Information on EC 1.14.15.4 - steroid 11beta-monooxygenase

New: Word Map on EC 1.14.15.4
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Opisthokonta

EC NUMBER
COMMENTARY
1.14.15.4
-
RECOMMENDED NAME
GeneOntology No.
steroid 11beta-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a steroid + 2 reduced adrenodoxin + O2 + 2 H+ = an 11beta-hydroxysteroid + 2 oxidized adrenodoxin + H2O
show the reaction diagram
superfamily of heme-containing enzyme, 11-/18-/19-hydroxylations of 11-deoxycorticosterone, 11-deoxycortisol and androstenedione
-
a steroid + 2 reduced adrenodoxin + O2 + 2 H+ = an 11beta-hydroxysteroid + 2 oxidized adrenodoxin + H2O
show the reaction diagram
one bifunctional cytochrome P-450, 11beta-/14alpha-hydroxylation
-
a steroid + 2 reduced adrenodoxin + O2 + 2 H+ = an 11beta-hydroxysteroid + 2 oxidized adrenodoxin + H2O
show the reaction diagram
cytochrome P45011beta is implicated in mineralocorticoid, synthesized and secreted from zona glomerulosa, as well as glucocorticoid, secreted primarily in zonae fasciculate and reticularis, biosynthesis with multiple catalytic activities, 11beta-/18-/19-hydroxylase and 18-/19-hydroxysteroid oxidase activities
-
a steroid + 2 reduced adrenodoxin + O2 + 2 H+ = an 11beta-hydroxysteroid + 2 oxidized adrenodoxin + H2O
show the reaction diagram
for synthesis of aldosterone 3 molecules P450 must be reduced or one molecule must be reduced 3 times
-
a steroid + 2 reduced adrenodoxin + O2 + 2 H+ = an 11beta-hydroxysteroid + 2 oxidized adrenodoxin + H2O
show the reaction diagram
P-45011beta responsible for two hydroxylase reactions
-
a steroid + 2 reduced adrenodoxin + O2 + 2 H+ = an 11beta-hydroxysteroid + 2 oxidized adrenodoxin + H2O
show the reaction diagram
single enzyme, 11beta-/18-hydroxylation and aldosterone synthetic activities
-
a steroid + 2 reduced adrenodoxin + O2 + 2 H+ = an 11beta-hydroxysteroid + 2 oxidized adrenodoxin + H2O
show the reaction diagram
11beta-/18-hydroxylation and aldosterone synthesis are catalyzed by 2 distinct forms of cytochrome P-45011beta
-
a steroid + 2 reduced adrenodoxin + O2 + 2 H+ = an 11beta-hydroxysteroid + 2 oxidized adrenodoxin + H2O
show the reaction diagram
11beta-/18-hydroxylation and aldosterone synthesis are catalyzed by 2 distinct forms of cytochrome P-45011beta
-
a steroid + 2 reduced adrenodoxin + O2 + 2 H+ = an 11beta-hydroxysteroid + 2 oxidized adrenodoxin + H2O
show the reaction diagram
A heme-thiolate protein (P-450). Also hydroxylates steroids at the 18-position, and converts 18-hydroxycorticosterone into aldosterone. Formerly EC 1.14.1.6 and 1.99.1.7
-
-
-
a steroid + 2 reduced adrenodoxin + O2 + 2 H+ = an 11beta-hydroxysteroid + 2 oxidized adrenodoxin + H2O
show the reaction diagram
2 step reduction: reduction of P-450 with non-specific donor and reduction which is specifically dependent on reduced iron-sulfur protein
-
a steroid + 2 reduced adrenodoxin + O2 + 2 H+ = an 11beta-hydroxysteroid + 2 oxidized adrenodoxin + H2O
show the reaction diagram
ferric cytochrome P-45011beta-deoxycorticosterone complex classified as a pentacoordinated species, H2O molecule binds ferric heme iron
-
a steroid + 2 reduced adrenodoxin + O2 + 2 H+ = an 11beta-hydroxysteroid + 2 oxidized adrenodoxin + H2O
show the reaction diagram
both hydroxylation activities seem to occur in a single enzyme
-
a steroid + 2 reduced adrenodoxin + O2 + 2 H+ = an 11beta-hydroxysteroid + 2 oxidized adrenodoxin + H2O
show the reaction diagram
both hydroxylation activities seem to occur in a single enzyme
-
a steroid + 2 reduced adrenodoxin + O2 + 2 H+ = an 11beta-hydroxysteroid + 2 oxidized adrenodoxin + H2O
show the reaction diagram
heme protein of so-called P-450 family
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydroxylation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glucocorticoid biosynthesis
-
-
Metabolic pathways
-
-
mineralocorticoid biosynthesis
-
-
Steroid hormone biosynthesis
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ALDOS
-
-
-
-
Aldosterone synthase
-
-
-
-
Aldosterone-synthesizing enzyme
-
-
-
-
C450XIB2
-
-
-
-
CYPXIB
-
-
-
-
CYPXIB1
-
-
-
-
CYPXIB2
-
-
-
-
CYPXIB3
-
-
-
-
P-450(11 beta,aldo)
-
-
-
-
P-450Aldo
-
-
-
-
P-450c11
-
-
-
-
P-450C18
-
-
-
-
P450(11 beta)-DS
-
-
-
-
P450C11
-
-
-
-
Steroid 11-beta-hydroxylase
-
-
-
-
steroid 11beta-hydroxylase
-
-
-
-
steroid 11beta-monooxygenase
-
-
-
-
steroid 11beta/18-hydroxylase
-
-
-
-
Steroid 18-hydroxylase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9029-66-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain IBL02
-
-
Manually annotated by BRENDA team
Absidia caerulea IBL02
strain IBL02
-
-
Manually annotated by BRENDA team
calf
-
-
Manually annotated by BRENDA team
Boedijn NRRL 2380
-
-
Manually annotated by BRENDA team
gene cyp11b, a protogynous hermaphroditic fish
UniProt
Manually annotated by BRENDA team
gene CYP11B
-
-
Manually annotated by BRENDA team
573 members of 105 British Caucasian families, genes CYP11B1 and CYP11B2
-
-
Manually annotated by BRENDA team
adult Danish Caucasian Type 1 diabetic patients with diabetic nephropathy
-
-
Manually annotated by BRENDA team
British hypertensive patients
-
-
Manually annotated by BRENDA team
cytochrome P450 11B1, mitochondrial precursor
SwissProt
Manually annotated by BRENDA team
gene CYP11B1
-
-
Manually annotated by BRENDA team
gene CYP11B1, a consanguineous Turkish family
-
-
Manually annotated by BRENDA team
Moroccan Jews
-
-
Manually annotated by BRENDA team
sole protogynous freshwater fish found that exhibits an adult sex change from functional females to males
UniProt
Manually annotated by BRENDA team
male Wistar
-
-
Manually annotated by BRENDA team
male Wistar Kyoto rats
-
-
Manually annotated by BRENDA team
male Wistar rats with heart failure induced by coronary artery ligation and sham-operated controls, stroke-prone spontaneously hypertensive rats and Wistar Kyoto rats as controls, cyp1a1Ren-2 transgenic rats and Fischer controls, and adult Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
male, Sprague-Dawley, low sodium, high potassium treated
-
-
Manually annotated by BRENDA team
male, Zur:SIV low sodium, high potassium or high sodium, low potassium treated for stimulation or supprssion, respectively
-
-
Manually annotated by BRENDA team
Milan hypertensive and normotensive rats
-
-
Manually annotated by BRENDA team
neonatal and adult
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
malfunction
-
familial hyperaldosteronism type I is caused by the unequal recombination between the 11beta-hydroxylase CYP11B1 and aldosterone synthase CYP11B2 genes, resulting in the generation of a CYP11B1/B2 chimeric gene and abnormal adrenal aldosterone production, which leads to severe hypertension and an elevated frequency of stroke at a young age
malfunction
-
overproduction of aldosterone in the adrenal gland can lead to hypertension, a major cause of heart disease and stroke
metabolism
-
aldosterone synthase, CYP11B2, is the key enzyme of mineralocorticoid biosynthesis and its malfunction is involved in hyperaldosteronism, congestive heart failure, and myocardial fibrosis
metabolism
-
CYP11B1 is a key enzyme in the biosynthesis of cortisol. CYP11B2 catalyzes the last three steps of aldosterone biosynthesis
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
-
steroid 11beta-hydroxylase converts 11-deoxycortisol and 11-deoxycorticosterone to cortisol and corticosterone, respectively
physiological function
-
aldosterone synthase regulates blood volume by synthesizing the mineralocorticoid aldosterone. Subcellular mechanisms of enzyme localization relate to production of aldosterone and reveal a rapid, promoter-independent regulation of aldosterone production
physiological function
-
aldosterone synthase, CYP11B2, is the sole enzyme responsible for the production of aldosterone in humans
physiological function
-
progesterone might regulate the 11beta-hydroxylase CYP11B1 and aldosterone synthase CYP11B2 enzymatic activities and contribute to the decay of aldosterone synthase activity in CYP11B1/B2 chimeric gene-positive patients. This regulatory mechanism of progesterone action might be involved in protecting pregnant women with FH-1 against hypertension
metabolism
-
very-low-density lipoprotein mediates transcriptional upregulation of aldosterone synthase in human adrenocortical cells through multiple signaling pathways, e.g. partially through scavenger receptor class B type I. Aldosterone, apart from its role in fluid and electrolyte homeostasis, is implicated in insulin resistance and myocardial fibrosis. Impact of VLDL as a potential risk factor for aldosterone-mediated cardiovascular injury in diabetes mellitus, intracellular mechanism, overview
additional information
-
steroid 11beta-hydroxylase, CYP11B1, deficiency, i.e. 11OHD, is the second most common form of congenital adrenal hyperplasia. Cases of nonclassic 11OHD are rare compared with the incidence of nonclassic 21-hydroxylase deficiency, genotypes and phenotypes, overview
additional information
-
a hydrophobic cavity with specific features is associated with corticosteroid recognition, substrate binding mode, overview
additional information
-
homology modeling and molecular docking of CYP11B2, overview
additional information
-
molecular modelling of CYP11B1 and CYP11B1/B2 chimeric proteins and steroids docking, overview
additional information
-
N-terminal 26 amino acids of the enzyme target cargo protein DHFR to the mitochondria
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
11-deoxy-cortisol + reduced ferredoxin + O2
cortisol + ferredoxin + H2O
show the reaction diagram
-
-
-
-
?
11-deoxycorticosterone + adrenal ferredoxin + H2O
corticosterone + reduced adrenal ferredoxin + O2
show the reaction diagram
-
-
-
-
?
