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11-deoxy-cortisol + reduced ferredoxin + O2
cortisol + ferredoxin + H2O
-
-
-
-
?
11-deoxycorticosterone + adrenal ferredoxin + H2O
corticosterone + reduced adrenal ferredoxin + O2
-
-
-
-
?
11-deoxycorticosterone + NADPH + O2
18-hydroxycorticosterone + NADP+ + H2O
-
-
-
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + 2 H+ + 2 O2
aldosterone + oxidized adrenal ferredoxin + 2 H2O
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
?
-
-
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
11-deoxycorticosterone + reduced adrenodoxin + O2
corticosterone + oxidized adrenodoxin + H2O
11-deoxycortisol + adrenal ferredoxin + H2O
cortisol + reduced adrenal ferredoxin + O2
-
-
-
-
?
11-deoxycortisol + NADPH + O2
cortisol + NADP+ + H2O
-
-
-
-
?
11-deoxycortisol + oxidized adrenodoxin + H2O
cortisol + reduced adrenodoxin + O2
-
-
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
14alpha-hydroxy-11-deoxycortisol + oxidized adrenal ferredoxin + H2O
-
14alpha-hydroxylase activity
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + oxidized adrenal ferredoxin + H2O
11-deoxycortisol + reduced adrenodoxin + O2
cortisol + oxidized adrenodoxin + H2O
-
-
-
?
16,17alpha-epoxyprogesterone + reduced adrenal ferredoxin + O2
11beta-hydroxy-16,17alpha-epoxyprogesterone + adrenal ferredoxin + H2O
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
-
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
-
i.e. Reichstein's compound, inducer
25%, 14alpha hydroxylation
?
18-hydroxy-corticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
-
18-hydroxylation, last 3 steps of pathway for aldosterone biosynthesis
-
?
18-hydroxycorticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
18-hydroxycorticosterone + reduced adrenodoxin + O2
aldosterone + oxidized adrenodoxin + H2O
-
-
-
?
18-hydroxycorticosterone + reduced ferredoxin + O2
aldosterone + ferredoxin + H2O
19-hydroxy-11-deoxycorticosterone + reduced adrenal ferredoxin + O2
19-oxo-11-deoxycorticosterone + oxidized adrenal ferredoxin + H2O
-
-
-
?
4-androstene-3,17-dione + reduced adrenal ferredoxin + O2
11beta-hydroxy-4-androstene-3,17-dione + oxidized adrenal ferredoxin + H2O
-
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
-
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
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
a steroid + reduced adrenodoxin + O2
an 11beta-hydroxysteroid + oxidized adrenodoxin + H2O
-
-
-
-
?
androstendione + reduced adrenodoxin + O2
? + oxidized adrenodoxin + H2O
corticosterone + reduced adrenal ferredoxin + O2
11-deoxycorticosterone + adrenal ferredoxin + ?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxy-11-deoxycorticosterone + oxidized adrenal ferredoxin + ?
-
addition of adrenodoxin and adrenodoxin reductase
-
?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxy-corticosterone + oxidized adrenal ferredoxin + H2O
-
18-hydroxylation, last 3 steps of pathway for aldosterone biosynthesis
-
?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
corticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
corticosterone + reduced adrenodoxin + O2
18-hydroxycorticosterone + oxidized adrenodoxin + H2O
cortisol + reduced adrenal ferredoxin + O2
11-deoxycortisol + adrenal ferredoxin + ?
cortisol + reduced adrenal ferredoxin + O2
cortisone + oxidized adrenal ferredoxin + ?
-
-
-
?
deoxycorticosterone + oxidized adrenodoxin + H2O
corticosterone + reduced adrenodoxin + O2
-
-
-
?
metyrapone + ?
metyrapol + ?
-
plasma, product-stereoselective reductive metabolism
enantiomers
r
progesterone + reduced adrenodoxin + O2
11beta-hydroxyprogesterone + oxidized adrenodoxin + H2O
testosterone + reduced adrenal ferredoxin + O2
11beta-hydroxytestosterone + oxidized adrenal ferredoxin + H2O
-
at low rate
-
-
?
testosterone + reduced adrenodoxin + O2
11-hydroxytestosterone + oxidized adrenodoxin + H2O
additional information
?
