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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.14.15.4 - steroid 11beta-monooxygenase and Organism(s) Homo sapiens and UniProt Accession P19099

for references in articles please use BRENDA:EC1.14.15.4
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
A heme-thiolate protein (P-450). Also hydroxylates steroids at the 18-position, and converts 18-hydroxycorticosterone into aldosterone.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P19099
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
cyp11b2, cyp11b1, aldosterone synthase, 11 beta-hydroxylase, 11beta-hydroxylase, 11-hydroxylase, p450c11, 11-beta-hydroxylase, p45011beta, steroid 11beta-hydroxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aldosterone synthase
-
cytochrome P450 11B2
-
cytochrome P450 11beta-hydroxylase
-
11-hydroxylase
-
-
11-beta hydroxylase
-
-
11-beta-hydroxylase
-
-
11-hydroxylase
-
-
11beta hydroxylase
-
-
ALDOS
-
-
-
-
Aldosterone synthase
Aldosterone-synthesizing enzyme
-
-
-
-
C450XIB2
-
-
-
-
CYP11B1
CYP11B2
CYPXIB
-
-
-
-
CYPXIB1
-
-
-
-
CYPXIB2
-
-
-
-
CYPXIB3
-
-
-
-
cytochrome P450 11B1
-
cytochrome P450 11beta-hydroxylase
-
cytochrome P45011beta
-
-
P-450(11 beta,aldo)
-
-
-
-
P-450Aldo
-
-
-
-
P-450c11
-
-
-
-
P-450C18
-
-
-
-
P450(11 beta)-DS
-
-
-
-
P450C11
-
-
-
-
Steroid 11-beta-hydroxylase
steroid 11-hydroxylase
-
-
steroid 11beta-hydroxylase
steroid 11beta-monooxygenase
-
-
-
-
steroid 11beta/18-hydroxylase
-
-
-
-
Steroid 18-hydroxylase
-
-
-
-
steroid-11beta-hydroxylase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
hydroxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
steroid,reduced-adrenal-ferredoxin:oxygen oxidoreductase (11beta-hydroxylating)
A heme-thiolate protein (P-450). Also hydroxylates steroids at the 18-position, and converts 18-hydroxycorticosterone into aldosterone.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-66-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
?
show the reaction diagram
-
-
-
?
11-deoxycorticosterone + reduced adrenodoxin + O2
corticosterone + oxidized adrenodoxin + H2O
show the reaction diagram
11-deoxycortisol + oxidized adrenodoxin + H2O
cortisol + reduced adrenodoxin + O2
show the reaction diagram
-
-
-
?
11-deoxycortisol + reduced adrenodoxin + O2
cortisol + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
?
18-hydroxycorticosterone + reduced adrenodoxin + O2
aldosterone + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
?
androstendione + reduced adrenodoxin + O2
? + oxidized adrenodoxin + H2O
show the reaction diagram
low activity with isozyme CYP11B2
-
-
?
corticosterone + reduced adrenodoxin + O2
18-hydroxycorticosterone + oxidized adrenodoxin + H2O
show the reaction diagram
deoxycorticosterone + oxidized adrenodoxin + H2O
corticosterone + reduced adrenodoxin + O2
show the reaction diagram
-
-
-
?
progesterone + reduced adrenodoxin + O2
11beta-hydroxyprogesterone + oxidized adrenodoxin + H2O
show the reaction diagram
low activity with isozyme CYP11B2
-
-
?
testosterone + reduced adrenodoxin + O2
11-hydroxytestosterone + oxidized adrenodoxin + H2O
show the reaction diagram
low activity with isozyme CYP11B2
-
-
?
11-deoxycorticosterone + adrenal ferredoxin + H2O
corticosterone + reduced adrenal ferredoxin + O2
show the reaction diagram
-
-
-
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
11beta-hydroxylation
-
?
11-deoxycorticosterone + reduced adrenodoxin + O2
corticosterone + oxidized adrenodoxin + H2O
show the reaction diagram
11-deoxycortisol + adrenal ferredoxin + H2O
cortisol + reduced adrenal ferredoxin + O2
show the reaction diagram
-
-
-
-
?
11-deoxycortisol + NADPH + O2
cortisol + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
11-deoxycortisol + oxidized adrenodoxin + H2O
cortisol + reduced adrenodoxin + O2
show the reaction diagram
-
-
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + oxidized adrenal ferredoxin + H2O
show the reaction diagram
11-deoxycortisol + reduced adrenodoxin + O2
cortisol + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
?
18-hydroxycorticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
18-hydroxycorticosterone + reduced ferredoxin + O2
aldosterone + ferredoxin + H2O
show the reaction diagram
a steroid + reduced adrenodoxin + O2
an 11beta-hydroxysteroid + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
androstendione + reduced adrenodoxin + O2
? + oxidized adrenodoxin + H2O
show the reaction diagram
low activity with isozyme CYP11B1
-
-
?
corticosterone + reduced adrenal ferredoxin + O2
11-deoxycorticosterone + adrenal ferredoxin + ?
show the reaction diagram
-
-
-
-
?
corticosterone + reduced adrenodoxin + O2
18-hydroxycorticosterone + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
?
cortisol + reduced adrenal ferredoxin + O2
11-deoxycortisol + adrenal ferredoxin + ?
show the reaction diagram
deoxycorticosterone + oxidized adrenodoxin + H2O
corticosterone + reduced adrenodoxin + O2
show the reaction diagram
-
-
-
?
progesterone + reduced adrenodoxin + O2
11beta-hydroxyprogesterone + oxidized adrenodoxin + H2O
show the reaction diagram
low activity with isozyme CYP11B1
-
-
?
testosterone + reduced adrenodoxin + O2
11-hydroxytestosterone + oxidized adrenodoxin + H2O
show the reaction diagram
low activity with isozyme CYP11B1
-
-
?
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
11-deoxycorticosterone + reduced adrenodoxin + O2
corticosterone + oxidized adrenodoxin + H2O
show the reaction diagram
18-hydroxycorticosterone + reduced adrenodoxin + O2
aldosterone + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
?
corticosterone + reduced adrenodoxin + O2
18-hydroxycorticosterone + oxidized adrenodoxin + H2O
show the reaction diagram
11-deoxycorticosterone + reduced adrenodoxin + O2
corticosterone + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
?
11-deoxycortisol + adrenal ferredoxin + H2O
cortisol + reduced adrenal ferredoxin + O2
show the reaction diagram
-
-
-
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + oxidized adrenal ferredoxin + H2O
show the reaction diagram
18-hydroxycorticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
18-hydroxycorticosterone + reduced ferredoxin + O2
aldosterone + ferredoxin + H2O
show the reaction diagram
-
aldosterone is one of the main effectors of the renin–angiotensin–aldosterone system, RAAS, regulating salt and water homeostasis and thereby also blood pressure
-
-
?
corticosterone + reduced adrenal ferredoxin + O2
11-deoxycorticosterone + adrenal ferredoxin + ?
show the reaction diagram
-
-
-
-
?
corticosterone + reduced adrenodoxin + O2
18-hydroxycorticosterone + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
?
cortisol + reduced adrenal ferredoxin + O2
11-deoxycortisol + adrenal ferredoxin + ?