11-deoxycorticosterone + NADPH + O2
18-hydroxycorticosterone + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + 2 H+ + 2 O2
aldosterone + oxidized adrenal ferredoxin + 2 H2O
show the reaction diagram
-
-
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + 2 H+ + 2 O2
aldosterone + oxidized adrenal ferredoxin + 2 H2O
show the reaction diagram
-
supported by adrenodoxin and adrenodoxin reductase, 3 step-hydroxylation with corticosterone and 18-hydroxycorticosterone as intermediates, 11beta-/18-hydroxylase
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + 2 H+ + 2 O2
aldosterone + oxidized adrenal ferredoxin + 2 H2O
show the reaction diagram
-
11beta-hydroxylase and 18-hydroxylase activities, after replacement of Tween 20 by phosphatidylcholine catalytic activity for aldosterone activity is exhibited, form 1 higher active in aldosterone and 18-hydroxycorticosterone production and less active in the production of corticosterone and 18-hydroxydeoxycorticosterone from deoxycorticosterone as form 2
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + 2 H+ + 2 O2
aldosterone + oxidized adrenal ferredoxin + 2 H2O
show the reaction diagram
-
49 kDa protein, exclusively in zona glomerulosa, 11beta -hydroxylation, as well as 18-hydroxylation and 18-hydroxydehydrogenation of corticosterone with 18-hydroxydeoxycorticosterone and 18-hydroxycorticosterone as intermediates
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + 2 H+ + 2 O2
aldosterone + oxidized adrenal ferredoxin + 2 H2O
show the reaction diagram
-
49 kDa protein, exclusively in zona glomerulosa, 11beta -hydroxylation, as well as 18-hydroxylation and 18-hydroxydehydrogenation of corticosterone with 18-hydroxydeoxycorticosterone and 18-hydroxycorticosterone as intermediates, 51 kDa protein, zona fasciculata and glomerulosa, high sodium and low potassium, 11beta-/18-hydroxylation
product of 49 kDa protein
?
11-deoxycorticosterone + reduced adrenal ferredoxin + 2 H+ + 2 O2
aldosterone + oxidized adrenal ferredoxin + 2 H2O
show the reaction diagram
-
11beta-/18-hydroxylation
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + 2 H+ + 2 O2
aldosterone + oxidized adrenal ferredoxin + 2 H2O
show the reaction diagram
-
3 steps in glomerulosa catalysed by one enzyme, 11beta-hydroxylation to corticosterone, 18-hydroxylation to 18-hydroxycorticosterone and aldehyde synthesis to aldosterone
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + 2 H+ + 2 O2
aldosterone + oxidized adrenal ferredoxin + 2 H2O
show the reaction diagram
-
3 step 11beta-/18-hydroxylation to aldosterone
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + 2 H+ + 2 O2
aldosterone + oxidized adrenal ferredoxin + 2 H2O
show the reaction diagram
-
by 49.5 kDa protein from capsular portion, 11beta-/18-hydroxylation by 51.5 kDa protein
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
by 49.5 kDa protein from capsular portion, 11beta-/18-hydroxylation by 51.5 kDa protein
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
18-/11beta-hydroxylation
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
containing adrenal ferredoxin, adrenal ferredoxin reductase and P-45011beta, highly active hydroxylation, 11beta-/18-hydroxylase activity
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
by 49.5 kDa protein from capsular portion, 11beta-/18-hydroxylation by 51.5 kDa protein
51.5 kDa protein
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
18-/11beta-hydroxylation
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
containing adrenal ferredoxin, adrenal ferredoxin reductase and P-45011beta, highly active hydroxylation, 11beta-/18-hydroxylase activity
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
11beta-hydroxylation
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
11beta-hydroxylation
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
11beta-hydroxylation
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
11beta-hydroxylation
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
11beta-hydroxylation
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
11beta-hydroxylation
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
adrenal
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
addition of adrenodoxin and adrenodoxin reductase
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
addition of adrenodoxin and adrenodoxin reductase
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
11beta-hydroxylation, last 3 steps of pathway for aldosterone biosynthesis
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
?
show the reaction diagram
P15538, P19099
-
-
-
?
11-deoxycorticosterone + reduced adrenodoxin + O2
corticosterone + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
11-deoxycorticosterone + reduced adrenodoxin + O2
corticosterone + oxidized adrenodoxin + H2O
show the reaction diagram
-
i.e. 21-hydroxyprogesterone
-
-
?
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 + reduced adrenal ferredoxin + O2
cortisol + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
11beta-hydroxylation
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
cytochrome P-45011beta-linked monoxygenase
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
11beta-hydroxylase activity
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
14alpha-hydroxy-11-deoxycortisol + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
11alpha-hydroxylase activity
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + adrenal ferredoxin + H2O
show the reaction diagram
-
-
-
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + adrenal ferredoxin + H2O
show the reaction diagram
P15538
-
-
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + adrenal ferredoxin + H2O
show the reaction diagram
-
CYP11B1
-
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + adrenal ferredoxin + H2O
show the reaction diagram
P15538, P19099
CYP11B1
-
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + adrenal ferredoxin + H2O
show the reaction diagram
-
deficiency of steroid 11-hydroxylase CYP11B1 due to mutations in the CYP11B1 gene causes congenital adrenal hyperplasia, a group of autosomal recessive disorders, overview
-
-
?
11-deoxycortisol + reduced adrenodoxin + O2
cortisol + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
16,17alpha-epoxyprogesterone + reduced adrenal ferredoxin + O2
11beta-hydroxy-16,17alpha-epoxyprogesterone + adrenal ferredoxin + H2O
show the reaction diagram
-
-
the product is an important intermediate for many anti-inflammatory drugs
-
?
16,17alpha-epoxyprogesterone + reduced adrenal ferredoxin + O2
11beta-hydroxy-16,17alpha-epoxyprogesterone + adrenal ferredoxin + H2O
show the reaction diagram
-
assay optimization
-
-
?
16,17alpha-epoxyprogesterone + reduced adrenal ferredoxin + O2
11beta-hydroxy-16,17alpha-epoxyprogesterone + adrenal ferredoxin + H2O
show the reaction diagram
Absidia caerulea IBL02
-
-
the product is an important intermediate for many anti-inflammatory drugs
-
?
16,17alpha-epoxyprogesterone + reduced adrenal ferredoxin + O2
11beta-hydroxy-16,17alpha-epoxyprogesterone + adrenal ferredoxin + H2O
show the reaction diagram
Absidia caerulea IBL02
-
assay optimization
-
-
?
17alpha,21-dihydroxy-pregn-4-ene-3,20-dione + reduced adrenal ferredoxin + O2
11beta,17alpha,21-trihydroxy-pregn-4-ene-3,20-dione + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
i.e. Reichstein's compound, inducer
hydrocortisone, 60%, 11beta hydroxylation
?
17alpha,21-dihydroxy-pregn-4-ene-3,20-dione + reduced adrenal ferredoxin + O2
14alpha,17alpha,21-trihydroxy-pregn-4-ene-3,20-dione + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
i.e. Reichstein's compound, inducer
25%, 14alpha hydroxylation
?
18-hydroxy-corticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
18-hydroxylation, last 3 steps of pathway for aldosterone biosynthesis
-
?
18-hydroxycorticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
-
-
?
18-hydroxycorticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
-
18-hydroxylation
?
18-hydroxycorticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
-
18-hydroxylation, aldosterone production exclusively in the zona glomerulosa
?
18-hydroxycorticosterone + reduced adrenal ferredoxin + O2
aldosterone + adrenal ferredoxin + H2O
show the reaction diagram
-
-
-
-
?
18-hydroxycorticosterone + reduced adrenal ferredoxin + O2
aldosterone + adrenal ferredoxin + H2O
show the reaction diagram
P15538
-
-
-
?
18-hydroxycorticosterone + reduced adrenal ferredoxin + O2
aldosterone + adrenal ferredoxin + H2O
show the reaction diagram
-
CYP11B2
-
-
?
18-hydroxycorticosterone + reduced adrenodoxin + O2
aldosterone + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
18-hydroxycorticosterone + reduced ferredoxin + O2
aldosterone + ferredoxin + H2O
show the reaction diagram
-
-
-
-
?
18-hydroxycorticosterone + reduced ferredoxin + O2
aldosterone + 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
-
-
?
19-hydroxy-11-deoxycorticosterone + reduced adrenal ferredoxin + O2
19-oxo-11-deoxycorticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
-
-
?
4-androstene-3,17-dione + reduced adrenal ferredoxin + O2
11beta-hydroxy-4-androstene-3,17-dione + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
i.e. testosterone, 11beta-/19-hydroxylase activity, good sustrate
-
?
4-androstene-3,17-dione + reduced adrenal ferredoxin + O2
19-hydroxy-4-androstene-3,17-dione + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
i.e. testosterone, 11beta-/19-hydroxylase activity, good sustrate
-
?
4-pregnen-21-ol-3,20-dione + reduced adrenal ferredoxin + O2
4-pregnene-11,21-diol-3,20-dione + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
11-deoxycorticosterone, fumarate required in mitochondria treated with hypotonic solutions of electrolytes
-
-
-
4-pregnen-21-ol-3,20-dione + reduced adrenal ferredoxin + O2
4-pregnene-11,21-diol-3,20-dione + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
11-hydroxylation
-
?
4-pregnene-17,21-diol-3,20-dione + reduced adrenal ferredoxin + O2
4-pregnene-11,17,21-triol-3,20-dione + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
11-hydroxylation
-
?
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, low activity with isozyme CYP11B2
-
-
?
corticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
18-hydroxylation
-
?
corticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
18-hydroxycorticosterone as intermediate of 11beta-hydroxylation
-
?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
addition of adrenodoxin and adrenodoxin reductase
-
?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
18-hydroxylation
-
?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
18-hydroxylation
-
?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxy-11-deoxycorticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
addition of adrenodoxin and adrenodoxin reductase
-
?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxy-corticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
18-hydroxylation, last 3 steps of pathway for aldosterone biosynthesis
-
?
corticosterone + reduced adrenal ferredoxin + O2
11-deoxycorticosterone + adrenal ferredoxin + H2O
show the reaction diagram
-
-
-
-
?
corticosterone + reduced adrenal ferredoxin + O2
11-deoxycorticosterone + adrenal ferredoxin + H2O
show the reaction diagram
A1XRK1
-
-
-
?
corticosterone + reduced adrenodoxin + O2
18-hydroxycorticosterone + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
cortisol + reduced adrenal ferredoxin + O2
cortisone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
-
-
?
cortisol + reduced adrenal ferredoxin + O2
11-deoxycortisol + adrenal ferredoxin + H2O
show the reaction diagram
-
in the adrenal zona fasciculata
-
-
?
progesterone + reduced adrenodoxin + O2
11beta-hydroxyprogesterone + oxidized adrenodoxin + H2O
show the reaction diagram
-
low activity with isozyme CYP11B1, low activity with isozyme CYP11B2
-
-
?
testosterone + reduced adrenal ferredoxin + O2
11beta-hydroxytestosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
at low rate
-
-
?
testosterone + reduced adrenodoxin + O2
11-hydroxytestosterone + oxidized adrenodoxin + H2O
show the reaction diagram
-
low activity with isozyme CYP11B1, low activity with isozyme CYP11B2
-
-
?
metyrapone + ?
metyrapol + ?
show the reaction diagram
-
plasma, product-stereoselective reductive metabolism
enantiomers
r
additional information
?
-
-
corticosterone generally believed to be preferred substrate for 18-hydroxylase
-
-
-
additional information
?