-
11-deoxycorticosterone + reduced adrenal ferredoxin + 2 H+ + 2 O2
aldosterone + oxidized adrenal ferredoxin + 2 H2O
-
-
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + 2 H+ + 2 O2
aldosterone + oxidized adrenal ferredoxin + 2 H2O
-
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
-
11beta-/18-hydroxylation
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + 2 H+ + 2 O2
aldosterone + oxidized adrenal ferredoxin + 2 H2O
-
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
-
3 step 11beta-/18-hydroxylation to aldosterone
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + 2 H+ + 2 O2
aldosterone + oxidized adrenal ferredoxin + 2 H2O
-
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
-
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
product of 49 kDa protein
?
11-deoxycorticosterone + reduced adrenal ferredoxin + 2 H+ + 2 O2
aldosterone + oxidized adrenal ferredoxin + 2 H2O
-
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
-
by 49.5 kDa protein from capsular portion, 11beta-/18-hydroxylation by 51.5 kDa protein
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + 2 H+ + 2 O2
aldosterone + oxidized adrenal ferredoxin + 2 H2O
-
supported by adrenodoxin and adrenodoxin reductase, 3 step-hydroxylation with corticosterone and 18-hydroxycorticosterone as intermediates, 11beta-/18-hydroxylase
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
-
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
-
11beta-hydroxylation
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
-
11beta-hydroxylation
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
-
11beta-hydroxylation
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
-
11beta-hydroxylation
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
-
addition of adrenodoxin and adrenodoxin reductase
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
-
addition of adrenodoxin and adrenodoxin reductase
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
-
11beta-hydroxylation
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
-
11beta-hydroxylation
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
-
11beta-hydroxylation, last 3 steps of pathway for aldosterone biosynthesis
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
-
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
-
18-/11beta-hydroxylation
-
?
11-deoxycorticosterone + reduced adrenal ferredoxin + O2
corticosterone + oxidized adrenal ferredoxin + H2O
-
adrenal
-
?
11-deoxycorticosterone + reduced adrenodoxin + O2
corticosterone + oxidized adrenodoxin + H2O
-
-
-
?
11-deoxycorticosterone + reduced adrenodoxin + O2
corticosterone + oxidized adrenodoxin + H2O
-
-
-
?
11-deoxycorticosterone + reduced adrenodoxin + O2
corticosterone + oxidized adrenodoxin + H2O
i.e. 21-hydroxyprogesterone
-
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + oxidized adrenal ferredoxin + H2O
-
cytochrome P-45011beta-linked monoxygenase
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + oxidized adrenal ferredoxin + H2O
-
11beta-hydroxylase activity
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + oxidized adrenal ferredoxin + H2O
-
-
-
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + oxidized adrenal ferredoxin + H2O
-
-
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + oxidized adrenal ferredoxin + H2O
-
11beta-hydroxylation
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + oxidized adrenal ferredoxin + H2O
-
CYP11B1
-
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + oxidized adrenal ferredoxin + H2O
CYP11B1
-
-
?
11-deoxycortisol + reduced adrenal ferredoxin + O2
cortisol + oxidized adrenal ferredoxin + H2O
-
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
-
-
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
-
assay optimization
-
-
?
16,17alpha-epoxyprogesterone + reduced adrenal ferredoxin + O2
11beta-hydroxy-16,17alpha-epoxyprogesterone + adrenal ferredoxin + H2O
-
-
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
-
assay optimization
-
-
?
18-hydroxycorticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
-
-
-
?
18-hydroxycorticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
-
-
18-hydroxylation
?
18-hydroxycorticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
-
-
-
-
?
18-hydroxycorticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
-
-
-
?
18-hydroxycorticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
-
CYP11B2
-
-
?
18-hydroxycorticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
-
-
18-hydroxylation, aldosterone production exclusively in the zona glomerulosa
?
18-hydroxycorticosterone + reduced ferredoxin + O2
aldosterone + ferredoxin + H2O
-
-
-
-
?
18-hydroxycorticosterone + reduced ferredoxin + O2
aldosterone + ferredoxin + H2O
-
aldosterone is one of the main effectors of the reninangiotensinaldosterone system, RAAS, regulating salt and water homeostasis and thereby also blood pressure
-
-
?