show the reaction diagram
-
in the adrenal zona fasciculata
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adrenodoxin
-
adrenodoxin
-
Ferredoxin
-
NADPH
reduced adrenal ferredoxin
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
heme iron
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-4-(5,6,7,8-tetrahydroimidazo[1,5-a]pyridin-5-yl)benzonitrile
FAD286
fadrozole
isoform-selective inhibitor binding. Fadrozole binds to aldosterone synthase in the R-configuration, using part of the active site cavity pointing toward the egress channel
ketoconazole
-
(1R)-2-[2-[(1S)-1-(4-chlorophenyl)ethyl]-3,3-dioxido-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazin-4-yl]-1-phenylethanol
-
-
(1S)-2-[2-[(1S)-1-(4-chlorophenyl)ethyl]-3,3-dioxido-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazin-4-yl]-1-phenylethanol
-
-
(5Z)-5-(1H-imidazol-5-ylmethylene)-5,6,7,8-tetrahydronaphthalene-2-carbonitrile
-
50% inhibition at 0.0069 mM, selective for CYP11B1
(R)-4-(5,6,7,8-tetrahydroimidazo[1,5-a]pyridin-5-yl)benzonitrile
FAD286, CYP11B2 inhibitor, inhibited CYP11B2 and CYP11B1 activities
1-(1H-inden-2-yl)-1H-imidazole
-
CYP11B2 IC50: 448 nM, no inhibition of CYP11B1, recombinant enzymes
1-(3,4-dihydronaphthalen-2-yl)-1H-imidazole
-
CYP11B1 IC50: 639 nM, CYP11B2 IC50: 334 nM, recombinant enzymes
1-(3-bromobenzyl)-1H-imidazole
-
-
1-(3-chlorobenzyl)-1H-imidazole
-
-
1-(3-cyanobenzyl)-1H-imidazole
-
-
1-(3-fluorobenzyl)-1H-imidazole
-
-
1-(4-aminobenzyl)-1H-imidazole
-
-
1-(4-bromobenzyl)-1H-imidazole
-
-
1-(4-bromobenzyl)-5-phenyl-1H-imidazole
-
-
1-(4-chlorobenzyl)-1H-imidazole
-
-
1-(4-chlorobenzyl)-5-phenyl-1H-imidazole
-
-
1-(4-cyanobenzyl)-1H-imidazole
-
-
1-(4-cyanobenzyl)-5-(2-fluorophenyl)-1H-imidazole
-
-
1-(4-cyanobenzyl)-5-(2-methylphenyl)-1H-imidazole
-
-
1-(4-cyanobenzyl)-5-(3-fluorophenyl)-1H-imidazole
-
-
1-(4-cyanobenzyl)-5-(3-methylphenyl)-1H-imidazole
-
-
1-(4-cyanobenzyl)-5-(4-fluorophenyl)-1H-imidazole
-
-
1-(4-cyanobenzyl)-5-(4-methylphenyl)-1H-imidazole
-
-
1-(4-cyanobenzyl)-5-(4-pyridyl)-1H-imidazole
-
-
1-(4-cyanobenzyl)-5-(methyl carboxylate)-1H-imidazole
-
-
1-(4-cyanobenzyl)-5-(methylene-acetate)-1H-imidazole
-
-
1-(4-cyanobenzyl)-5-bromo-1H-imidazole
-
-
1-(4-cyanobenzyl)-5-formyl-1H-imidazole
-
-
1-(4-cyanobenzyl)-5-hydroxymethyl-1H-imidazole
-
-
1-(4-cyanobenzyl)-5-methyl-1H-imidazole
-
-
1-(4-cyanobenzyl)-5-phenyl-1H-imidazole
-
-
1-(4-fluorobenzyl)-1H-imidazole
-
-
1-(4-fluorobenzyl)-5-phenyl-1H-imidazole
-
-
1-(4-methoxybenzyl)-5-phenyl-1H-imidazole
-
-
1-(6-methoxy-3,4-dihydronaphthalen-2-yl)-1H-imidazole
-
CYP11B1 IC50: 763 nM, CYP11B2 IC50: 411 nM, recombinant enzymes
1-benzyl-5-phenyl-1H-imidazole
-
-
2,3-dichloro-N-(pyridin-3-yl)benzamide
-
51% inhibition of CYP11B2 at 0.5 mM, no inhibition of CYP11B22
2,4,5-trifluoro-N-(pyridin-3-yl)benzamide
-
70% inhibition of CYP11B2 at 0.5 mM, no inhibition of CYP11B23
2-(4-chlorobenzyl)-4-(2-methylpropyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
-
-
2-(4-fluorobenzyl)-4-(2-methylpropyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
-
-
2-benzyl-4-(2-methylpropyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
-
-
2-fluoro-N-(pyridin-3-yl)benzamide
-
34% inhibition of CYP11B2 at 0.5 mM, no inhibition of CYP11B19
2-[(1R)-1-(4-chlorophenyl)ethyl]-4-(2-methylpropyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
-
-
2-[(1S)-1-(4-chlorophenyl)ethyl]-4-(2-methylpropyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
-
-
2-[(1S)-1-(4-chlorophenyl)ethyl]-4-(3-methoxy-2-methylpropyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
-
-
2-[(1S)-1-(4-chlorophenyl)ethyl]-4-(cyclopropylmethyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
-
-
2-[(1S)-1-(4-chlorophenyl)ethyl]-4-[(3-methyloxetan-3-yl)methyl]-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
-
-
2-[(1S)-1-(4-chlorophenyl)ethyl]-4-[(propan-2-yloxy)methyl]-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
-
-
3,4-difluoro-N-(pyridin-3-yl)benzamide
-
83% inhibition of CYP11B2 at 0.5 mM, 6% inhibition of CYP11B20
3,4-dimethoxy-N-(pyridin-3-yl)benzamide
-
-
3-(1-benzyl-1H-imidazol-5-yl)-1-propanol
-
-
3-(1-ethyl-3,4-dihydronaphthalen-2-yl)-pyridine
-
CYP11B1 IC50: 2117 nM, CYP11B2 IC50: 30 nM, recombinant enzymes
3-(1-methyl-3,4-dihydronaphthalen-2-yl)-pyridine
-
CYP11B1 IC50: 1268 nM, CYP11B2 IC50: 7 nM, recombinant enzymes
3-(1H-imidazol-1-ylmethyl)aniline
-
-
3-(3,4-dihydronaphthalen-2-yl)pyridine
-
CYP11B1 IC50: 1729 nM, CYP11B2 IC50: 7 nM, recombinant enzymes
3-(3-methyl-3,4-dihydronaphthalen-2-yl)pyridine
-
CYP11B1 IC50: 503 nM, CYP11B2 IC50: 5 nM, recombinant enzymes
3-(4-ethyl-3,4-dihydronaphthalen-2-yl)pyridine
-
CYP11B1 IC50: 1615 nM, CYP11B2 IC50: 176 nM, recombinant enzymes
3-(4-methyl-3,4-dihydronaphthalen-2-yl)pyridine
-
CYP11B1 IC50: 1291 nM, CYP11B2 IC50: 13 nM, recombinant enzymes
3-(6-methoxy-1H-inden-2-yl)pyridine
-
competitive, CYP11B1 IC50: 5684 nM, CYP11B2 IC50: 4 nM, recombinant enzymes
3-(6-methoxy-3,4-dihydronaphthalen-2-yl)pyridine
-
competitive, CYP11B1 IC50: 578 nM, CYP11B2 IC50: 2 nM, recombinant enzymes
3-(7-methoxy-3,4-dihydronaphthalen-2-yl)pyridine
-
CYP11B2 IC50: 45 nM, no inhibition of CYP11B1, recombinant enzymes
3-chloro-N-(pyridin-3-yl)benzamide
-
26% inhibition of CYP11B2 at 0.5 mM, no inhibition of CYP11B18
3-fluoro-N-(pyridin-3-yl)benzamide
-
47% inhibition of CYP11B2 at 0.5 mM, no inhibition of CYP11B17
3-[(Z)-2,3-dihydro-1H-inden-1-ylidenemethyl]pyridine
-
50% inhibition at 0.087 mM
3-[(Z)-2-phenylvinyl]pyridine
-
CYP11B1 IC50: 288 nM, CYP11B2 IC50: 735 nM, no inhibition by the 3-[(E)-2-phenylvinyl]pyridine isomer, recombinant enzymes
3-[1-(4-bromobenzyl)-1H-imidazol-5-yl]-1-propanol
-
-
3-[1-(4-chlorobenzyl)-1H-imidazol-5-yl]-1-propanol
-
-
3-[1-(4-cyanobenzyl)-1H-imidazol-5-yl]-1-propanol
-
-
3-[1-(4-fluorobenzyl)-1H-imidazol-5-yl]-1-propanol
-
-
3-[1-(4-methoxybenzyl)-1H-imidazol-5-yl]-1-propanol
-
-
3-[2-[(1S)-1-(4-chlorophenyl)ethyl]-3,3-dioxido-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazin-4-yl]-2-methylpropan-1-ol
-
-
4-((5-phenyl-1H-imidazol-1-yl)methyl)benzonitrile
-
-
4-(2-methylpropyl)-2-(thiophen-2-ylmethyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
-
-
4-(2-methylpropyl)-2-[4-(trifluoromethoxy)benzyl]-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
-
-
4-(2-methylpropyl)-2-[4-(trifluoromethyl)benzyl]-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
-
-
4-(6-methoxy-3,4-dihydronaphthalen-2-yl)pyridine
-
CYP11B1 IC50: 2529 nM, CYP11B2 IC50: 2834 nM, recombinant enzymes
4-(7-benzyl-6-oxo-5,6,7,8-tetrahydroimidazo[1,5-a]pyrazin-5-yl)benzonitrile
-
-
4-bromo-N-(pyridin-3-yl)benzamide