-
-
corticosterone normal substrate in vivo
-
-
-
additional information
?
-
-
androgen production of male animal is partially regulated by changes in abundance of enzyme mRNA
-
-
-
additional information
?
-
-
-344T/C polymorphism is associated with a clinically relevant phenotype for diabetic nephropathy such as hypertension
-
-
-
additional information
?
-
-
CYP11B2-CYP11B1 haplotypes associate with decreased 11beta-hydroxylase activity, overview
-
-
-
additional information
?
-
-
effects of enzyme inhibition of steroid biosynthesis and mineralcorticoid formation, overview
-
-
-
additional information
?
-
-
enzyme deficiency is a cause for congenital adrenal hyperplasia, overview
-
-
-
additional information
?
-
-
genetic variation at the locus encompassing 11-beta hydroxylase and aldosterone synthase accounts for heritability in cortisol precursor 11-deoxycortisol urinary metabolite excretion, overview
-
-
-
additional information
?
-
-
non-classical enzyme deficiency causes mild androgen excess, hirsutism, precocious adrenarche and accelerated growth in children, missense mutations are responsible for non-classical adrenal hyperplasia in children, overview
-
-
-
additional information
?
-
-
variation of 344 C/T and intron 2 in the CYP11B2 gene, encoding aldosterone synthase, is associated with CYP11B1 deficiency due to variations of gene CYP11B1 at positions 1889 and 1859 and disequiliibrium with CYP11B2, overview
-
-
-
additional information
?
-
-
11-beta-hydroxylase deficiency, i.e. 11betaOHD is caused by CYP11B1 gene defects and leads to congenital adrenal hyperplasia associated with hypertension, overview
-
-
-
additional information
?
-
-
11beta-hydroxylase deficiency is the second most common form of congenital adrenal hyperplasia after 21-hydroxylase deficiency, overview
-
-
-
additional information
?
-
-
a key mitochondrial enzyme for the production of 11-oxygenated androgens, which have been shown to be potent masculinising steroids in several fish species, it plays a role in testicular development
-
-
-
additional information
?
-
-
congenital adrenal hyperplasia due to steroid 11beta-hydroxylase deficiency is a genetic disorder of steroidogenesis, transmitted as an autosomal recessive trait. It is associated with low renin hypertension, hypokalemia, hyperandrogenemia and genital ambiguity in affected females, overview
-
-
-
additional information
?
-
-
deficiency of 11beta-hydroxylase results in decreased synthesis of cortisol and glucocorticoids, and thus causes weakened depressive feedback ofACTH and increased synthesis of ACTH in pituitary, which leads to production of more cortisol precursor in zona fasciculata, enzyme regulation, overview
-
-
-
additional information
?
-
-
enzyme deficiency leads to hypokalemia and further, when under-treated, to rhabdomyolysis, overview
-
-
-
additional information
?
-
A1XRK1
the enzyme is involved in gonadal transformation in the zebrafish, enzyme expression regulation, overview
-
-
-
additional information
?
-
-
the enzyme is involved in sex differentiation in the protandrous anemonefish, overview
-
-
-
additional information
?
-
-
the ezyme is regulated by adrenocorticotrophic hormone, ACTH
-
-
-
additional information
?
-
-
the polymorphism genotype of gene CYP11B2, encoding aldosterone synthase, affects the activity of the 11beta-hydroxylase, encoded by gene CYP11B1, overview
-
-
-
additional information
?
-
-
the recombinant enzyme is capable of hydroxylating its substrates at position 11-beta
-
-
-
additional information
?
-
P15538, P19099
enzyme is responsible for the final step of aldosterone synthesis. It requires electron transfer from the adrenodoxin/adrenodoxin reductase system to catalyze the production of aldosterone
-
-
-
additional information
?
-
-
prolactin regulatory element-binding (PREB) protein. It regulates the transcription of the CYP11B1 gene via cAMP. PREB can function as a transcriptional regulator of the CYP11B1 promoter. PREB binds to the CYP11B1 promoter, and in cells expressing PREB, it increases CYP11B1 expression. Knockdown of PREB expression attenuated the effects of cAMP on CYP11B1 expression. CYP11B1 promoter activity is increased in the cells treated with the scrambled siRNA and cAMP, while the CYP11B1 promoter activity is markedly reduced in the cells treated with the PREB-specific siRNA. Enzyme is regulated by cAMP, which stimulates the expression of PREB. Knockdown of PREB expression attenuates the effects of cAMP on CYP11B1 expression, responsible for the last step of glucocorticoid biosynthesis in the adrenal cortices of many kinds of animals
-
-
-
additional information
?
-
Q2I128
the concomitant down-regulation of P450arom and up-regulation of P45011beta are of pivotal importance to the sex change
-
-
-
additional information
?
-
-
CYP11B2 hydroxylates 18-hydroxycorticosterone
-
-
-
additional information
?
-
-
steroid 11beta-hydroxylase converts 11-deoxycortisol and 11-deoxycorticosterone to cortisol and corticosterone, respectively
-
-
-
additional information
?
-
-
bifunctional enzyme catalyzing the biosynthesis of aldosterone by successive 11beta- and 18-hydroxylation followed by an 18-oxidation of 11-deoxycorticosterone
-
-
-
additional information
?
-
-
N-terminally unprocessed enzyme has 2fold more activity than the mature physiological enzyme
-
-
-
additional information
?
-
-
aldosterone synthase shows high 11beta-hydroxylase activity toward both gluco- and mineralocorticoid formation, and additional 18-oxidase activity, substrate specificties of isozymes CYP11B2 and CYP11B1, overview. No oxidation activity of CYP11B2 with 18-hydroxycorticosterone, 11-dehydrocorticosterone, 21-hydroxypregnenolone, and poor activity with cortisol, substrate specificties of isozymes CYP11B2 and CYP11B1, overview. No or poor activity of CYP11B1 with cortisol, 18-hydroxycorticosterone, 11-dehydrocorticosterone, 21-hydroxypregnenolone, and 11beta-hydroxyprogesterone
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
11-deoxy-cortisol + reduced ferredoxin + O2
cortisol + ferredoxin + H2O
show the reaction diagram
-
-
-
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
11beta-hydroxylation, last 3 steps of pathway for aldosterone biosynthesis
-
?
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 + adrenal ferredoxin + H2O
show the reaction diagram
-
-
-
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + adrenal ferredoxin + H2O
show the reaction diagram
P15538
-
-
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + adrenal ferredoxin + H2O
show the reaction diagram
-
CYP11B1
-
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + adrenal ferredoxin + H2O
show the reaction diagram
-
deficiency of steroid 11-hydroxylase CYP11B1 due to mutations in the CYP11B1 gene causes congenital adrenal hyperplasia, a group of autosomal recessive disorders, overview
-
-
?
16,17alpha-epoxyprogesterone + reduced adrenal ferredoxin + O2
11beta-hydroxy-16,17alpha-epoxyprogesterone + adrenal ferredoxin + H2O
show the reaction diagram
Absidia caerulea, Absidia caerulea IBL02
-
-
the product is an important intermediate for many anti-inflammatory drugs
-
?
18-hydroxy-corticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
18-hydroxylation, last 3 steps of pathway for aldosterone biosynthesis
-
?
18-hydroxycorticosterone + reduced adrenal ferredoxin + O2
aldosterone + adrenal ferredoxin + H2O
show the reaction diagram
-
-
-
-
?
18-hydroxycorticosterone + reduced adrenal ferredoxin + O2
aldosterone + adrenal ferredoxin + H2O
show the reaction diagram
P15538
-
-
-
?
18-hydroxycorticosterone + reduced adrenal ferredoxin + O2
aldosterone + adrenal ferredoxin + H2O
show the reaction diagram
-
CYP11B2
-
-
?
18-hydroxycorticosterone + reduced adrenodoxin + O2
aldosterone + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
18-hydroxycorticosterone + reduced ferredoxin + O2
aldosterone + 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
18-hydroxy-corticosterone + oxidized adrenal ferredoxin + H2O
show the reaction diagram
-
18-hydroxylation, last 3 steps of pathway for aldosterone biosynthesis
-
?
corticosterone + reduced adrenal ferredoxin + O2
11-deoxycorticosterone + adrenal ferredoxin + H2O
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 + H2O
show the reaction diagram
-
in the adrenal zona fasciculata
-
-
?
additional information
?
-
-
corticosterone generally believed to be preferred substrate for 18-hydroxylase
-
-
-
additional information
?
-
-
corticosterone normal substrate in vivo
-
-
-
additional information
?
-
-
androgen production of male animal is partially regulated by changes in abundance of enzyme mRNA
-
-
-
additional information
?
-
-
-344T/C polymorphism is associated with a clinically relevant phenotype for diabetic nephropathy such as hypertension
-
-
-
additional information
?
-
-
CYP11B2-CYP11B1 haplotypes associate with decreased 11beta-hydroxylase activity, overview
-
-
-
additional information
?
-
-
effects of enzyme inhibition of steroid biosynthesis and mineralcorticoid formation, overview
-
-
-
additional information
?
-
-
enzyme deficiency is a cause for congenital adrenal hyperplasia, overview
-
-
-
additional information
?
-
-
genetic variation at the locus encompassing 11-beta hydroxylase and aldosterone synthase accounts for heritability in cortisol precursor 11-deoxycortisol urinary metabolite excretion, overview
-
-
-
additional information
?
-
-
non-classical enzyme deficiency causes mild androgen excess, hirsutism, precocious adrenarche and accelerated growth in children, missense mutations are responsible for non-classical adrenal hyperplasia in children, overview
-
-
-
additional information
?
-
-
variation of 344 C/T and intron 2 in the CYP11B2 gene, encoding aldosterone synthase, is associated with CYP11B1 deficiency due to variations of gene CYP11B1 at positions 1889 and 1859 and disequiliibrium with CYP11B2, overview
-
-
-
additional information
?
-
-
11-beta-hydroxylase deficiency, i.e. 11betaOHD is caused by CYP11B1 gene defects and leads to congenital adrenal hyperplasia associated with hypertension, overview
-
-
-
additional information
?
-
-
11beta-hydroxylase deficiency is the second most common form of congenital adrenal hyperplasia after 21-hydroxylase deficiency, overview
-
-
-
additional information
?
-
-
a key mitochondrial enzyme for the production of 11-oxygenated androgens, which have been shown to be potent masculinising steroids in several fish species, it plays a role in testicular development
-
-
-
additional information
?
-
-
congenital adrenal hyperplasia due to steroid 11beta-hydroxylase deficiency is a genetic disorder of steroidogenesis, transmitted as an autosomal recessive trait. It is associated with low renin hypertension, hypokalemia, hyperandrogenemia and genital ambiguity in affected females, overview
-
-
-
additional information
?
-
-
deficiency of 11beta-hydroxylase results in decreased synthesis of cortisol and glucocorticoids, and thus causes weakened depressive feedback ofACTH and increased synthesis of ACTH in pituitary, which leads to production of more cortisol precursor in zona fasciculata, enzyme regulation, overview
-
-
-
additional information
?
