (CYP51)
J. Biol. Chem.
283
15152-15159
2008
Mycobacterium tuberculosis (P9WPP9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPP9)
Manually annotated by BRENDA team
Buckner, F.S.
Sterol 14-demethylase inhibitors for Trypanosoma cruzi infections
Adv. Exp. Med. Biol.
625
61-80
2008
Candida albicans, Homo sapiens, Mycobacterium tuberculosis, Trypanosoma brucei, Trypanosoma cruzi (Q7Z1V1), Trypanosoma cruzi
Manually annotated by BRENDA team
Maurice, H.; Tuarira, E.; Mwambete, K.
Virtual high screening throughput and design of 14alpha-lanosterol demethylase inhibitors against Mycobacterium tuberculosis
Afr. J. Biotechnol.
8
3072-3078
2009
Mycobacterium tuberculosis (P9WPP9), Mycobacterium tuberculosis H37Rv (P9WPP9)
-
Manually annotated by BRENDA team
Sen, K.; Hackett, J.C.
Molecular oxygen activation and proton transfer mechanisms in lanosterol 14alpha-demethylase catalysis
J. Phys. Chem. B
113
8170-8182
2009
Mycobacterium tuberculosis (P9WPP9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPP9)
Manually annotated by BRENDA team
Petushkova, N.; Lisitsa, A.; Pozdnev, V.; Karuzina, I.
A fluorometric method for determination of catalytic activity of CYP51b1 (sterol 14alpha-demethylase) with coumarin derivatives
Biochemistry (Moscow) Suppl. B
4
104-106
2010
Mycobacterium tuberculosis
-
Manually annotated by BRENDA team
Emami, S.; Banipoulad, T.; Irannejad, H.; Foroumadi, A.; Falahati, M.; Ashrafi-Khozani, M.; Sharifynia, S.
Imidazolylchromanones containing alkyl side chain as lanosterol 14alpha-demethylase inhibitors: synthesis, antifungal activity and docking study
J. Enzyme Inhib. Med. Chem.
29
263-271
2014
Mycobacterium tuberculosis (P9WPP9), Mycobacterium tuberculosis H37Rv (P9WPP9)
Manually annotated by BRENDA team