-
64% inhibition of CYP11B2 at 0.5 mM, no inhibition of CYP11B9
4-chloro-N-(pyridin-3-yl)benzamide
-
88% inhibition of CYP11B2 at 0.5 mM, 5% inhibition of CYP11B8
4-cyano-N-(pyridin-3-yl)benzamide
-
81% inhibition of CYP11B2 at 0.5 mM, 9% inhibition of CYP11B15
4-fluoro-N-(pyridin-3-yl)benzamide
-
86% inhibition of CYP11B2 at 0.5 mM, 7% inhibition of CYP11B7
4-methoxy-N-(pyridin-3-yl)benzamide
-
19% inhibition of CYP11B2 at 0.5 mM, no inhibition of CYP11B10
4-methyl-N-(pyridin-3-yl)benzamide
-
25% inhibition of CYP11B2 at 0.5 mM, no% inhibition of CYP11B13
4-nitro-N-(pyridin-3-yl)benzamide
-
64% inhibition of CYP11B2 at 0.5 mM, no inhibition of CYP11B16
4-[(Z)-(5-fluoro-2,3-dihydro-1H-inden-1-ylidene)methyl]pyridine
-
50% inhibition at 0.034 mM, selective for CYP11B1
5-bromo-N-(pyridin-3-yl)pyridine-3-carboxamide
-
29% inhibition of CYP11B2 at 0.5 mM, no inhibition of CYP11B5
5-[(1E)-1-(5-fluoro-2,3-dihydro-1H-inden-1-ylidene)ethyl]isoquinoline
-
50% inhibition at 0.096 mM
5-[(E)-(5-fluoro-2,3-dihydro-1H-inden-1-ylidene)methyl]isoquinoline
-
50% inhibition at 0.058 mM, selective for CYP11B1
5-[(E)-(5-fluoro-2,3-dihydro-1H-inden-1-ylidene)methyl]pyrimidine
-
50% inhibition at 0.027 mM, very selective for CYP11B1
5-[(Z)-(5-fluoro-2,3-dihydro-1H-inden-1-ylidene)methyl]isoquinoline
-
50% inhibition at 0.026 mM, selective for CYP11B1
5-[(Z)-2,3-dihydro-1H-inden-1-ylidenemethyl]-1H-imidazole
-
50% inhibition at 0.0061 mM
5-[(Z)-3,4-dihydronaphthalen-1(2H)-ylidenemethyl]-1H-imidazole
-
50% inhibition at 0.0033 mM
6,6-dimethyl-8-(pyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
6-(5,8-dihydroisoquinolin-4-yl)-3,4-dihydroquinolin-2(1H)-one
-
94% inhibition of CYP11B2 at 0.5 mM, 91% inhibition of CYP11B1
6-methoxydihydronaphthalene
-
-
8-(1H-imidazol-1-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-(2,3'-bipyridin-5-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-(5-ethoxypyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-(5-fluoropyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-(5-hydroxypyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-(5-methoxypyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-(5-phenylpyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]-quinolin-4-one
-
-
8-(isoquinolin-4-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-(pyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-(pyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinoline-4-thione
-
-
8-(pyrimidin-5-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-[5-(2,5-difluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-[5-(2-fluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-[5-(2-methoxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-[5-(3,4-difluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-[5-(3,5-difluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-[5-(3-fluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-[5-(3-hydroxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-[5-(3-methoxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-[5-(4-fluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-[5-(4-methoxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-[5-(propan-2-yloxy)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-[5-(trifluoromethyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-[5-[3-(trifluoromethoxy)phenyl]pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
8-[5-[3-(trifluoromethyl)phenyl]pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
-
9-(5-methoxypyridin-3-yl)-2,3,6,7-tetrahydro-1H,5H-pyrido[3,2,1-ij]quinolin-5-one
-
-
9-(pyridin-3-yl)-1,2,6,7-tetrahydro-5H-pyrido[ 3,2,1-ij]quinolin-3-one
-
-
9-[6-(isoquinolin-4-yl)pyridin-3-yl]-2,3,6,7-tetrahydro-1H,5H-pyrido[3,2,1-ij]quinolin-5-one
-
-
atenolol
-
potent inhibition of CYP11B2, recombinant enzyme
clotrimazole
-
azole derivative, antimycotic drug, strong dose-dependent inhibition
erythromycin
-
potent inhibition of CYP11B2, recombinant enzyme
FAD286
-
inhibitor of 11-beta-hydroxylase CYP11B1
fadrozole
ketoconazole
ketoprofene
-
potent inhibition of CYP11B2, recombinant enzyme
methyl 3-(1-benzyl-1H-imidazol-5-yl)-propanoate
-
-
methyl 3-[1-(4-bromobenzyl)-1H-imidazol-5-yl]-propanoate
-
-
methyl 3-[1-(4-chlorobenzyl)-1H-imidazol-5-yl]-propanoate
-
-
methyl 3-[1-(4-cyanobenzyl)-1H-imidazol-5-yl]-propanoate
-
-
methyl 3-[1-(4-fluorobenzyl)-1H-imidazol-5-yl]-propanoate
-
-
methyl 3-[1-(4-methoxybenzyl)-1H-imidazol-5-yl]-propanoate
-
-
Metyrapone
miconazole
-
azole derivative, antimycotic drug, strong dose-dependent inhibition
N-(pyridin-3-yl)-4-(trifluoromethoxy)benzamide
-
-
N-(pyridin-3-yl)-4-(trifluoromethyl)benzamide
-
-
N-(pyridin-3-yl)benzamide
-
30% inhibition of CYP11B2 at 0.5 mM, no inhibition of CYP11B6
N-(pyridin-3-yl)biphenyl-4-carboxamide
-
-
N-(pyridin-3-yl)pyridine-3-carboxamide
-
8% inhibition of CYP11B2 at 0.5 mM, no inhibition of CYP11B3
N-(pyridin-3-yl)pyridine-4-carboxamide
-
39% inhibition of CYP11B2 at 0.5 mM, 4% inhibition of CYP11B4
progesterone
-
progesterone acts as a competitive inhibitor for 11beta-hydroxylase and aldosterone synthase, inhibits aldosterone production by wild-type CYP11B1 and chimeric mutant CYP11B1/B2 in HEK-293 cells. The wild-type is more strongly inhibited than the chimera
R-fadrozole
-
-
S-fadrozole
-
-
spironolactone
-
diuretic and antihypertensive drug, competitive aldosterone antagonist, slight inhibition
testosterone
-
potent inhibition of CYP11B2, recombinant enzyme
[3-(1H-imidazol-1-ylmethyl)phenyl]methanol
-
-
[4-(1H-imidazol-1-ylmethyl)phenyl]methanol
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
polychlorinated biphenyl 126 induces CYP11B1 and CYP11B2 expression, 3',4'-dimethoxyflavone synergistically increases the stimulatory effects of PCB126, PCB126 has little effects on the transcription rate of both genes, but protects both RNA transcripts from degradation, mechanism of up-regulation, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18
11-deoxycorticosterone
-
pH 7.4, recombinant enzyme
0.338
11-deoxycortisol
-
pH 7.4, recombinant enzyme
0.002 - 0.0024
adrenal ferredoxin
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.85
11-deoxycorticosterone
-
pH 7.4, recombinant enzyme
0.167
11-deoxycortisol
-
pH 7.4, recombinant enzyme
1 - 1.48
adrenal ferredoxin
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000008
(R)-4-(5,6,7,8-tetrahydroimidazo[1,5-a]pyridin-5-yl)benzonitrile
competitive inhibition, pH 7.4
0.0000022
(R)-4-(5,6,7,8-tetrahydroimidazo[1,5-a]pyridin-5-yl)benzonitrile
competitive inhibition, pH 7.4, 25°C
0.0000013
6-methoxydihydronaphthalene
-
recombinant enzyme
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000016