-
-
enzyme deficiency leads to hypokalemia and further, when under-treated, to rhabdomyolysis, overview
-
-
-
additional information
?
-
A1XRK1
the enzyme is involved in gonadal transformation in the zebrafish, enzyme expression regulation, overview
-
-
-
additional information
?
-
-
the enzyme is involved in sex differentiation in the protandrous anemonefish, overview
-
-
-
additional information
?
-
-
the ezyme is regulated by adrenocorticotrophic hormone, ACTH
-
-
-
additional information
?
-
-
the polymorphism genotype of gene CYP11B2, encoding aldosterone synthase, affects the activity of the 11beta-hydroxylase, encoded by gene CYP11B1, overview
-
-
-
additional information
?
-
P15538, P19099
enzyme is responsible for the final step of aldosterone synthesis. It requires electron transfer from the adrenodoxin/adrenodoxin reductase system to catalyze the production of aldosterone
-
-
-
additional information
?
-
-
prolactin regulatory element-binding (PREB) protein. It regulates the transcription of the CYP11B1 gene via cAMP. PREB can function as a transcriptional regulator of the CYP11B1 promoter. PREB binds to the CYP11B1 promoter, and in cells expressing PREB, it increases CYP11B1 expression. Knockdown of PREB expression attenuated the effects of cAMP on CYP11B1 expression. CYP11B1 promoter activity is increased in the cells treated with the scrambled siRNA and cAMP, while the CYP11B1 promoter activity is markedly reduced in the cells treated with the PREB-specific siRNA. Enzyme is regulated by cAMP, which stimulates the expression of PREB. Knockdown of PREB expression attenuates the effects of cAMP on CYP11B1 expression, responsible for the last step of glucocorticoid biosynthesis in the adrenal cortices of many kinds of animals
-
-
-
additional information
?
-
Q2I128
the concomitant down-regulation of P450arom and up-regulation of P45011beta are of pivotal importance to the sex change
-
-
-
additional information
?
-
-
CYP11B2 hydroxylates 18-hydroxycorticosterone
-
-
-
additional information
?
-
-
steroid 11beta-hydroxylase converts 11-deoxycortisol and 11-deoxycorticosterone to cortisol and corticosterone, respectively
-
-
-
additional information
?
-
-
bifunctional enzyme catalyzing the biosynthesis of aldosterone by successive 11beta- and 18-hydroxylation followed by an 18-oxidation of 11-deoxycorticosterone
-
-
-
additional information
?
-
-
N-terminally unprocessed enzyme has 2fold more activity than the mature physiological enzyme
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adrenodoxin
-
;
-
adrenodoxin
-
-
-
ascorbate
-
plus NADH very low conversion and no aldosterone production, in synergism with NADH, malate and NADP+ increase of aldosterone synthetase activity in zona glomerulosa, not zona fasciculate
Ferredoxin
-
-
-
Ferredoxin
-
-
-
NADH
-
less effective than NADPH
NADH
-
-
NADP+
-
plus malate supports all 4 conversions, increase of aldosterone synthetase activity
NADPH
-
no reaction with NADH or NADP+
NADPH
-
-
NADPH
-
adrenodoxin and NADPH-linked adrenodoxin reductase; requirement during inactivation
NADPH
-
adrenodoxin and NADPH-linked adrenodoxin reductase
NADPH
-
adrenodoxin and adrenodoxin reductase required in cell line homogenates, in living cells in absence of cofactors
NADPH
-
NADPH-linked cytochrome P-450 reductase
reduced adrenal ferredoxin
A1XRK1
-
reduced adrenal ferredoxin
-
-
Ferredoxin
-
[2Fe-2S] ferredoxin
-
additional information
-
cofactor screening, overview, the enzyme is active with NADPH
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
highly activating
Fe2+
-
heme iron
Fe2+
-
highly activating
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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; 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
-
-
11beta-hydroxy-dehydroepiandrosterone
-
50% inhibition at 0.0033 mM
11beta-hydroxy-progesterone
-
50% inhibition at 0.0004 mM
11beta-hydroxy-testosterone
-
50% inhibition at 0.0017 mM
18-ethynylprogesterone
-
mechanism-based inhibition; weaker than 18-vinylprogesterone, inhibitor of aldosterone synthesis for both activities, stronger for 18-hydroxylation inhibition
18-ethynylprogesterone
-
mechanism-based inhibition; progesterone analog, time-dependent pseudo-first-order inactivation, concentration dependent
18-ethynylprogesterone
-
suicide-substrate of aldosterone biosythesis, inhibits more strongly the 18-hydroxylation step
18-vinyldeoxycorticosterone
-
deoxycorticosterone analog, very strong and reversible inhibitor for deoxycorticosterone and corticosterone oxidation, 0.001 mM leads to decrease in corticosterone production with 30% of total activity after 1 min, 100fold more efficient than 18-vinylprogesterone for inhibition of 11beta-hydroxylation step, only 6fold of more inhibition of 18-hydroxylation step
18-vinylprogesterone
-
competitive, potent inhibitor of aldosterone synthesis for both activities, 18-hydroxylation more effected, 65% inhibition of corticosterone and 11-deoxy-18-hydroxycorticosterone production by 0.03 mM; mechanism-based inhibition
18-vinylprogesterone
-
mechanism-based inhibition; progesterone analog, with NADPH, time and concentration dependent, irreversible, pseudo-first-order process, covalent binding to and destruction of prosthetic heme group, 5fold more effective than its acetylenic analog 18-ethynylprogesterone
18-vinylprogesterone
-
with 0.001 mM no inhibition detectable, with 0.01 mM 23% decrease in corticosterone production, better suicide-substrate of aldosterone biosythesis than 18-ethynylprogesterone, inhibits more strongly the 18-hydroxylation step
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
-
-
acetone
-
10%, v/v, complete inhibition of hydroxylation
Anti-11beta-hydroxylase IgG
-
polyclonal, raised in rabbits, inhibition of 11-beta/18-hydroxylation and aldosterone synthesis of corticosterone
-
Anti-11beta-hydroxylase IgG
-
cross-reaction with 51 kDa protein
-
antiserum
-
produced by rabbits
-
ascorbate
-
without NADH, inhibition of aldosterone synthetase
atenolol
-
potent inhibition of CYP11B2, recombinant enzyme
clotrimazole
-
azole derivative, antimycotic drug, strong dose-dependent inhibition
CO
-
affects 11beta-/19-hydroxylase reaction
CO
-
strongly
corticosterone
-
competitive inhibition of 11beta-hydroxylase activity
deoxycorticosterone
-
competitive substrate inhibition
diphosphatidyl glycerol
-
cardiolipin, dipalmitoyl phasphatidylcholine vesicles, 50% inhibition with 4-5 mol%, complete inhibition at 15 mol%
EDTA
-
10 mM
erythromycin
-
potent inhibition of CYP11B2, recombinant enzyme
ethanol
-
10%, v/v, complete inhibition of hydroxylation
FAD286
-
inhibitor of 11-beta-hydroxylase CYP11B1
fadrozole
-
50% inhibition at 0.001 mM
fadrozole
-
50% inhibition at 0.010 mM
fadrozole
-
CYP11B2 IC50: 1 nM, CYP11B1 IC50: 10 nM, recombinant enzymes
fadrozole
-
in vitro and in vivo inhibition
fadrozole
-
inhibitor of CYP11B2
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
HgCl2
-
0.2 mM, 50% inhibition
iron-sulfur protein
-
adrenodoxin, at high concentrations, 25% inhibition
-
KCl
-
total inactivation
KCN
-
slight inhibitor
ketoconazole
-
azole derivative, antimycotic drug, strong dose-dependent inhibition
ketoconazole
-
-
ketoconazole
-
50% inhibition at 0.081 mM
ketoconazole
-
CYP11B2 IC50: 81 nM, CYP11B1 IC50: 224 nM, recombinant enzymes
ketoconazole
-
-
ketoprofene
-
potent inhibition of CYP11B2, recombinant enzyme
methanol
-
10%, v/v, complete inhibition of hydroxylation
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
-
-
methyltrienolone
-
synthetic androgen, used as photoaffinity ligand and substrate analog, covalent binding, 0.1 mM inhibits cortisol synthesis, during photolabeling radioactivity incorporation via radioactive methyltrienolone is blocked by 11-deoxycorticosterone, so it binds to the conserved substrate binding region Trp428-Leu429-Asp430-Arg431 between beta3-sheet and the L-helix analysed by trypsin digest
metyrapol
-
11beta-hydroxylase inhibition, 40.8% by racemate, 38.1% by (+)-enantiomer and 33.8% by (-)-enantiomer, each 0.4 mM
Metyrapone
-
2 mM
Metyrapone
-
competitive substrate inhibition
Metyrapone
-
competitive with substrate, affects strongly 11beta-/18-hydroxylation and 11beta-/19-hydroxylation
Metyrapone
-
-
Metyrapone
-
inhibition of the purified 11beta-hydroxylase, 18-hydroxylation and aldosterone synthesis of corticosterone are inhibited
Metyrapone
-
11beta-hydroxylase, 39.7% inhibition by 0.4 mM
Metyrapone
-
diagnostic inhibitor, strong inhibition, 0.02 mM complete inhibition
Metyrapone
-
-
Metyrapone
-
79% inhibition of CYP11B2 at 0.5 mM, 94% inhibition of CYP11B2
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
norharman
-
beta-carboline, high affinity type II ligand to both cytochromes, progesterone binding to CYP17 competitively inhibited
p-chloromercuribenzoate
-
1 mM
PCMB
-
0.1 mM, 50% inhibition
phenazine methosulfate
-
1 mM, crude extract
phosphate
-
-
phosphatidylcholine
-
unsaturated increasing dioleoyl/diphytanoyl phosphatidylcholine
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
-
-
SKF 525A
-
little inhibition of the purified 11beta-hydroxylase, 18-hydroxylation and aldosterone synthesis of corticosterone are inhibited
Sodium cholate
-
0.2% effect nearly 20% inhibition
spironolactone
-
diuretic and antihypertensive drug, competitive aldosterone antagonist, slight inhibition
Stilbestrol
-
-
sulfhydryl reagents
-
strongly
testosterone
-
potent inhibition of CYP11B2, recombinant enzyme
[3-(1H-imidazol-1-ylmethyl)phenyl]methanol
-
-
[4-(1H-imidazol-1-ylmethyl)phenyl]methanol
-
-
additional information
-
conversion of labelled steroid to labelled aldosterone is inhibited by the addition of an excess of the same unlabelled steroid
-
additional information
-
no inhibition with Harman, tetrahydronorharman and tetrahydroharman
-
additional information
-
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 inhibitors above 300 nM, overview
-
additional information
-
synthesis and evaluation of heteroaryl-substituted dihydronaphthalenes and indenes: potent and selective inhibitors of CYP11B2 for the treatment of congestive heart failure and myocardial fibrosis, ligand-protein interactions, docking and molecular dynamics studies using homology-modeled CYP11B2 structure, overview
-
additional information
-
effects of enzyme inhibition of steroid biosynthesis and mineralcorticoid formation, overview
-
additional information
-
dexamethasone represses the enzyme in nervous system tissues, overview
-
additional information
-
a sulfonamide-imidazole scaffold is a potent inhibitor of CYP11B2, the scaffold can achieve high levels of selectivity for CYP11B2 over CYP11B1, overview. Evaluation of a lactam series of derivatives of the R-enantiomer of fadrozole, FAD286, homology modelling, overview
-
additional information
-
synthesis of 23 N-(pyridin-3-yl)benzamides and evaluation for their potential to inhibit steroid-11beta-hydroxylase CYP11B1 and aldosterone synthase CYP11B2, overview. N-(Pyridin-3-yl)benzamides are a highly selective class of CYP11B2 inhibitors in vitro. No or poor inhibition of both isozymes by 3i, 3j, 3l, and 3s