18-hydroxycorticosterone + reduced ferredoxin + O2
aldosterone + ferredoxin + H2O
-
-
-
-
?
4-pregnen-21-ol-3,20-dione + reduced adrenal ferredoxin + O2
4-pregnene-11,21-diol-3,20-dione + oxidized adrenal ferredoxin + H2O
-
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
-
11-hydroxylation
-
?
4-pregnen-21-ol-3,20-dione + reduced adrenal ferredoxin + O2
4-pregnene-11,21-diol-3,20-dione + oxidized adrenal ferredoxin + H2O
-
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
-
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
-
11-hydroxylation
-
?
androstendione + reduced adrenodoxin + O2
? + oxidized adrenodoxin + H2O
low activity with isozyme CYP11B1
-
-
?
androstendione + reduced adrenodoxin + O2
? + oxidized adrenodoxin + H2O
low activity with isozyme CYP11B2
-
-
?
corticosterone + reduced adrenal ferredoxin + O2
11-deoxycorticosterone + adrenal ferredoxin + ?
-
-
-
?
corticosterone + reduced adrenal ferredoxin + O2
11-deoxycorticosterone + adrenal ferredoxin + ?
-
-
-
-
?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
-
addition of adrenodoxin and adrenodoxin reductase
-
?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
-
18-hydroxylation
-
?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
-
18-hydroxylation
-
?
corticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
-
18-hydroxylation
-
?
corticosterone + reduced adrenal ferredoxin + O2
aldosterone + oxidized adrenal ferredoxin + H2O
-
18-hydroxycorticosterone as intermediate of 11beta-hydroxylation
-
?
corticosterone + reduced adrenodoxin + O2
18-hydroxycorticosterone + oxidized adrenodoxin + H2O
-
-
-
?
corticosterone + reduced adrenodoxin + O2
18-hydroxycorticosterone + oxidized adrenodoxin + H2O
-
-
-
?
cortisol + reduced adrenal ferredoxin + O2
11-deoxycortisol + adrenal ferredoxin + ?
-
-
-
-
?
cortisol + reduced adrenal ferredoxin + O2
11-deoxycortisol + adrenal ferredoxin + ?
-
in the adrenal zona fasciculata
-
-
?
progesterone + reduced adrenodoxin + O2
11beta-hydroxyprogesterone + oxidized adrenodoxin + H2O
low activity with isozyme CYP11B1
-
-
?
progesterone + reduced adrenodoxin + O2
11beta-hydroxyprogesterone + oxidized adrenodoxin + H2O
low activity with isozyme CYP11B2
-
-
?
testosterone + reduced adrenodoxin + O2
11-hydroxytestosterone + oxidized adrenodoxin + H2O
low activity with isozyme CYP11B1
-
-
?
testosterone + reduced adrenodoxin + O2
11-hydroxytestosterone + oxidized adrenodoxin + H2O
low activity with isozyme CYP11B2
-
-
?
additional information
?
-
-
the enzyme is involved in sex differentiation in the protandrous anemonefish, overview
-
-
?
additional information
?
-
-
corticosterone generally believed to be preferred substrate for 18-hydroxylase
-
-
?
additional information
?
-
-
corticosterone normal substrate in vivo
-
-
?
additional information
?
-
the enzyme is involved in gonadal transformation in the zebrafish, enzyme expression regulation, overview
-
-
?
additional information
?
-
-
the enzyme is involved in gonadal transformation in the zebrafish, enzyme expression regulation, 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
?
-
-
-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
?
-
-
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
?
-
-
the enzyme 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
?
-
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
?
-
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
?
-
-
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
?
-
-
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
?
-
-
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the concomitant down-regulation of P450arom and up-regulation of P45011beta are of pivotal importance to the sex change
-
-
?
additional information
?
-
-
the concomitant down-regulation of P450arom and up-regulation of P45011beta are of pivotal importance to the sex change
-
-
?
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
-
-
?
additional information
?
-
-
responsible for the last step of glucocorticoid biosynthesis in the adrenal cortices of many kinds of animals
-
-
?
additional information
?