(R)-4-(5,6,7,8-tetrahydroimidazo[1,5-a]pyridin-5-yl)benzonitrile
Homo sapiens
competitive inhibition, pH 7.4
0.0000024
(1R)-2-[2-[(1S)-1-(4-chlorophenyl)ethyl]-3,3-dioxido-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazin-4-yl]-1-phenylethanol
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000003
(1S)-2-[2-[(1S)-1-(4-chlorophenyl)ethyl]-3,3-dioxido-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazin-4-yl]-1-phenylethanol
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000099
(R)-4-(5,6,7,8-tetrahydroimidazo[1,5-a]pyridin-5-yl)benzonitrile
Homo sapiens
competitive inhibition, pH 7.4, 25°C
0.000448
1-(1H-inden-2-yl)-1H-imidazole
Homo sapiens
-
CYP11B2 IC50: 448 nM, no inhibition of CYP11B1, recombinant enzymes
0.000334 - 0.000639
1-(3,4-dihydronaphthalen-2-yl)-1H-imidazole
0.000143 - 0.000365
1-(3-bromobenzyl)-1H-imidazole
0.000151 - 0.000457
1-(3-chlorobenzyl)-1H-imidazole
0.001
1-(3-cyanobenzyl)-1H-imidazole
0.000206 - 0.000815
1-(3-fluorobenzyl)-1H-imidazole
0.000236 - 0.001
1-(4-aminobenzyl)-1H-imidazole
0.000211 - 0.000479
1-(4-bromobenzyl)-1H-imidazole
0.0000051 - 0.000007
1-(4-bromobenzyl)-5-phenyl-1H-imidazole
0.001
1-(4-chlorobenzyl)-1H-imidazole
0.0000058 - 0.000025
1-(4-chlorobenzyl)-5-phenyl-1H-imidazole
0.000368 - 0.000372
1-(4-cyanobenzyl)-1H-imidazole
0.0000023 - 0.00002
1-(4-cyanobenzyl)-5-(2-fluorophenyl)-1H-imidazole
0.0000037 - 0.0000057
1-(4-cyanobenzyl)-5-(2-methylphenyl)-1H-imidazole
0.0000055 - 0.000032
1-(4-cyanobenzyl)-5-(3-fluorophenyl)-1H-imidazole
0.0000052 - 0.0000062
1-(4-cyanobenzyl)-5-(3-methylphenyl)-1H-imidazole
0.000025 - 0.000027
1-(4-cyanobenzyl)-5-(4-fluorophenyl)-1H-imidazole
0.000117 - 0.00013
1-(4-cyanobenzyl)-5-(4-methylphenyl)-1H-imidazole
0.000307 - 0.000407
1-(4-cyanobenzyl)-5-(4-pyridyl)-1H-imidazole
0.000007 - 0.000048
1-(4-cyanobenzyl)-5-(methyl carboxylate)-1H-imidazole
0.000044 - 0.000213
1-(4-cyanobenzyl)-5-(methylene-acetate)-1H-imidazole
0.000023 - 0.000073
1-(4-cyanobenzyl)-5-bromo-1H-imidazole
0.000062 - 0.000478
1-(4-cyanobenzyl)-5-formyl-1H-imidazole
0.000029 - 0.000285
1-(4-cyanobenzyl)-5-hydroxymethyl-1H-imidazole
0.000012 - 0.000141
1-(4-cyanobenzyl)-5-methyl-1H-imidazole
0.0000017 - 0.000028
1-(4-cyanobenzyl)-5-phenyl-1H-imidazole
0.00033 - 0.001799
1-(4-fluorobenzyl)-1H-imidazole
0.000011 - 0.000016
1-(4-fluorobenzyl)-5-phenyl-1H-imidazole
0.000011 - 0.000014
1-(4-methoxybenzyl)-5-phenyl-1H-imidazole
0.000411 - 0.000763
1-(6-methoxy-3,4-dihydronaphthalen-2-yl)-1H-imidazole
0.0000048 - 0.000011
1-benzyl-5-phenyl-1H-imidazole
0.0000161 - 0.000166
2,4,5-trifluoro-N-(pyridin-3-yl)benzamide
0.0000052
2-(4-chlorobenzyl)-4-(2-methylpropyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000186
2-benzyl-4-(2-methylpropyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000094
2-[(1R)-1-(4-chlorophenyl)ethyl]-4-(2-methylpropyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000617
2-[(1S)-1-(4-chlorophenyl)ethyl]-4-(2-methylpropyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000007
2-[(1S)-1-(4-chlorophenyl)ethyl]-4-(3-methoxy-2-methylpropyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000013
2-[(1S)-1-(4-chlorophenyl)ethyl]-4-(cyclopropylmethyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000078
2-[(1S)-1-(4-chlorophenyl)ethyl]-4-[(3-methyloxetan-3-yl)methyl]-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000008
2-[(1S)-1-(4-chlorophenyl)ethyl]-4-[(propan-2-yloxy)methyl]-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000059 - 0.0000535
3,4-difluoro-N-(pyridin-3-yl)benzamide
0.000181 - 0.000286
3-(1-benzyl-1H-imidazol-5-yl)-1-propanol
0.00003 - 0.002117
3-(1-ethyl-3,4-dihydronaphthalen-2-yl)-pyridine
0.000007 - 0.001268
3-(1-methyl-3,4-dihydronaphthalen-2-yl)-pyridine
0.00039 - 0.0006
3-(1H-imidazol-1-ylmethyl)aniline
0.000007 - 0.001729
3-(3,4-dihydronaphthalen-2-yl)pyridine
0.000005 - 0.000503
3-(3-methyl-3,4-dihydronaphthalen-2-yl)pyridine
0.000176 - 0.001615
3-(4-ethyl-3,4-dihydronaphthalen-2-yl)pyridine
0.000013 - 0.001291
3-(4-methyl-3,4-dihydronaphthalen-2-yl)pyridine
0.000004 - 0.005684
3-(6-methoxy-1H-inden-2-yl)pyridine
0.000002 - 0.000578
3-(6-methoxy-3,4-dihydronaphthalen-2-yl)pyridine
0.000045
3-(7-methoxy-3,4-dihydronaphthalen-2-yl)pyridine
Homo sapiens
-
CYP11B2 IC50: 45 nM, no inhibition of CYP11B1, recombinant enzymes
0.000288 - 0.000735
3-[(Z)-2-phenylvinyl]pyridine
0.0000062 - 0.000018
3-[1-(4-bromobenzyl)-1H-imidazol-5-yl]-1-propanol
0.000044 - 0.000055
3-[1-(4-chlorobenzyl)-1H-imidazol-5-yl]-1-propanol
0.000013 - 0.000048
3-[1-(4-cyanobenzyl)-1H-imidazol-5-yl]-1-propanol
0.000016 - 0.000116
3-[1-(4-fluorobenzyl)-1H-imidazol-5-yl]-1-propanol
0.000012 - 0.000059
3-[1-(4-methoxybenzyl)-1H-imidazol-5-yl]-1-propanol
0.0000114
3-[2-[(1S)-1-(4-chlorophenyl)ethyl]-3,3-dioxido-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazin-4-yl]-2-methylpropan-1-ol
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000005 - 0.0000017
4-((5-phenyl-1H-imidazol-1-yl)methyl)benzonitrile
0.000117
4-(2-methylpropyl)-2-(thiophen-2-ylmethyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000104
4-(2-methylpropyl)-2-[4-(trifluoromethoxy)benzyl]-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000121
4-(2-methylpropyl)-2-[4-(trifluoromethyl)benzyl]-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.002529 - 0.002834
4-(6-methoxy-3,4-dihydronaphthalen-2-yl)pyridine
0.000104 - 0.000167
4-bromo-N-(pyridin-3-yl)benzamide
0.0000102 - 0.000065
4-chloro-N-(pyridin-3-yl)benzamide
0.0000075 - 0.000078
4-cyano-N-(pyridin-3-yl)benzamide
0.0000143 - 0.000082
4-fluoro-N-(pyridin-3-yl)benzamide
0.0000248 - 0.000145
4-nitro-N-(pyridin-3-yl)benzamide
0.0000002 - 0.000033
6-(5,8-dihydroisoquinolin-4-yl)-3,4-dihydroquinolin-2(1H)-one
0.000089 - 0.002077
8-(1H-imidazol-1-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.000001 - 0.000158
8-(5-ethoxypyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000044 - 0.001288
8-(5-fluoropyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000043 - 0.002045
8-(5-hydroxypyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000006 - 0.000247
8-(5-methoxypyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000013 - 0.000058
8-(5-phenylpyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]-quinolin-4-one
0.0000002 - 0.000013
8-(isoquinolin-4-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000011 - 0.000715
8-(pyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000012 - 0.000333
8-(pyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinoline-4-thione
0.000056 - 0.02855
8-(pyrimidin-5-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000036 - 0.000183