-
additional information
-
three-dimensional modeling of CYP11B2 to model the binding modes of the natural substrate 18-hydroxycorticosterone and the CYP11B2 inhibitor R-fadrozole, overview. Synthesis, biological evaluation, and molecular modeling of 1-benzyl-1H-imidazoles as selective inhibitors of aldosterone synthase, overview. Molecular docking in the CYP11B1 and CYP11B2 models
-
additional information
-
development of 1,2,5,6-tetrahydropyrrolo[3,2,1-ij]quinolin-4-ones and structurally related aldosterone synthase inhibitors, molecular modelling, overview. No inhibition of both isozymes by 32 and 15
-
additional information
-
structure homology modelling for inhibitor design, overview
-
additional information
-
estradiol has no effect on aldosterone production by wild-type CYP11B1 and chimeric mutant CYP11B1/B2 in HEK-293 cells
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
-
most potent activator in intact mitochondria
fumarate
-
increase of activity
KCN
-
slight
lipid extract
-
from adrenocortical mitochondria, increase of aldosterone production from corticosterone
-
malate
-
plus NADP+ and in synergism with ascorbate plus NADH increase of aldosterone synthetase activity in zona glomerulosa, no stimulation of 11beta-/18-hydroxylation
MnCl2
-
1 mM, reactivation of dialysed enzyme
NAD(P)H
-
enhance activity of crude extracts that show hydroxylation without any cofactor
phosphatidylcholine
-
saturated acyl chains such as dipalmitoyl/dimyristoyl phosphatidylcholine
MnCl2
-
causes most of activity to disappear in crude extracts
additional information
-
treatment of adult rate ventricular myocytes ACTH and angiotensin II has no stimulatory effect on CYP11B1 and CYP11B2 expression
-
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
-
additional information
A1XRK1
genes amh and cyp11b are both upregulated during juvenile ovary-to-testis transformation
-
additional information
-
progesterone induces the enzyme
-
additional information
-
adrenocorticotrophin induces the enzyme in central nervous system tissues, adrenal ectomy does only slightly increase enzyme expression, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0008
11-deoxycorticosterone
-
presence of methyltrienolone
0.00087
11-deoxycorticosterone
-
without phospholipids
0.0011
11-deoxycorticosterone
-
with phospholipids
0.0015
11-deoxycorticosterone
-
+/-0.00008
0.00197
11-deoxycorticosterone
-
+/-0.00026
0.002
11-deoxycorticosterone
-
absence of methyltrienolone
0.005
11-deoxycorticosterone
-
dipalmitoyl-phosphatidylcholine vesicles
0.0073
11-deoxycorticosterone
-
37°C
0.01
11-deoxycorticosterone
-
dipalmitoyl/diphytanoyl-phosphatidylcholine vesicles
0.033
11-deoxycorticosterone
-
dipalmitoyl phosphatidylcholine/diphosphatidyl glycerol vesicles
0.18
11-deoxycorticosterone
-
pH 7.4, recombinant enzyme
0.077
11-deoxycortisol
-
11beta-hydroxylation
0.338
11-deoxycortisol
-
pH 7.4, recombinant enzyme
0.013
4-androstene-3,17-dione
-
identical for both enzyme activities
0.002
adrenal ferredoxin
-
pH 7.4, recombinant enzyme, with 11-deoxycorticosterone as substrate
-
0.0024
adrenal ferredoxin
-
pH 7.4, recombinant enzyme, with 11-deoxycortisol as substrate
-
0.0059
corticosterone
-
+/-0.00018
0.0084
corticosterone
-
without phospholipids
0.009
corticosterone
-
+/-0.0009
0.06 - 0.09
corticosterone
-
presence of methyltrienolone
0.087
corticosterone
-
with phospholipids
0.006
deoxycorticosterone
-
identical for both enzyme activities
0.02
deoxycorticosterone
-
identical for both enzymes activities
additional information
additional information
-
kinetic parameters only slightly modified by presence of phospholipids, 0.2% soybean lecithin
-
additional information
additional information
-
lipids such as DLPC required
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
steady-state kinetics, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.133
11-deoxycorticosterone
-
dipalmitoyl phosphatidylcholine vesicles + diphosphatidyl glycerol
0.3
11-deoxycorticosterone
-
18-hydroxylation
0.583
11-deoxycorticosterone
-
dipalmitoyl phosphatidylcholine vesicles
0.66
11-deoxycorticosterone
-
+/-2.112, calculatetd from Kcat/Km
0.85
11-deoxycorticosterone
-
pH 7.4, recombinant enzyme
1.83
11-deoxycorticosterone
-
11beta-hydroxylation
0.167
11-deoxycortisol
-
pH 7.4, recombinant enzyme
3.45
11-deoxycortisol
-
11beta-hydroxylation
1
adrenal ferredoxin
-
pH 7.4, recombinant enzyme, with 11-deoxycorticosterone as substrate
-
1.48
adrenal ferredoxin
-
pH 7.4, recombinant enzyme, with 11-deoxycortisol as substrate
-
0.0378
corticosterone
-
+/-0.2268, calculatetd from Kcat/Km
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
IMAGE
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
-
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
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000016
(R)-4-(5,6,7,8-tetrahydroimidazo[1,5-a]pyridin-5-yl)benzonitrile
-
competitive inhibition, pH 7.4
0.0000099
(R)-4-(5,6,7,8-tetrahydroimidazo[1,5-a]pyridin-5-yl)benzonitrile
-
competitive inhibition, pH 7.4, 25°C
0.000448
1-(1H-inden-2-yl)-1H-imidazole
-
CYP11B2 IC50: 448 nM, no inhibition of CYP11B1, recombinant enzymes
0.000334
1-(3,4-dihydronaphthalen-2-yl)-1H-imidazole
-
CYP11B2 IC50: 334 nM, recombinant enzymes
0.000639
1-(3,4-dihydronaphthalen-2-yl)-1H-imidazole
-
CYP11B1 IC50: 639 nM
0.000143
1-(3-bromobenzyl)-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000365
1-(3-bromobenzyl)-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000151
1-(3-chlorobenzyl)-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000457
1-(3-chlorobenzyl)-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.001
1-(3-cyanobenzyl)-1H-imidazole
-
above, inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication; above, inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000206
1-(3-fluorobenzyl)-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000815
1-(3-fluorobenzyl)-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000236
1-(4-aminobenzyl)-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.001
1-(4-aminobenzyl)-1H-imidazole
-
above, inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000211
1-(4-bromobenzyl)-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000479
1-(4-bromobenzyl)-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000051
1-(4-bromobenzyl)-5-phenyl-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000007
1-(4-bromobenzyl)-5-phenyl-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.001
1-(4-chlorobenzyl)-1H-imidazole
-
above, inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication; above, inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000058
1-(4-chlorobenzyl)-5-phenyl-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000025
1-(4-chlorobenzyl)-5-phenyl-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000368
1-(4-cyanobenzyl)-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000372
1-(4-cyanobenzyl)-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000023
1-(4-cyanobenzyl)-5-(2-fluorophenyl)-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.00002
1-(4-cyanobenzyl)-5-(2-fluorophenyl)-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.0000037
1-(4-cyanobenzyl)-5-(2-methylphenyl)-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000057
1-(4-cyanobenzyl)-5-(2-methylphenyl)-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.0000055
1-(4-cyanobenzyl)-5-(3-fluorophenyl)-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000032
1-(4-cyanobenzyl)-5-(3-fluorophenyl)-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.0000052
1-(4-cyanobenzyl)-5-(3-methylphenyl)-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000062
1-(4-cyanobenzyl)-5-(3-methylphenyl)-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000025
1-(4-cyanobenzyl)-5-(4-fluorophenyl)-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000027
1-(4-cyanobenzyl)-5-(4-fluorophenyl)-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000117
1-(4-cyanobenzyl)-5-(4-methylphenyl)-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.00013
1-(4-cyanobenzyl)-5-(4-methylphenyl)-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000307
1-(4-cyanobenzyl)-5-(4-pyridyl)-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000407
1-(4-cyanobenzyl)-5-(4-pyridyl)-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000007
1-(4-cyanobenzyl)-5-(methyl carboxylate)-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000048
1-(4-cyanobenzyl)-5-(methyl carboxylate)-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000044
1-(4-cyanobenzyl)-5-(methylene-acetate)-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000213
1-(4-cyanobenzyl)-5-(methylene-acetate)-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000023
1-(4-cyanobenzyl)-5-bromo-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000073
1-(4-cyanobenzyl)-5-bromo-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000062
1-(4-cyanobenzyl)-5-formyl-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000478
1-(4-cyanobenzyl)-5-formyl-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000029
1-(4-cyanobenzyl)-5-hydroxymethyl-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000285
1-(4-cyanobenzyl)-5-hydroxymethyl-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000012
1-(4-cyanobenzyl)-5-methyl-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000141
1-(4-cyanobenzyl)-5-methyl-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.0000017
1-(4-cyanobenzyl)-5-phenyl-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000028
1-(4-cyanobenzyl)-5-phenyl-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.00033
1-(4-fluorobenzyl)-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000494
1-(4-fluorobenzyl)-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000709
1-(4-fluorobenzyl)-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.001799
1-(4-fluorobenzyl)-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000011
1-(4-fluorobenzyl)-5-phenyl-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000016
1-(4-fluorobenzyl)-5-phenyl-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000011
1-(4-methoxybenzyl)-5-phenyl-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000014
1-(4-methoxybenzyl)-5-phenyl-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000411
1-(6-methoxy-3,4-dihydronaphthalen-2-yl)-1H-imidazole
-
CYP11B2 IC50: 411 nM, recombinant enzymes
0.000763
1-(6-methoxy-3,4-dihydronaphthalen-2-yl)-1H-imidazole
-
CYP11B1 IC50: 763 nM
0.0000048
1-benzyl-5-phenyl-1H-imidazole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000011
1-benzyl-5-phenyl-1H-imidazole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000161
2,4,5-trifluoro-N-(pyridin-3-yl)benzamide
-
inhibition of CYP11B1, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.000166
2,4,5-trifluoro-N-(pyridin-3-yl)benzamide
-
inhibition of CYP11B2, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.0000052
2-(4-chlorobenzyl)-4-(2-methylpropyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000059