-
-
androgen production of male animal is partially regulated by changes in abundance of enzyme mRNA
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(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-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
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
-
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
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%
erythromycin
-
potent inhibition of CYP11B2, recombinant enzyme
ethanol
-
10%, v/v, complete inhibition of hydroxylation
FAD286
-
inhibitor of 11-beta-hydroxylase CYP11B1
HgCl2
-
0.2 mM, 50% inhibition
iron-sulfur protein
-
adrenodoxin, at high concentrations, 25% inhibition
-
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
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
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
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
sulfhydryl reagents
-
strongly
testosterone
-
potent inhibition of CYP11B2, recombinant enzyme
[3-(1H-imidazol-1-ylmethyl)phenyl]methanol
-
-
[4-(1H-imidazol-1-ylmethyl)phenyl]methanol
-
-
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-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
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
-
CO
-
-
CO
-
affects 11beta-/19-hydroxylase reaction
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
ketoconazole
-
-
ketoconazole
-
azole derivative, antimycotic drug, strong dose-dependent inhibition
ketoconazole
-
50% inhibition at 0.081 mM
ketoconazole
-
CYP11B2 IC50: 81 nM, CYP11B1 IC50: 224 nM, recombinant enzymes
Metyrapone
-
competitive substrate inhibition
Metyrapone
-
competitive with substrate, affects strongly 11beta-/18-hydroxylation and 11beta-/19-hydroxylation
Metyrapone
-
diagnostic inhibitor, strong inhibition, 0.02 mM complete inhibition
Metyrapone
-
79% inhibition of CYP11B2 at 0.5 mM, 94% inhibition of CYP11B2
Metyrapone
-
11beta-hydroxylase, 39.7% inhibition by 0.4 mM
Metyrapone
-
inhibition of the purified 11beta-hydroxylase, 18-hydroxylation and aldosterone synthesis of corticosterone are inhibited
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
-
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
structure homology modelling for inhibitor design, overview
-
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
-
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
-
dexamethasone represses the enzyme in nervous system tissues, overview
-
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0.0000024
(1R)-2-[2-[(1S)-1-(4-chlorophenyl)ethyl]-3,3-dioxido-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazin-4-yl]-1-phenylethanol
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000003
(1S)-2-[2-[(1S)-1-(4-chlorophenyl)ethyl]-3,3-dioxido-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazin-4-yl]-1-phenylethanol
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000016 - 0.0000099
(R)-4-(5,6,7,8-tetrahydroimidazo[1,5-a]pyridin-5-yl)benzonitrile
0.000448
1-(1H-inden-2-yl)-1H-imidazole
Homo sapiens
-
CYP11B2 IC50: 448 nM, no inhibition of CYP11B1, recombinant enzymes
0.000334 - 0.000639
1-(3,4-dihydronaphthalen-2-yl)-1H-imidazole
0.000143 - 0.000365
1-(3-bromobenzyl)-1H-imidazole
0.000151 - 0.000457
1-(3-chlorobenzyl)-1H-imidazole
0.001
1-(3-cyanobenzyl)-1H-imidazole
0.000206 - 0.000815
1-(3-fluorobenzyl)-1H-imidazole
0.000236 - 0.001
1-(4-aminobenzyl)-1H-imidazole
0.000211 - 0.000479
1-(4-bromobenzyl)-1H-imidazole
0.0000051 - 0.000007
1-(4-bromobenzyl)-5-phenyl-1H-imidazole
0.001
1-(4-chlorobenzyl)-1H-imidazole
0.0000058 - 0.000025
1-(4-chlorobenzyl)-5-phenyl-1H-imidazole
0.000368 - 0.000372
1-(4-cyanobenzyl)-1H-imidazole
0.0000023 - 0.00002