8-[5-(2,5-difluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000007 - 0.000043
8-[5-(2-fluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000024 - 0.000128
8-[5-(2-methoxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000023 - 0.000496
8-[5-(3,4-difluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.000018 - 0.001748
8-[5-(3,5-difluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000014 - 0.00049
8-[5-(3-fluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000012 - 0.000044
8-[5-(3-hydroxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000046 - 0.001374
8-[5-(3-methoxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000009 - 0.00004
8-[5-(4-fluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000014 - 0.000021
8-[5-(4-methoxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000022 - 0.000103
8-[5-(propan-2-yloxy)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000059 - 0.000141
8-[5-(trifluoromethyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.000016 - 0.002058
8-[5-[3-(trifluoromethoxy)phenyl]pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.000033 - 0.004646
8-[5-[3-(trifluoromethyl)phenyl]pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000009 - 0.000545
9-(5-methoxypyridin-3-yl)-2,3,6,7-tetrahydro-1H,5H-pyrido[3,2,1-ij]quinolin-5-one
0.0000024 - 0.002296
9-(pyridin-3-yl)-1,2,6,7-tetrahydro-5H-pyrido[ 3,2,1-ij]quinolin-3-one
0.0000002 - 0.000034
9-[6-(isoquinolin-4-yl)pyridin-3-yl]-2,3,6,7-tetrahydro-1H,5H-pyrido[3,2,1-ij]quinolin-5-one
0.000001 - 0.00001
fadrozole
0.000081 - 0.000224
ketoconazole
0.000193 - 0.000326
methyl 3-(1-benzyl-1H-imidazol-5-yl)-propanoate
0.000004 - 0.000057
methyl 3-[1-(4-bromobenzyl)-1H-imidazol-5-yl]-propanoate
0.000123 - 0.000177
methyl 3-[1-(4-chlorobenzyl)-1H-imidazol-5-yl]-propanoate
0.0000035 - 0.000031
methyl 3-[1-(4-cyanobenzyl)-1H-imidazol-5-yl]-propanoate
0.00005 - 0.000104
methyl 3-[1-(4-fluorobenzyl)-1H-imidazol-5-yl]-propanoate
0.000111 - 0.000121
methyl 3-[1-(4-methoxybenzyl)-1H-imidazol-5-yl]-propanoate
0.0000146 - 0.000072
Metyrapone
0.000006 - 0.000119
R-fadrozole
0.00004 - 0.000171
S-fadrozole
0.000206 - 0.001174
[3-(1H-imidazol-1-ylmethyl)phenyl]methanol
0.000695 - 0.001
[4-(1H-imidazol-1-ylmethyl)phenyl]methanol
0.0001
additional information
Homo sapiens
-
development and analysis of inhibitory potency of diverse inhibitors by superimposition of active and non-active compounds, modelling based on two pyridyl substituted acenaphthene derivatives, IC50 values of good inhibitors below 100 nM and of weak inhibi
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0198
-
purified recombinant enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
isolated mitochondria from human NCI-H295 adrenal cells
Manually annotated by BRENDA team
CYP11B1 expression
Manually annotated by BRENDA team
CYP11B1 expression
Manually annotated by BRENDA team
additional information
-
enzyme expression analysis
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
although the active site pocket is lined by identical residues between CYP11B isoforms, most of the divergent residues that confer additional 18-oxidase activity of aldosterone synthase are located in the I-helix, vicinity of the O2 activation path and loops around the H-helix, affecting an egress channel closure required for retaining intermediates in the active site
metabolism
human aldosterone synthase is responsible for the biosynthesis of aldosterone from 11-deoxycorticosterone in a sequential three-step reaction with two intermediates, corticosterone and 18-hydroxycorticosterone
physiological function
aldosterone synthase, CYP11B2, is the sole enzyme responsible for the production of aldosterone in humans
evolution
although the active site pocket is lined by identical residues between CYP11B isoforms, most of the divergent residues that confer additional 18-oxidase activity of aldosterone synthase are located in the I-helix, vicinity of the O2 activation path and loops around the H-helix, affecting an egress channel closure required for retaining intermediates in the active site
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
C11B2_HUMAN
503
0
57560
Swiss-Prot
Mitochondrion (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
x * 50000, recombinant His-tagged enzyme without the mitochondrial targeting sequence, SDS-PAGE, x * 55890, sequence calculation of enzyme without the mitochondrial targeting sequence but with His6-tag
55890
x * 50000, recombinant His-tagged enzyme without the mitochondrial targeting sequence, SDS-PAGE, x * 55890, sequence calculation of enzyme without the mitochondrial targeting sequence but with His6-tag
55555
-
x * 55555, calculated from full-length cDNA of 1.5 kb
55761
-
x * 55761, recombinant enzyme, mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 50000, recombinant His-tagged enzyme without the mitochondrial targeting sequence, SDS-PAGE, x * 55890, sequence calculation of enzyme without the mitochondrial targeting sequence but with His6-tag
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant N-terminally MAKKTSS-tagged and C-terminally His6-tagged CYP11B2 without mitochondrial targeting peptide complexed with substrate or inhibitor, hanging drop vapor diffusion method, 14 mg/ml protein in 50 mM potassium phosphate, pH 7.4, containing 500 mM NaCl, 0.5% CHAPS, 20% glycerol, and 0.05 mM 11-deoxycortisosterone or 0.05 mM fadrozole, mixing with reservoir solution containing 10% PEG 4000, 0.2 M lithium sulfate, and 0.1 M Tris, pH 8.5, X-ray diffraction structure determination and analysis at 2.5-2.7 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
V386A
the combination of the V386A mutation with the variant CYP11B2 173Arg only slightly reduces the 18-hydroxylase and 18-oxidase activity, whereas the V386A mutation with the CYP11B2 173Lys variant almost abolishes the 18-hydroxylation and 18-oxidation. In both cases the 11-hydroxylase activity is not affected
A165D
-
naturally occuring mutation in CYP11B1, inactive or almost inactive mutant
A1859G
-
naturally occuring polymorphisms at positions 1889 and 1859 in hypertensive patients, overview
A1889G
-
naturally occuring polymorphisms at positions 1889 and 1859 in hypertensive patients, overview
G314R/Q43R/V386A
naturally occuring mutant isolated from a patient with adrenal hyperplasia, gene structure, overview, CYP11B1 deficiency is caused by compound heterozygosity for mutation G314R of one CYP11B1 allele, and a chimeric CYP11B2/CYP11B1 in the other allele, the PSV11 beta2-beta1 chimera dioes not have 18-hydroxylase/oxidase activity, but shows 11beta-hydroxylase activity
K254_A259del