3,4-difluoro-N-(pyridin-3-yl)benzamide
-
inhibition of CYP11B1, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.0000535
3,4-difluoro-N-(pyridin-3-yl)benzamide
-
inhibition of CYP11B2, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.000181
3-(1-benzyl-1H-imidazol-5-yl)-1-propanol
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000286
3-(1-benzyl-1H-imidazol-5-yl)-1-propanol
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.00003
3-(1-ethyl-3,4-dihydronaphthalen-2-yl)-pyridine
-
CYP11B2 IC50: 30 nM, recombinant enzymes
0.002117
3-(1-ethyl-3,4-dihydronaphthalen-2-yl)-pyridine
-
CYP11B1 IC50: 2117 nM
0.000007
3-(1-methyl-3,4-dihydronaphthalen-2-yl)-pyridine
-
CYP11B2 IC50: 7 nM, recombinant enzymes
0.001268
3-(1-methyl-3,4-dihydronaphthalen-2-yl)-pyridine
-
CYP11B1 IC50: 1268 nM
0.00039
3-(1H-imidazol-1-ylmethyl)aniline
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.0006
3-(1H-imidazol-1-ylmethyl)aniline
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000007
3-(3,4-dihydronaphthalen-2-yl)pyridine
-
CYP11B2 IC50: 7 nM, recombinant enzymes
0.001729
3-(3,4-dihydronaphthalen-2-yl)pyridine
-
CYP11B1 IC50: 1729 nM
0.000005
3-(3-methyl-3,4-dihydronaphthalen-2-yl)pyridine
-
CYP11B2 IC50: 5 nM, recombinant enzymes
0.000503
3-(3-methyl-3,4-dihydronaphthalen-2-yl)pyridine
-
CYP11B1 IC50: 503 nM
0.000176
3-(4-ethyl-3,4-dihydronaphthalen-2-yl)pyridine
-
CYP11B2 IC50: 176 nM, recombinant enzymes
0.001615
3-(4-ethyl-3,4-dihydronaphthalen-2-yl)pyridine
-
CYP11B1 IC50: 1615 nM
0.000013
3-(4-methyl-3,4-dihydronaphthalen-2-yl)pyridine
-
, CYP11B2 IC50: 13 nM, recombinant enzymes
0.001291
3-(4-methyl-3,4-dihydronaphthalen-2-yl)pyridine
-
CYP11B1 IC50: 1291 nM
0.000004
3-(6-methoxy-1H-inden-2-yl)pyridine
-
CYP11B2 IC50: 4 nM, recombinant enzymes
0.005684
3-(6-methoxy-1H-inden-2-yl)pyridine
-
competitive, CYP11B1 IC50: 5684 nM
0.000002
3-(6-methoxy-3,4-dihydronaphthalen-2-yl)pyridine
-
CYP11B2 IC50: 2 nM, recombinant enzymes
0.000578
3-(6-methoxy-3,4-dihydronaphthalen-2-yl)pyridine
-
competitive, CYP11B1 IC50: 578 nM
0.000045
3-(7-methoxy-3,4-dihydronaphthalen-2-yl)pyridine
-
CYP11B2 IC50: 45 nM, no inhibition of CYP11B1, recombinant enzymes
0.000288
3-[(Z)-2-phenylvinyl]pyridine
-
CYP11B1 IC50: 288 nM
0.000735
3-[(Z)-2-phenylvinyl]pyridine
-
CYP11B2 IC50: 735 nM, no inhibition by the 3-[(E)-2-phenylvinyl]pyridine isomer, recombinant enzymes
0.0000062
3-[1-(4-bromobenzyl)-1H-imidazol-5-yl]-1-propanol
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000018
3-[1-(4-bromobenzyl)-1H-imidazol-5-yl]-1-propanol
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000044
3-[1-(4-chlorobenzyl)-1H-imidazol-5-yl]-1-propanol
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000055
3-[1-(4-chlorobenzyl)-1H-imidazol-5-yl]-1-propanol
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000013
3-[1-(4-cyanobenzyl)-1H-imidazol-5-yl]-1-propanol
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000048
3-[1-(4-cyanobenzyl)-1H-imidazol-5-yl]-1-propanol
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000016
3-[1-(4-fluorobenzyl)-1H-imidazol-5-yl]-1-propanol
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000116
3-[1-(4-fluorobenzyl)-1H-imidazol-5-yl]-1-propanol
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000012
3-[1-(4-methoxybenzyl)-1H-imidazol-5-yl]-1-propanol
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000059
3-[1-(4-methoxybenzyl)-1H-imidazol-5-yl]-1-propanol
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
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
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000005
4-((5-phenyl-1H-imidazol-1-yl)methyl)benzonitrile
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.0000017
4-((5-phenyl-1H-imidazol-1-yl)methyl)benzonitrile
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000117
4-(2-methylpropyl)-2-(thiophen-2-ylmethyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
-
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
-
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
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.002529
4-(6-methoxy-3,4-dihydronaphthalen-2-yl)pyridine
-
CYP11B1 IC50: 2529 nM
0.002834
4-(6-methoxy-3,4-dihydronaphthalen-2-yl)pyridine
-
CYP11B2 IC50: 2834 nM, recombinant enzymes
0.000104
4-bromo-N-(pyridin-3-yl)benzamide
-
inhibition of CYP11B2, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.000167
4-bromo-N-(pyridin-3-yl)benzamide
-
inhibition of CYP11B1, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.0000102
4-chloro-N-(pyridin-3-yl)benzamide
-
inhibition of CYP11B1, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.000065
4-chloro-N-(pyridin-3-yl)benzamide
-
inhibition of CYP11B2, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.0000075
4-cyano-N-(pyridin-3-yl)benzamide
-
inhibition of CYP11B1, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.000078
4-cyano-N-(pyridin-3-yl)benzamide
-
inhibition of CYP11B2, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.0000143
4-fluoro-N-(pyridin-3-yl)benzamide
-
inhibition of CYP11B1, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.000082
4-fluoro-N-(pyridin-3-yl)benzamide
-
inhibition of CYP11B2, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.0000248
4-nitro-N-(pyridin-3-yl)benzamide
-
inhibition of CYP11B1, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.000145
4-nitro-N-(pyridin-3-yl)benzamide
-
inhibition of CYP11B2, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.0000002
6-(5,8-dihydroisoquinolin-4-yl)-3,4-dihydroquinolin-2(1H)-one
-
inhibition of CYP11B2, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.000033
6-(5,8-dihydroisoquinolin-4-yl)-3,4-dihydroquinolin-2(1H)-one
-
inhibition of CYP11B1, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.000089
8-(1H-imidazol-1-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.002077
8-(1H-imidazol-1-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000001
8-(5-ethoxypyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000158
8-(5-ethoxypyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000044
8-(5-fluoropyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.001288
8-(5-fluoropyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000043
8-(5-hydroxypyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.002045
8-(5-hydroxypyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000006
8-(5-methoxypyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000247
8-(5-methoxypyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000013
8-(5-phenylpyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]-quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000058
8-(5-phenylpyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]-quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000002
8-(isoquinolin-4-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000013
8-(isoquinolin-4-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000011
8-(pyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000715
8-(pyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000012
8-(pyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinoline-4-thione
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000333
8-(pyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinoline-4-thione
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000056
8-(pyrimidin-5-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.02855
8-(pyrimidin-5-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000036
8-[5-(2,5-difluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000183
8-[5-(2,5-difluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000007
8-[5-(2-fluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000043
8-[5-(2-fluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000024
8-[5-(2-methoxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000128
8-[5-(2-methoxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000023
8-[5-(3,4-difluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000496
8-[5-(3,4-difluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000018
8-[5-(3,5-difluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.001748
8-[5-(3,5-difluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000014
8-[5-(3-fluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.00049
8-[5-(3-fluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000012
8-[5-(3-hydroxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000044
8-[5-(3-hydroxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000046
8-[5-(3-methoxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.001374
8-[5-(3-methoxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000009
8-[5-(4-fluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.00004
8-[5-(4-fluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000014
8-[5-(4-methoxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000021
8-[5-(4-methoxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000022
8-[5-(propan-2-yloxy)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000103
8-[5-(propan-2-yloxy)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000059
8-[5-(trifluoromethyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000141
8-[5-(trifluoromethyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000016
8-[5-[3-(trifluoromethoxy)phenyl]pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.002058
8-[5-[3-(trifluoromethoxy)phenyl]pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000033
8-[5-[3-(trifluoromethyl)phenyl]pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.004646
8-[5-[3-(trifluoromethyl)phenyl]pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000009
9-(5-methoxypyridin-3-yl)-2,3,6,7-tetrahydro-1H,5H-pyrido[3,2,1-ij]quinolin-5-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000545
9-(5-methoxypyridin-3-yl)-2,3,6,7-tetrahydro-1H,5H-pyrido[3,2,1-ij]quinolin-5-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000024
9-(pyridin-3-yl)-1,2,6,7-tetrahydro-5H-pyrido[ 3,2,1-ij]quinolin-3-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.002296
9-(pyridin-3-yl)-1,2,6,7-tetrahydro-5H-pyrido[ 3,2,1-ij]quinolin-3-one
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000002
9-[6-(isoquinolin-4-yl)pyridin-3-yl]-2,3,6,7-tetrahydro-1H,5H-pyrido[3,2,1-ij]quinolin-5-one
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
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
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000001
fadrozole
-
CYP11B2 IC50: 1 nM
0.00001
fadrozole
-
CYP11B1 IC50: 10 nM, recombinant enzymes
0.000081
ketoconazole
-
CYP11B2 IC50: 81 nM
0.000224
ketoconazole
-
IC50 CYP11B1 IC50: 224 nM, recombinant enzymes
0.000193
methyl 3-(1-benzyl-1H-imidazol-5-yl)-propanoate
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000326
methyl 3-(1-benzyl-1H-imidazol-5-yl)-propanoate
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000004
methyl 3-[1-(4-bromobenzyl)-1H-imidazol-5-yl]-propanoate
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000057
methyl 3-[1-(4-bromobenzyl)-1H-imidazol-5-yl]-propanoate