1-(4-cyanobenzyl)-5-(2-fluorophenyl)-1H-imidazole
0.0000037 - 0.0000057
1-(4-cyanobenzyl)-5-(2-methylphenyl)-1H-imidazole
0.0000055 - 0.000032
1-(4-cyanobenzyl)-5-(3-fluorophenyl)-1H-imidazole
0.0000052 - 0.0000062
1-(4-cyanobenzyl)-5-(3-methylphenyl)-1H-imidazole
0.000025 - 0.000027
1-(4-cyanobenzyl)-5-(4-fluorophenyl)-1H-imidazole
0.000117 - 0.00013
1-(4-cyanobenzyl)-5-(4-methylphenyl)-1H-imidazole
0.000307 - 0.000407
1-(4-cyanobenzyl)-5-(4-pyridyl)-1H-imidazole
0.000007 - 0.000048
1-(4-cyanobenzyl)-5-(methyl carboxylate)-1H-imidazole
0.000044 - 0.000213
1-(4-cyanobenzyl)-5-(methylene-acetate)-1H-imidazole
0.000023 - 0.000073
1-(4-cyanobenzyl)-5-bromo-1H-imidazole
0.000062 - 0.000478
1-(4-cyanobenzyl)-5-formyl-1H-imidazole
0.000029 - 0.000285
1-(4-cyanobenzyl)-5-hydroxymethyl-1H-imidazole
0.000012 - 0.000141
1-(4-cyanobenzyl)-5-methyl-1H-imidazole
0.0000017 - 0.000028
1-(4-cyanobenzyl)-5-phenyl-1H-imidazole
0.00033 - 0.001799
1-(4-fluorobenzyl)-1H-imidazole
0.000011 - 0.000016
1-(4-fluorobenzyl)-5-phenyl-1H-imidazole
0.000011 - 0.000014
1-(4-methoxybenzyl)-5-phenyl-1H-imidazole
0.000411 - 0.000763
1-(6-methoxy-3,4-dihydronaphthalen-2-yl)-1H-imidazole
0.0000048 - 0.000011
1-benzyl-5-phenyl-1H-imidazole
0.0000161 - 0.000166
2,4,5-trifluoro-N-(pyridin-3-yl)benzamide
0.0000052
2-(4-chlorobenzyl)-4-(2-methylpropyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000186
2-benzyl-4-(2-methylpropyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000094
2-[(1R)-1-(4-chlorophenyl)ethyl]-4-(2-methylpropyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000617
2-[(1S)-1-(4-chlorophenyl)ethyl]-4-(2-methylpropyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000007
2-[(1S)-1-(4-chlorophenyl)ethyl]-4-(3-methoxy-2-methylpropyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000013
2-[(1S)-1-(4-chlorophenyl)ethyl]-4-(cyclopropylmethyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000078
2-[(1S)-1-(4-chlorophenyl)ethyl]-4-[(3-methyloxetan-3-yl)methyl]-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000008
2-[(1S)-1-(4-chlorophenyl)ethyl]-4-[(propan-2-yloxy)methyl]-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000059 - 0.0000535
3,4-difluoro-N-(pyridin-3-yl)benzamide
0.000181 - 0.000286
3-(1-benzyl-1H-imidazol-5-yl)-1-propanol
0.00003 - 0.002117
3-(1-ethyl-3,4-dihydronaphthalen-2-yl)-pyridine
0.000007 - 0.001268
3-(1-methyl-3,4-dihydronaphthalen-2-yl)-pyridine
0.00039 - 0.0006
3-(1H-imidazol-1-ylmethyl)aniline
0.000007 - 0.001729
3-(3,4-dihydronaphthalen-2-yl)pyridine
0.000005 - 0.000503
3-(3-methyl-3,4-dihydronaphthalen-2-yl)pyridine
0.000176 - 0.001615
3-(4-ethyl-3,4-dihydronaphthalen-2-yl)pyridine
0.000013 - 0.001291
3-(4-methyl-3,4-dihydronaphthalen-2-yl)pyridine
0.000004 - 0.005684
3-(6-methoxy-1H-inden-2-yl)pyridine
0.000002 - 0.000578
3-(6-methoxy-3,4-dihydronaphthalen-2-yl)pyridine
0.000045
3-(7-methoxy-3,4-dihydronaphthalen-2-yl)pyridine
Homo sapiens
-
CYP11B2 IC50: 45 nM, no inhibition of CYP11B1, recombinant enzymes
0.000288 - 0.000735
3-[(Z)-2-phenylvinyl]pyridine
0.0000062 - 0.000018
3-[1-(4-bromobenzyl)-1H-imidazol-5-yl]-1-propanol
0.000044 - 0.000055
3-[1-(4-chlorobenzyl)-1H-imidazol-5-yl]-1-propanol
0.000013 - 0.000048
3-[1-(4-cyanobenzyl)-1H-imidazol-5-yl]-1-propanol
0.000016 - 0.000116
3-[1-(4-fluorobenzyl)-1H-imidazol-5-yl]-1-propanol
0.000012 - 0.000059
3-[1-(4-methoxybenzyl)-1H-imidazol-5-yl]-1-propanol
0.0000114
3-[2-[(1S)-1-(4-chlorophenyl)ethyl]-3,3-dioxido-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazin-4-yl]-2-methylpropan-1-ol
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000005 - 0.0000017
4-((5-phenyl-1H-imidazol-1-yl)methyl)benzonitrile
0.000117
4-(2-methylpropyl)-2-(thiophen-2-ylmethyl)-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000104