-
naturally occuring mutation in CYP11B1, inactive or almost inactive mutant
L299P
L489S
-
naturally occuring mutation from homozygous patients, non-classical congenital adrenal hyperplasia clinical phenotype, that cosegregates, with early pubic hair development and infertility, genotyping and phenotyping of a Turkish family
M88I
-
naturally occuring mutation in CYP11B1, the mutant shows 40% of wild-type activity
P159L
-
naturally occuring mutation in CYP11B1, the mutant shows 25% of wild-type activity
R366C
-
naturally occuring mutation in CYP11B1, the mutant shows 23% of wild-type activity
R383Q
-
naturally occuring mutation in CYP11B1, the mutant shows highly reduced activity and is severely involved in CYP11B1 deficiency and congenital adrenal hyperplasia
R448C
R448H
-
isolation and analysis of the narurally occuring mutation in gene CYP11B1 and mutation frequency in congenital adrenal hyperplasia in Moroccan Jews, phenotype, overview
R448H/R448C
-
isolation and analysis of the narurally occuring mutation in gene CYP11B1 and mutation frequency in congenital adrenal hyperplasia in Moroccan Jews, phenotype, overview
T401A
-
naturally occuring mutation in CYP11B1, the mutant shows 37% of wild-type activity
W116C
W116G
-
naturally occuring mutation in CYP11B1, inactive or almost inactive mutant
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged CYP11B2 from Escherichia coli by nickel affinity chromatography and anion and cation exchange chromatography
recombinant mature form of C-terminally His6-tagged CYP11B2 from Escherichia coli strain JM109 by nickel affinity and cation exchange chromatography to homogeneity
recombinant enzyme from Escherichia coli to homogeneity
-
recombinant mature form of C-terminally His6-tagged CYP11B1 from Escherichia coli strain JM109 by nickel affinity and cation exchange chromatography to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of C-terminally His6-tagged CYP11B2 mature form without the mitochondrial targeting sequence of 24 residues at the N-terminus in Escherichia coli, co-expression with the molecular chaperones GroEL and GroES
expression of mature form of CYP11B2 protein without the mitochondrial targeting peptide and with N-terminal tag MAKKTSS added to the 30th residue of CYP11B2, and with C-terminal His6-tag, coexpression with GroEL/ES in Escherichia coli strain JM109
overexpressed in V79-4 Chinese hamster lung cell line
CYP11B1 genotyping, overview. Expression of wild-type and mutant CYP11B1s in COS-7 cells
-
DNA and amino acid sequence analysis, expression analysis and regulation
-
enzyme expression analysis, expression of CYP11B1 and CYP11B2 in H295R adrenocortical cells
-
expression analysis
-
expression in Escherichia coli, coexpression with molecular chaperones GroES and GroEL
-
expression of CYP11B1 and CYP11B2 in V79 cells
-
expression of CYP11B2 in Schizosaccharomyces pombe and in V79 MZh cells
-
expression of mature form of CYP11B1 protein without the mitochondrial targeting peptide and with N-terminal tag MAKKTSS added to the 26th residue of CYP11B1, and with C-terminal His6-tag, coexpression with GroEL/ES in Escherichia coli strain JM109
expression of the different enzyme-DHFR fusion constructs in NCI-H295 cells
-
expression of wild-type CYP11B1 and of chimeric mutant CYP11B1/B2 in HEK-293 cells
-
full-length P45011B1 cDNA cloned into and expressed in lung fibroblast derived V79 Chinese hamster cells
-
gene CYP11B1 variants, DNA and amino acid sequence analysis of 512 samples from hypertensive patients, genotyping, polymorphism frequency at positions 1889 and 1859, overview
-
gene CYP11B1, DNA and aamino acid sequence determination of wild-type and mutant genes
-
gene CYP11B1, DNA and amino acid sequence determination and analysis, genotyping
-
gene CYP11B1, DNA and amino acid sequence determination and analysis, localization on chromosome 8 adjacent to gene CYP11B2, genotyping and determination of polymorphisms in 1428 samples of Caucasian families, overview
-
gene CYP11B1, DNA and amino acid sequence determination and analysis, localization on chromosome 8 adjacent to gene CYP11B2, genotyping of CwtCG and TconvGTA haplotypes
-
gene CYP11B1, DNA and amino acid sequence determination, located on chromosome 8q22
-
gene CYP11B1, located on chromosome 8q22, DNA and amino acid sequence determination of wild-type and mutant enzymes from different samples, expression in COS-7 cells
-
gene CYP11B1, maps to chromosome 8q24, DNA and amino acid sequence determination and analysis of wild-type and mutant enzymes, genotyping, the breakpoint in 3p might be a candidate region affecting variations in pheotypes of enzyme deficiency, overview
-
gene CYP11B2, located on chromosome 8q22, DAN and amino acid sequence determination, determination and analysis of the -344 polymorphism
-
genes CYP11B1 and CYP11B2, DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in COS-7 cells
overexpressed in V79-4 Chinese hamster lung cell line
stable expression of human CYP11B2 or CYP11B1 enzymes in V79 Chinese hamster cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
native very-low-density lipoprotein as well as glycoxidized VLDL, but not oxidized VLDL, mediate transcriptional upregulation of aldosterone synthase in human adrenocortical cells through multiple signaling pathways, e.g. partially through scavenger receptor class B type I. Very-low-density lipoprotein , irrespective of modification, presumably recruits PKA, ERK1/2 and Jak-2 for steroid hormone release through modulation of Cyp11B2 mRNA level
-
stimulation of enzyme expression by the renin-angiotensin system, which takes 12 h to reach full effect, and then 24 h to subside
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the enzyme is a target for development of selective and potent CYP11B2 inhibitors
medicine
blocking of aldosterone synthesis by mediating aldosterone synthase activity is a possible pharmacological therapy for hypertension
medicine
-
treatment of hyperaldosteronism, congestive heart failure, and myocardial fibrosis by lowering the elevated plasma aldosterone levels via blockade of aldosterone synthase, CYP11B2, the key enzyme of mineralocorticoid biosynthesis
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Denner, K.; Vogel, R.; Schmalix, W.; Doehmer, J.; Bernhardt, R.
Cloning and stable expression of the human mitochondrial cytochrome P45011B1 cDNA in V79 Chinese hamster cells and their application for testing of potential inhibitors
Pharmacogenetics
5
89-96
1995
Homo sapiens
Manually annotated by BRENDA team
Ulmschneider, S.; Muller-Vieira, U.; Klein, C.D.; Antes, I.; Lengauer, T.; Hartmann, R.W.