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000123
methyl 3-[1-(4-chlorobenzyl)-1H-imidazol-5-yl]-propanoate
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000177
methyl 3-[1-(4-chlorobenzyl)-1H-imidazol-5-yl]-propanoate
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000035
methyl 3-[1-(4-cyanobenzyl)-1H-imidazol-5-yl]-propanoate
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000031
methyl 3-[1-(4-cyanobenzyl)-1H-imidazol-5-yl]-propanoate
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.00005
methyl 3-[1-(4-fluorobenzyl)-1H-imidazol-5-yl]-propanoate
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000104
methyl 3-[1-(4-fluorobenzyl)-1H-imidazol-5-yl]-propanoate
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000111
methyl 3-[1-(4-methoxybenzyl)-1H-imidazol-5-yl]-propanoate
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000121
methyl 3-[1-(4-methoxybenzyl)-1H-imidazol-5-yl]-propanoate
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000146
Metyrapone
-
inhibition of CYP11B1, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.000006
R-fadrozole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000119
R-fadrozole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.00004
S-fadrozole
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000171
S-fadrozole
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000206
[3-(1H-imidazol-1-ylmethyl)phenyl]methanol
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.001174
[3-(1H-imidazol-1-ylmethyl)phenyl]methanol
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000695
[4-(1H-imidazol-1-ylmethyl)phenyl]methanol
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.001
[4-(1H-imidazol-1-ylmethyl)phenyl]methanol
-
above, inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000072
Metyrapone
-
inhibition of CYP11B2, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.0001
additional information
-
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
LITERATURE
0.00000314
-
aldosterone production, mitochondria from zona glomerulosa
0.0000236
-
18-hydroxycorticosterone production, mitochondria from zona fasciculata
0.00003
-
18-hydroxylation
0.000119
-
18-hydroxycorticosterone production, mitochondria from zona glomerulosa
0.000171
-
18-hydroxylation activity, 4% O2, 96% N2
0.000211
-
18-hydroxylation activity, 21% O2, 79% N2
0.001061
-
deoxycorticosterone, 18-hydroxylation activity in
0.00205
-
11beta-hydroxylation activity, 4% O2, 96% N2
0.00206
-
18-hydroxydeoxycorticosterone production, mitochondria from zona glomerulosa
0.00278
-
11beta-hydroxylation activity, 21% O2, 79% N2
0.0053
-
11beta-hydroxylation
0.00599
-
18-hydroxydeoxycorticosterone production, mitochondria from zona fasciculata
0.00691
-
corticosterone production, mitochondria from zona glomerulosa
0.00951
-
corticosterone production, mitochondria from zona fasciculata
0.00968
-
+/-0.00126, 40.8% inhibition by 0.4 mM metyrapol, adrenal tissue
0.00986
-
+/-0.00044, 39.7% inhibition by 0.4 mM metyrapone, adrenal tissue
0.01011
-
+/-0.00126, 38.1% inhibition by 0.4 mM (+)-metyrapol, adrenal tissue
0.01081
-
+/-0.00269, 33.8% inhibition by 0.4 mM (-)-metyrapol, adrenal tissue
0.01193
-
deoxycorticosterone, 11beta-hydroxylation activity
0.01633
-
+/-0.00237, no inhibitor, adrenal tissue
0.0198
-
purified recombinant enzyme
1.35 - 1.36
-
corticosterone, enzyme incorporated into liposomes
1.38
-
corticosterone, soluble form of enzyme
additional information
-
activities of sonicated mitochondria and cholate extract of hydroxylation activities with deoxycotricosterone and 4-androstene-3,17-dione as substrates
additional information
-
several activities of 49.5 and 51.5 kDa proteins for multihydroxylation steps
additional information
-
conversion of 11-deoxycorticosterone
additional information
-
dependent on DLPC concentration, with 0.05 mM maximum activity, 2fold increase with addition of 15% glycerol, 0.6 mM GSH, 0.01 mM FAD and 0.01 mM FMN
additional information
-
CYP11B2 and CYP11B1 expression analysis in male Wistar rats with heart failure induced by coronary artery ligation and sham-operated controls, in stroke-prone spontaneously hypertensive rats and Wistar Kyoto rats as controls, in cyp1a1Ren-2 transgenic rats and Fischer controls, and in isolated adult Sprague-Dawley ventricular myocytes incubated with 11-deoxycorticosterone, overview
additional information
P15538
-
additional information
-
urinary steroid profiling of halpotype mutants
additional information
-
urinary steroid analyses
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
assay at
7.2
-
assay at; assay at
7.4
-
30 mM sodium phosphate buffer
7.4
-
assay at; assay at
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 7.2
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
-
assay at
26
-
assay at
30
-
assay at
30
-
assay at
35
-
30 mM sodium phosphate buffer
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
P15538
assay at
37
-
assay at
37
-
assay at; assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 15
-
2fold decrease of activity with increase of temperature, temperatures above 25°C unfavourable
2 - 50
-
at 50°C almost no activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
capsular portion in zona glomerulosa cells, decapsular in zonae fasciculata and reticularis
Manually annotated by BRENDA team
-
isolated mitochondria from human NCI-H295 adrenal cells
Manually annotated by BRENDA team
-
zona fasciculata in the adrenal cortex
Manually annotated by BRENDA team
-
zona fasiculata
Manually annotated by BRENDA team
-
zona glomerulosa
Manually annotated by BRENDA team
-
cerebellar granule layer
Manually annotated by BRENDA team
-
CYP11B shows a highly dimorphic expression pattern throughout gonadogenesis
Manually annotated by BRENDA team
A1XRK1
during development all zebrafish males first develop a juvenile ovary, that later degenerates and transforms into a testis, the enzyme is involved, but not inducing, in gonadal transformation in the zebrafish, but its localization is not related to the position of degenerating oocytes, overview
Manually annotated by BRENDA team
-
enzyme expression during sex differentiation and in adult fish at the breeding stage, the enzyme level is higher in the male phase than during testicular differentiation or in the female phase
Manually annotated by BRENDA team
-
cardiac tissue from several rat models of cardiovascular pathology, low constitutive expression, which seems to be of no physiologic relevance
Manually annotated by BRENDA team
-
primary culture of hippocampal neurons isolated from fetus
Manually annotated by BRENDA team
-
corresponding to mammalian adrenal gland, P-450(11beta,aldo) and adrenodoxin reductase exist more in outer regions of frogs during the spring and the summer
Manually annotated by BRENDA team
-
Leydig cells and inter-renal cells of head kidney
Manually annotated by BRENDA team
A1XRK1
higher enzyme expression level
Manually annotated by BRENDA team
Absidia caerulea IBL02
-
-
-
Manually annotated by BRENDA team
-
adrenocortical tumor cell line
Manually annotated by BRENDA team
Q2I128
faintly expressed
Manually annotated by BRENDA team
Q2I128
slightly expressed
Manually annotated by BRENDA team
-
pharmacokinetics of metyrapone and metyrapol
Manually annotated by BRENDA team
A1XRK1
very high expression level
Manually annotated by BRENDA team
Q2I128
fully expressed, markedly up-regulated at the onset of testicular development
Manually annotated by BRENDA team
-
adrenocortical tumor cell line Y-1
Manually annotated by BRENDA team
P15538
CYP11B1 expression
Manually annotated by BRENDA team
-
cells of the adrenal gland express CYP11B2
Manually annotated by BRENDA team
P15538
CYP11B1 expression
Manually annotated by BRENDA team
additional information
-
no signal: brain, pituitary, gill, heart, liver, pyloric caeca, intestine, ovary, muscle, skin, blood
Manually annotated by BRENDA team
additional information
-
enzyme expression analysis
Manually annotated by BRENDA team
additional information
-
no activity in adult ventricular myocyte
Manually annotated by BRENDA team
additional information
-
gene expression during the thermosensitive period and gonadogenesis, maximally residual activity in tissues other than head kidney and gonads, overview
Manually annotated by BRENDA team
additional information
A1XRK1
the mRNA of cyp11b is detected in all the adult organs tested
Manually annotated by BRENDA team
additional information
-
tissue expression analysis, overview
Manually annotated by BRENDA team
additional information
Q2I128
genes differentially expressed during the sex change process. The ratio of male to female expression (male P45011beta/female P45011beta) is higher than 20
Manually annotated by BRENDA team
additional information
-
no expression in the ovary
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
cytochrome P-45011beta in inner mitochondrial membrane, adrenodoxin reductase and adrenodoxin are loosely associated, inclusion of purified P-45011beta into phospholipid vesicles mimics the situation in vivo
Manually annotated by BRENDA team
-
from zona fasciculata
Manually annotated by BRENDA team
-
reconstitution of cytochrome P45011beta, an intrinsic protein of inner membrane, into phospholipid vesicles via detergent dialysis procedure
Manually annotated by BRENDA team
-
from zona glomerulosa and fasciculata
Manually annotated by BRENDA team
-
CYP11B1 in zona fasciculata, CYP11B2 in zona glomerulosa, new CYP11B3
Manually annotated by BRENDA team
-
from zona reticularis
Manually annotated by BRENDA team
-
from zona reticularis
Manually annotated by BRENDA team
-
from zona glomerulosa
Manually annotated by BRENDA team
-
inner membrane, all 3 zones
Manually annotated by BRENDA team
-
the precursor form of the enzyme translocates into the matrix of the mitochondria, where it undergoes cleavage by mitochondrial processing peptidase to a mature form of approximately 54 kDa. Mature enzyme seems to translocate across the inner mitochondrial membrane a second time to finally reside in the intermembrane space
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
185000
-
exclusion chromatography
285389
1000000
-
glycerol density gradient
285389
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 48000, SDS-PAGE
?
-
x * 60000, SDS-PAGE
?
-
x * 60000, SDS-PAGE
?
-
x * 55555, calculated from full-length cDNA of 1.5 kb
?
-
x * 51000, SDS-PAGE, enzyme expressed from mitochondria of interregnal tissue
?
-
x * 48500 major form, x * 49500 isoform, SDS-PAGE
?
-
x * 47500, SDS-PAGE
?
-
x * 49000 and x * 51000, SDS-PAGE
?
-
x * 46000, two-dimensional gel
?
-
x * 49500 of capsular portion and x * 51500 of capsular and decapsular portion, 11beta-hydroxylase activities, SDS-PAGE
?
-
x * 46000
?
-
x * 47500
?
-
x * 48500-51500, SDS-PAGE after Sepharose, x * 48400/49500, SDS-PAGE after HPLC
?
-
x * 51500, SDS-PAGE
?
-
x * 55761, recombinant enzyme, mass spectrometry
?
-
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
tetramer
-
4 * 47500, SDS-PAGE
?