4-(2-methylpropyl)-2-[4-(trifluoromethoxy)benzyl]-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000121
4-(2-methylpropyl)-2-[4-(trifluoromethyl)benzyl]-1,2-dihydroimidazo[5,1-d][1,2,5]thiadiazine 3,3-dioxide
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.002529 - 0.002834
4-(6-methoxy-3,4-dihydronaphthalen-2-yl)pyridine
0.000104 - 0.000167
4-bromo-N-(pyridin-3-yl)benzamide
0.0000102 - 0.000065
4-chloro-N-(pyridin-3-yl)benzamide
0.0000075 - 0.000078
4-cyano-N-(pyridin-3-yl)benzamide
0.0000143 - 0.000082
4-fluoro-N-(pyridin-3-yl)benzamide
0.0000248 - 0.000145
4-nitro-N-(pyridin-3-yl)benzamide
0.0000002 - 0.000033
6-(5,8-dihydroisoquinolin-4-yl)-3,4-dihydroquinolin-2(1H)-one
0.000089 - 0.002077
8-(1H-imidazol-1-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.000001 - 0.000158
8-(5-ethoxypyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000044 - 0.001288
8-(5-fluoropyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000043 - 0.002045
8-(5-hydroxypyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000006 - 0.000247
8-(5-methoxypyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000013 - 0.000058
8-(5-phenylpyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]-quinolin-4-one
0.0000002 - 0.000013
8-(isoquinolin-4-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000011 - 0.000715
8-(pyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000012 - 0.000333
8-(pyridin-3-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinoline-4-thione
0.000056 - 0.02855
8-(pyrimidin-5-yl)-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000036 - 0.000183
8-[5-(2,5-difluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000007 - 0.000043
8-[5-(2-fluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000024 - 0.000128
8-[5-(2-methoxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000023 - 0.000496
8-[5-(3,4-difluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.000018 - 0.001748
8-[5-(3,5-difluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000014 - 0.00049
8-[5-(3-fluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000012 - 0.000044
8-[5-(3-hydroxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000046 - 0.001374
8-[5-(3-methoxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000009 - 0.00004
8-[5-(4-fluorophenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000014 - 0.000021
8-[5-(4-methoxyphenyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000022 - 0.000103
8-[5-(propan-2-yloxy)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000059 - 0.000141
8-[5-(trifluoromethyl)pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.000016 - 0.002058
8-[5-[3-(trifluoromethoxy)phenyl]pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.000033 - 0.004646
8-[5-[3-(trifluoromethyl)phenyl]pyridin-3-yl]-1,2,5,6-tetrahydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
0.0000009 - 0.000545
9-(5-methoxypyridin-3-yl)-2,3,6,7-tetrahydro-1H,5H-pyrido[3,2,1-ij]quinolin-5-one
0.0000024 - 0.002296
9-(pyridin-3-yl)-1,2,6,7-tetrahydro-5H-pyrido[ 3,2,1-ij]quinolin-3-one
0.0000002 - 0.000034
9-[6-(isoquinolin-4-yl)pyridin-3-yl]-2,3,6,7-tetrahydro-1H,5H-pyrido[3,2,1-ij]quinolin-5-one
0.000001 - 0.00001
fadrozole
0.000081 - 0.000224
ketoconazole
0.000193 - 0.000326
methyl 3-(1-benzyl-1H-imidazol-5-yl)-propanoate
0.000004 - 0.000057
methyl 3-[1-(4-bromobenzyl)-1H-imidazol-5-yl]-propanoate
0.000123 - 0.000177
methyl 3-[1-(4-chlorobenzyl)-1H-imidazol-5-yl]-propanoate
0.0000035 - 0.000031
methyl 3-[1-(4-cyanobenzyl)-1H-imidazol-5-yl]-propanoate
0.00005 - 0.000104
methyl 3-[1-(4-fluorobenzyl)-1H-imidazol-5-yl]-propanoate
0.000111 - 0.000121
methyl 3-[1-(4-methoxybenzyl)-1H-imidazol-5-yl]-propanoate