Synthesis and evaluation of (pyridylmethylene)tetrahydronaphthalenes/-indanes and structurally modified derivatives: potent and selective inhibitors of aldosterone synthase
J. Med. Chem.
48
1563-1575
2005
Homo sapiens
Manually annotated by BRENDA team
Ulmschneider, S.; Muller-Vieira, U.; Mitrenga, M.; Hartmann, R.W.; Oberwinkler-Marchais, S.; Klein, C.D.; Bureik, M.; Bernhardt, R.; Antes, I.; Lengauer, T.
Synthesis and evaluation of imidazolylmethylenetetrahydronaphthalenes and imidazolylmethyleneindanes: potent inhibitors of aldosterone synthase
J. Med. Chem.
48
1796-1805
2005
Homo sapiens
Manually annotated by BRENDA team
Ulmschneider, S.; Negri, M.; Voets, M.; Hartmann, R.W.
Development and evaluation of a pharmacophore model for inhibitors of aldosterone synthase (CYP11B2)
Bioorg. Med. Chem. Lett.
16
25-30
2006
Homo sapiens
Manually annotated by BRENDA team
Lajer, M.; Schjoedt, K.J.; Jacobsen, P.; Tarnow, L.; Parving, H.H.
Aldosterone synthase (CYP11B2) -344T/C polymorphism is not associated with the initiation and progression of diabetic nephropathy in Caucasian Type 1 diabetic patients
Diabet. Med.
23
675-680
2006
Homo sapiens
Manually annotated by BRENDA team
Lin, T.C.; Chien, S.C.; Hsu, P.C.; Li, L.A.
Mechanistic study of polychlorinated biphenyl 126-induced CYP11B1 and CYP11B2 up-regulation
Endocrinology
147
1536-1544
2006
Homo sapiens
Manually annotated by BRENDA team
Kuribayashi, I.; Nomoto, S.; Massa, G.; Oostdijk, W.; Wit, J.M.; Wolffenbuttel, B.H.; Shizuta, Y.; Honke, K.
Steroid 11-beta-hydroxylase deficiency caused by compound heterozygosity for a novel mutation, p.G314R, in one CYP11B1 allele, and a chimeric CYP11B2/CYP11B1 in the other allele
Horm. Res.
63
284-293
2005
Homo sapiens (P15538)
Manually annotated by BRENDA team
Peters, C.J.; Nugent, T.; Perry, L.A.; Davies, K.; Morel, Y.; Drake, W.M.; Savage, M.O.; Johnston, L.B.
Cosegregation of a novel homozygous CYP11B1 mutation with the phenotype of non-classical congenital adrenal hyperplasia in a consanguineous family
Horm. Res.
67
189-193
2007
Homo sapiens
Manually annotated by BRENDA team
Barr, M.; MacKenzie, S.M.; Friel, E.C.; Holloway, C.D.; Wilkinson, D.M.; Brain, N.J.; Ingram, M.C.; Fraser, R.; Brown, M.; Samani, N.J.; Caulfield, M.; Munroe, P.B.; Farrall, M.; Webster, J.; Clayton, D.; Dominiczak, A.F.; Connell, J.M.; Davies, E.
Polymorphic variation in the 11beta-hydroxylase gene associates with reduced 11-hydroxylase efficiency
Hypertension
49
113-119
2006
Homo sapiens
Manually annotated by BRENDA team
Keavney, B.; Mayosi, B.; Gaukrodger, N.; Imrie, H.; Baker, M.; Fraser, R.; Ingram, M.; Watkins, H.; Farrall, M.; Davies, E.; Connell, J.
Genetic variation at the locus encompassing 11-beta hydroxylase and aldosterone synthase accounts for heritability in cortisol precursor (11-deoxycortisol) urinary metabolite excretion
J. Clin. Endocrinol. Metab.
90
1072-1077
2005
Homo sapiens
Manually annotated by BRENDA team
Ganapathipillai, S.; Laval, G.; Hoffmann, I.S.; Castejon, A.M.; Nicod, J.; Dick, B.; Frey, F.J.; Frey, B.M.; Cubeddu, L.X.; Ferrari, P.
CYP11B2-CYP11B1 haplotypes associated with decreased 11beta-hydroxylase activity
J. Clin. Endocrinol. Metab.
90
1220-1225
2005
Homo sapiens
Manually annotated by BRENDA team
Krone, N.; Riepe, F.G.; Goetze, D.; Korsch, E.; Rister, M.; Commentz, J.; Partsch, C.J.; Groetzinger, J.; Peter, M.; Sippell, W.G.
Congenital adrenal hyperplasia due to 11-hydroxylase deficiency: functional characterization of two novel point mutations and a three-base pair deletion in the CYP11B1 gene
J. Clin. Endocrinol. Metab.
90
3724-3730
2005
Homo sapiens
Manually annotated by BRENDA team
Paperna, T.; Gershoni-Baruch, R.; Badarneh, K.; Kasinetz, L.; Hochberg, Z.
Mutations in CYP11B1 and congenital adrenal hyperplasia in Moroccan Jews
J. Clin. Endocrinol. Metab.
90
5463-5465
2005
Homo sapiens
Manually annotated by BRENDA team
Imrie, H.; Freel, M.; Mayosi, B.M.; Davies, E.; Fraser, R.; Ingram, M.; Cordell, H.J.; Farrall, M.; Avery, P.J.; Watkins, H.; Keavney, B.; Connell, J.M.
Association between aldosterone production and variation in the 11beta-hydroxylase (CYP11B1) gene
J. Clin. Endocrinol. Metab.
91
5051-5056
2006
Homo sapiens
Manually annotated by BRENDA team
Voets, M.; Antes, I.; Scherer, C.; Mueller-Vieira, U.; Biemel, K.; Marchais-Oberwinkler, S.; Hartmann, R.W.
Synthesis and evaluation of heteroaryl-substituted dihydronaphthalenes and indenes: potent and selective inhibitors of aldosterone synthase (CYP11B2) for the treatment of congestive heart failure and myocardial fibrosis
J. Med. Chem.
49
2222-2231
2006
Homo sapiens
Manually annotated by BRENDA team
Mueller-Vieira, U.; Angotti, M.; Hartmann, R.W.
The adrenocortical tumor cell line NCI-H295R as an in vitro screening system for the evaluation of CYP11B2 (aldosterone synthase) and CYP11B1 (steroid-11beta-hydroxylase) inhibitors
J. Steroid Biochem. Mol. Biol.
96
259-270
2005
Homo sapiens
Manually annotated by BRENDA team
Freel, E.M.; Ingram, M.; Wallace, A.M.; White, A.; Fraser, R.; Davies, E.; Connell, J.M.
Effect of variation in CYP11B1 and CYP11B2 on corticosteroid phenotype and hypothalamic-pituitary-adrenal axis activity in hypertensive and normotensive subjects
Clin. Endocrinol. (Oxf.)
68
700-706
2008
Homo sapiens
Manually annotated by BRENDA team
Zoellner, A.; Kagawa, N.; Waterman, M.R.; Nonaka, Y.; Takio, K.; Shiro, Y.; Hannemann, F.; Bernhardt, R.
Purification and functional characterization of human 11beta hydroxylase expressed in Escherichia coli
FEBS J.
275
799-810
2008
Homo sapiens
Manually annotated by BRENDA team
Simm, P.J.; Zacharin, M.R.
Successful pregnancy in a patient with severe 11-beta-hydroxylase deficiency and novel mutations in CYP11B1 gene
Horm. Res.
68
294-297
2007
Homo sapiens
Manually annotated by BRENDA team
Peter, M.; Janzen, N.; Sander, S.; Korsch, E.; Riepe, F.G.; Sander, J.