Absidia caerulea IBL02
-
x * 60000, SDS-PAGE
-
additional information
-
enzyme secondary structure, overview
additional information
-
homology modeling and molecular docking of CYP11B2, overview
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
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2
-
crude extract, 7 mg/ml, 24 h, loss of half the activity, DEAE fraction unstable
285388
2
-
14% residual activity of 11beta- and 18-hydroxylation
285390
30
-
after preincubation for 20 min, 27% residual activity, after 60 min 5.7%
285390
30
-
in presence of phospholipids, catalytic activity stable to extended incubation and increased resistance of hemoprotein to denaturation
285402
30
-
30 min, 30 mM sodium phosphate buffer, pH 8.0, decrease to 30%, improved to 45-70% by addition of 1 mM GSH, 0.2 mM 11-deoxycortisol, 0.5 mM PMSF or 20% glycerol
285409
30
-
purified enzyme, loss of 75% activity after 3 h, and of all activity after 8 h
686458
50
-
complete inactivation
285390
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
deoxycorticosterone stabilizes
-
deoxycorticosterone, protection of enzyme from inactivation by 18-ethynylprogesterone
-
inclusion into phospholipid vesicles stabilizes
-
phospholipid vesicles, 0.2% soybean lecithin, added to purified P-45011beta for storage and during incubation
-
11-deoxycortisol, partially stabilizes
-
alpha-lipoic acid, during DEAE chromatography stabilizes
-
EDTA, stabilizes during purification
-
glycerol, partially stabilizes
-
GSH, partially stabilizes
-
GSH, stabilizes during purification, as well as other sulfhydryl compounds
-
PMSF, partially stabilizes
-
Tween 80, positive influence on activity conservation during extraction and fractionation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified enzyme, 24 h, addition of 20% glycerol, 0.5 mM PMSF, 0.5 mM DTT, 95.3% remaining activity
-
-20°C, 50% glycerol, 1 week, without significant loss of activity
-
-80°C, 20 mM potassium phosphate buffer, pH 7.4, 0.01 mM 11-deoxycorticosterone, 0.1 mM EDTA, 0.1 mM dithiothreitol, 1%, w/v, sodium cholate
-
-80°C, 59 mM potassium phosphate buffer, pH 7.4, 0.1 mM EDTA, 0.1 mM dithiothreitol, 0.01 mM deoxycorticosterone, 0.3% cholate, 0.3% Tween 20
-
-80°C, after ammonium sulfate precipitation, 50 mM potassium phosphate, pH 7.4, 0.1 mM EDTA, 0.1 mM dithiothreitol, 0.5% sodium cholate, 0.5% soybean lecithin, several months, without loss of activity
-
-80°C, after hydroxyapatite column/FPLC system, 50 mM potassium phosphate, pH 7.4, 0.01% sodium cholate, 0.05% soybean lecithin, 0.01 mM 11-deoxycorticosterone, 0.1 mM dithiothreitol, 0.1 mM EDTA, without loss of activity
-
-80°C, after octyl-Sepharose, deoxycorticosterone-bound, 50 mM potassium phosphate, pH 7.4, 0.5% sodium cholate, 0.2% Tween 20, 0.01 mM 11-deoxycorticosterone, 0.1 mM dithiothreitol, 0.1 mM EDTA
-
4°C, 1 week, without significant loss of activity
-
4°C, 11 days, both activities decrease considerably in a similar way, deoxycorticosterone delays decline
-
4°C, enzyme incorporated into liposomes, stable during 2 weeks
-
4°C, soluble form, loses part of activity in few days, after 2 weeks 1/4 of original activity observed
-
4°C, sonicated mitochondria, stable
-
-30°C, extract precipitate stable, solution less stable, DEAE fraction unstable
-
-30°C, preserved by Tween 80, conservation of activity
-
-80°C, purified, 200 mM sodium phosphate buffer, pH 8.0, 0.2 mM 11-deoxycortisol, 20% glycerol, 0.1 mM GSH, 0.1% sodium cholate, several days without loss of activity
-
0°C, preserved by Tween 80, conservation of activity
-
2°C, crude extract loses 50% activity in 24 h
-
purified or partially purified enzyme unstable during storage
-
blood samples, 4°C
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme by anion exchange and hydrophobic interaction chromatography, and two additonal steps of anion exchange chromatography
-
ammonium sulfate precipitation, octyl-Sepharose adsorption with cholate and phosphotidylcholine extraction
-
copurification of 11beta-/18-hydroxylase with 11beta-/19-hydroxylase, cholate extraction
-
copurification of 11beta-/18-hydroxylase, cholate extraction, ammonium sulfate precipitation, Tween extraction, octymine-Sepharose
-
copurification of 11beta-hydroxylase with 18-hydroxylase, ammonium sulfate, DEAE-chromatography
-
copurification of P-450 11beta-2 and 11beta-3, ammonium sulfate precipitation, octyl-Sepharose, separation of 2 isoforms by hydroxyapatite column connected to an FPLC system
-
Na-cholate extraction, ammonium sulfate precipitation, aniline-Sepharose chromatography, hydroxylapatite HPLC
-
RP HPLC for detection of photolabeled peptide after digest with TPCK-treated trypsin of purified cytochrome P-45011beta, which is photolabeled with radioactive methyltrienolone
-
sonication, acetone and butanol extraction, Triton extraction
-
ultracentrifugation, ammonium sulfate precipitation, omega-aminooctyl-Sepharose, adrenodoxin-Sepharose, no glycerol used
-
without ionic detergents, ammonium sulfate fractionation, hexyl agarose
-
ammonium sulfate fractionation, ion-exchange chromatography
-
Triton X-100, sodium cholate, column chromatographies
-
recombinant C-terminally His6-tagged CYP11B2 from Escherichia coli by nickel affinity chromatography and anion and cation exchange chromatography
-
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; recombinant mature form of C-terminally His6-tagged CYP11B2 from Escherichia coli strain JM109 by nickel affinity and cation exchange chromatography to homogeneity
-
cholate extraction, hydroxyapatite HPLC
-
octyl-Sepharose chromatography, cholate extraction
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 P-45011beta cDNAs, pc P-450 11beta-3 and -2, cloned into and expressed in COS-7 cells
-
gene cyp11b, sequence comparison and expression analysis
A1XRK1
gene CYP11B, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic tree, expression analysis
-
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 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 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 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
-
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
P15538
overexpressed in V79-4 Chinese hamster lung cell line; overexpressed in V79-4 Chinese hamster lung cell line
-
stable expression of human CYP11B2 or CYP11B1 enzymes in V79 Chinese hamster cells
-
expressed in Escherichia coli
-
two alternative splicing isoforms P450(11beta)-1 and P450(11beta)-2 cDNAs are cloned
-
cDNA transfected into COS-7 cells simultaneously with bovine adrenodoxin cDNA expression plasmid
-
P-450(11beta,aldo) expressed in COS-7 cells
-
CYP11B3 enzyme cDNA cloned into and expressed in COS-7 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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
P15538
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
-
naturally occuring missense mutations involved in development of congenital adrenal hyperplasia due to enzyme deficiency, the L299P mutation causes a change in the position of the I helix relative to the heme group, multisteroid analysis and phenotype, overview, the mutant enzymes shows 1.2% of wild-type activity with 11-deoxycortisol
L299P
-
naturally occuring mutation in a consanguineous Turkish family, phenotype with complete external virilization, borderline elevated blood pressure, and genital alterations, overview
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
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
-
isolation and analysis of the narurally occuring mutation in gene CYP11B1 and mutation frequency in congenital adrenal hyperplasia in Moroccan Jews, the mutation is restricted to one family, phenotype, overview
R448C
-
naturally occuring mutation, cytogenetic analysis and phenotyping, overview
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
-
naturally occuring missense mutations involved in development of congenital adrenal hyperplasia due to enzyme deficiency, the W116C mutation influences the conformational change of the 11-hydroxylase protein necessary for substrate access and product release, multisteroid analysis and phenotype, overview, the mutant enzymes shows 2.9% of wild-type activity with 11-deoxycortisol
W116C
-
a naturally occuring mutation leading to enzyme deficiency, which causes decreased cortisol secretion, elevated plasma levels of ACTH, and accumulation of steroid precursors. These are shunted into the androgen synthesis pathway, leading to hyperandrogenism. Accumulation of 11-deoxycorticosterone and its metabolites causes hypertension in about two thirds of patients. Phenotypical expression of classic 11OHD leads to virilization of external genitalia in newborn females and precocious pseudopuberty combined with rapid somatic growth and bone age acceleration, due to reactive androgen overproduction in both sexes,overview
G59S
-
mutation in CYP11B3, 5-6fold reduction of activity
M88I
-
naturally occuring mutation in CYP11B1, the mutant shows 40% of wild-type activity
additional information
-
CYP11B2-CYP11B1 haplotypes associate with decreased 11beta-hydroxylase activity, CwtCG and TconvGTA haplotype genotyping, phenotypes, overview
additional information
-
genetic variation at the locus encompassing 11-beta hydroxylase and aldosterone synthase accounts for heritability in cortisol precursor 11-deoxycortisol urinary metabolite excretion, genotyping, linkages of polymorphisms in CYP11B1, at exon1, intron 3, and exon 8, and CYP11B2, phenotypes, overview
additional information
-
genotyping of 573 members of 105 British Caucasian families, geno- and phenotype, nine diallelic polymorphisms, overview, association between aldosterone production and variation in gene CYP11B1, overview
additional information
-
isolation of a narually occuring in-frame 3-bp deletion, DELTAF438, in the CYP11B gene, that is involved in development of congenital adrenal hyperplasia due to enzyme deficiency, the DELTAF438 mutation results in a steric disarrangement of the heme group relative to the enzyme, the mutant is inactive, phenotype, overview, molecular modeling of insertional and deletion mutations
additional information
-
the -344 T/C promoter polymorphism of CYP11B2 is involved in diabetic nephropathy, analysis of allele and genotype distributions and frequencies of the CYP11B2 -344T/C polymorphism
additional information
-
11beta-hydroxylase deficiency caused by mutations inthe CYP11B1 gene can cause congenital adrenal hyperplasia, identification of mutations involved, biochemical androgen status of a mutant female during pregnancy and after delivery, overview
additional information
-
11beta-hydroxylase deficiency combined with 21-hydroxylase deficiency leads to development of ambiguous genitalia and salt-loss with increased steroid, e.g. 11-deoxycortisol, contents, mutation in 11beta-hydroxylase partially causes congenital adrenal hyperplasia, phenotype, overview
additional information
-
congenital adrenal hyperplasia due to steroid 11beta-hydroxylase deficiency is a genetic disorder of steroidogenesis, transmitted as an autosomal recessive trait. It is associated with low renin hypertension, hypokalemia, hyperandrogenemia and genital ambiguity in affected females, phenotype including female pseudohermaphroditism and partially with hypertension, diagnostic steroid pattern of 11beta-hydroxylase deficiency, overview
additional information
-
determination and analysis of naturally occuring mutant enzyme variants and their phenotypes, construction of chimeric enzymes with 21-hydroxylase, gene CYP11B2, detailed overview
additional information
-
enzyme deficiency leads to hypokalemia and further, when under-treated, to rhabdomyolysis, phenotype, overview
additional information
-
construction of a chimeric mutant from 11beta-hydroxylase CYP11B1 and aldosterone synthase CYP11B2 genes analogously to the naturally occuring mutant resulting from an unequal crossover break point
additional information
-
generation of different enzyme-DHFR fusion constructs, where the full-length DHFR is fused to the N-terminally varying length of enzyme, analysis of subcellular localization after recombinant expression, overview. The rate of enzyme translocation is independent of the targeting sequence
W116G
-
naturally occuring mutation in CYP11B1, inactive or almost inactive mutant
additional information
-
all enzymes with aldosterone synthesis activity have a glycine residue at position 288, in nonaldosterone synthesising P45011beta it is valine or serine
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
inhibitors for P-45011beta, against aldosterone overproduction which leads to oedematous diseases and hypertension
drug development
-
the enzyme is a target for development of selective and potent CYP11B2 inhibitors
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
analysis
-
use of primary culture of hippocampal neurons isolated from fetus as a model system to study the regulation of the enzymes responsible for corticoid synthesis
medicine
-
increased sensitivity of adrenocortical stereoidgenesis to adrenocorticotropic hormone in Milan hypertensive rats, enzyme is not affected
medicine
-
blocking of aldosterone synthesis by mediating aldosterone synthase activity is a possible pharmacological therapy for hypertension
additional information
-
assays can be used for assessing the potency and selectivity of CYP11B2 inhibitors for the treatment of hypertension and heart failure