A case of 11beta-hydroxylase deficiency detected in a newborn screening program by second-tier LC-MS/MS
Horm. Res.
69
253-256
2008
Homo sapiens
Manually annotated by BRENDA team
Riedl, S.; Nguyen, H.H.; Clausmeyer, S.; Schulze, E.; Waldhauser, F.; Bernhardt, R.
A homozygous L299P mutation in the CYP11B1 gene leads to complete virilization in 46,XX individuals with 11-beta-hydroxylase deficiency
Horm. Res.
70
145-149
2008
Homo sapiens
Manually annotated by BRENDA team
Cingoez, S.; Ozkan, B.; Doeneray, H.; Sakizli, M.
Familial pericentric inversion chromosome 3 and R448C mutation of CYP11B1 gene in Turkish kindred with 11beta-hydroxylase deficiency
J. Endocrinol. Invest.
30
285-291
2007
Homo sapiens
Manually annotated by BRENDA team
Tonetto-Fernandes, V.; Lemos-Marini, S.H.; De Mello, M.P.; Ribeiro-Neto, L.M.; Kater, C.E.
21-hydroxylase deficiency transiently mimicking combined 21- and 11beta-hydroxylase deficiency
J. Pediatr. Endocrinol. Metab.
21
487-494
2008
Homo sapiens
Manually annotated by BRENDA team
Atabek, M.E.; Pirgon, O.; Sert, A.
Hypokalemic rhabdomyolysis in a child with 11-hydroxylase deficiency
J. Pediatr. Endocrinol. Metab.
21
93-96
2008
Homo sapiens
Manually annotated by BRENDA team
Nimkarn, S.; New, M.I.
Steroid 11beta-hydroxylase deficiency congenital adrenal hyperplasia
Trends Endocrinol. Metab.
19
96-99
2008
Homo sapiens
Manually annotated by BRENDA team
Zhao, L.Q.; Han, S.; Tian, H.M.
Progress in molecular-genetic studies on congenital adrenal hyperplasia due to 11beta-hydroxylase deficiency
World J. Pediatr.
4
85-90
2008
Homo sapiens
Manually annotated by BRENDA team
LaSala, D.; Shibanaka, Y.; Jeng, A.Y.
Coexpression of CYP11B2 or CYP11B1 with adrenodoxin and adrenodoxin reductase for assessing the potency and selectivity of aldosterone synthase inhibitors
Anal. Biochem.
394
56-61
2009
Homo sapiens (P15538), Homo sapiens (P19099), Homo sapiens
Manually annotated by BRENDA team
Adams, C.M.; Hu, C.W.; Jeng, A.Y.; Karki, R.; Ksander, G.; Lasala, D.; Leung-Chu, J.; Liang, G.; Liu, Q.; Meredith, E.; Rao, C.; Rigel, D.F.; Shi, J.; Smith, S.; Springer, C.; Zhang, C.
The discovery of potent inhibitors of aldosterone synthase that exhibit selectivity over 11-beta-hydroxylase
Bioorg. Med. Chem. Lett.
20
4324-4327
2010
Homo sapiens
Manually annotated by BRENDA team
Zimmer, C.; Hafner, M.; Zender, M.; Ammann, D.; Hartmann, R.W.; Vock, C.A.
N-(Pyridin-3-yl)benzamides as selective inhibitors of human aldosterone synthase (CYP11B2)
Bioorg. Med. Chem. Lett.
21
186-190
2011
Homo sapiens
Manually annotated by BRENDA team
Parajes, S.; Loidi, L.; Reisch, N.; Dhir, V.; Rose, I.T.; Hampel, R.; Quinkler, M.; Conway, G.S.; Castro-Feijoo, L.; Araujo-Vilar, D.; Pombo, M.; Dominguez, F.; Williams, E.L.; Cole, T.R.; Kirk, J.M.; Kaminsky, E.; Rumsby, G.; Arlt, W.; Krone, N.
Functional consequences of seven novel mutations in the CYP11B1 gene: four mutations associated with nonclassic and three mutations causing classic 11beta-hydroxylase deficiency
J. Clin. Endocrinol. Metab.
95
779-788
2010
Homo sapiens
Manually annotated by BRENDA team
Roumen, L.; Peeters, J.W.; Emmen, J.M.; Beugels, I.P.; Custers, E.M.; de Gooyer, M.; Plate, R.; Pieterse, K.; Hilbers, P.A.; Smits, J.F.; Vekemans, J.A.; Leysen, D.; Ottenheijm, H.C.; Janssen, H.M.; Hermans, J.J.
Synthesis, biological evaluation, and molecular modeling of 1-benzyl-1H-imidazoles as selective inhibitors of aldosterone synthase (CYP11B2)
J. Med. Chem.
53
1712-1725
2010
Homo sapiens
Manually annotated by BRENDA team
Lucas, S.; Negri, M.; Heim, R.; Zimmer, C.; Hartmann, R.W.
Fine-tuning the selectivity of aldosterone synthase inhibitors: structure-activity and structure-selectivity insights from studies of heteroaryl substituted 1,2,5,6-tetrahydropyrrolo[3,2,1-ij]quinolin-4-one derivatives
J. Med. Chem.
54
2307-2319
2011
Homo sapiens
Manually annotated by BRENDA team
Saha, S.; Bornstein, S.R.; Graessler, J.; Kopprasch, S.
Very-low-density lipoprotein mediates transcriptional regulation of aldosterone synthase in human adrenocortical cells through multiple signaling pathways
Cell Tissue Res.
348
71-80
2012
Homo sapiens
Manually annotated by BRENDA team
Hobler, A.; Kagawa, N.; Hutter, M.C.; Hartmann, M.F.; Wudy, S.A.; Hannemann, F.; Bernhardt, R.
Human aldosterone synthase: recombinant expression in E. coli and purification enables a detailed biochemical analysis of the protein on the molecular level
J. Steroid Biochem. Mol. Biol.
132
57-65
2012
Homo sapiens (P19099), Homo sapiens
Manually annotated by BRENDA team
Strushkevich, N.; Gilep, A.A.; Shen, L.; Arrowsmith, C.H.; Edwards, A.M.; Usanov, S.A.; Park, H.W.
Structural insights into aldosterone synthase substrate specificity and targeted inhibition
Mol. Endocrinol.
27
315-324
2013
Homo sapiens (P15538), Homo sapiens (P19099), Homo sapiens
Manually annotated by BRENDA team
Adams, B.P.; Bose, H.S.
Alteration in accumulated aldosterone synthesis as a result of N-terminal cleavage of aldosterone synthase
Mol. Pharmacol.
81
465-474
2012
Homo sapiens
Manually annotated by BRENDA team
Vecchiola, A.; Lagos, C.F.; Fuentes, C.A.; Allende, F.; Campino, C.; Valdivia, C.; Tapia-Castillo, A.; Ogishima, T.; Mukai, K.; Owen, G.; Solari, S.; Carvajal, C.A.; Fardella, C.E.
Different effects of progesterone and estradiol on chimeric and wild type aldosterone synthase in vitro
Reprod. Biol. Endocrinol.
11
76
2013
Homo sapiens
Manually annotated by BRENDA team
Neunzig, J.; Khatri, Y.; Bernhardt, R.
The impact of the clinical CYP11B2 mutation V386A strongly depends on the enzymes genetic background
Endocr. J.
64
457-461
2017
Homo sapiens (P19099), Homo sapiens
Manually annotated by BRENDA team
van Rooyen, D.; Gent, R.; Barnard, L.; Swart, A.C.
The in vitro metabolism of 11beta-hydroxyprogesterone and 11-ketoprogesterone to 11-ketodihydrotestosterone in the backdoor pathway
J. Steroid Biochem. Mol. Biol.
178
203-212
2018
Homo sapiens (P15538), Homo sapiens (P19099), Homo sapiens
Manually annotated by BRENDA team