0.0000146 - 0.000072
Metyrapone
0.000006 - 0.000119
R-fadrozole
0.00004 - 0.000171
S-fadrozole
0.000206 - 0.001174
[3-(1H-imidazol-1-ylmethyl)phenyl]methanol
0.000695 - 0.001
[4-(1H-imidazol-1-ylmethyl)phenyl]methanol
0.0001
additional information
Homo sapiens
-
development and analysis of inhibitory potency of diverse inhibitors by superimposition of active and non-active compounds, modelling based on two pyridyl substituted acenaphthene derivatives, IC50 values of good inhibitors below 100 nM and of weak inhibi
-
0.0000016
(R)-4-(5,6,7,8-tetrahydroimidazo[1,5-a]pyridin-5-yl)benzonitrile
Homo sapiens
competitive inhibition, pH 7.4
0.0000099
(R)-4-(5,6,7,8-tetrahydroimidazo[1,5-a]pyridin-5-yl)benzonitrile
Homo sapiens
competitive inhibition, pH 7.4, 25°C
0.000334
1-(3,4-dihydronaphthalen-2-yl)-1H-imidazole
Homo sapiens
-
CYP11B2 IC50: 334 nM, recombinant enzymes
0.000639
1-(3,4-dihydronaphthalen-2-yl)-1H-imidazole
Homo sapiens
-
CYP11B1 IC50: 639 nM
0.000143
1-(3-bromobenzyl)-1H-imidazole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000365
1-(3-bromobenzyl)-1H-imidazole
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000151
1-(3-chlorobenzyl)-1H-imidazole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000457
1-(3-chlorobenzyl)-1H-imidazole
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.001
1-(3-cyanobenzyl)-1H-imidazole
Homo sapiens
-
above, inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.001
1-(3-cyanobenzyl)-1H-imidazole
Homo sapiens
-
above, inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000206
1-(3-fluorobenzyl)-1H-imidazole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000815
1-(3-fluorobenzyl)-1H-imidazole
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000236
1-(4-aminobenzyl)-1H-imidazole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.001
1-(4-aminobenzyl)-1H-imidazole
Homo sapiens
-
above, inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000211
1-(4-bromobenzyl)-1H-imidazole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000479
1-(4-bromobenzyl)-1H-imidazole
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000051
1-(4-bromobenzyl)-5-phenyl-1H-imidazole
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000007
1-(4-bromobenzyl)-5-phenyl-1H-imidazole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.001
1-(4-chlorobenzyl)-1H-imidazole
Homo sapiens
-
above, inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.001
1-(4-chlorobenzyl)-1H-imidazole
Homo sapiens
-
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
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000025
1-(4-chlorobenzyl)-5-phenyl-1H-imidazole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000368
1-(4-cyanobenzyl)-1H-imidazole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000372
1-(4-cyanobenzyl)-1H-imidazole
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000023
1-(4-cyanobenzyl)-5-bromo-1H-imidazole
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000073
1-(4-cyanobenzyl)-5-bromo-1H-imidazole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000062
1-(4-cyanobenzyl)-5-formyl-1H-imidazole
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000478
1-(4-cyanobenzyl)-5-formyl-1H-imidazole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000029
1-(4-cyanobenzyl)-5-hydroxymethyl-1H-imidazole
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000285
1-(4-cyanobenzyl)-5-hydroxymethyl-1H-imidazole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000012
1-(4-cyanobenzyl)-5-methyl-1H-imidazole
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000141
1-(4-cyanobenzyl)-5-methyl-1H-imidazole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.0000017
1-(4-cyanobenzyl)-5-phenyl-1H-imidazole
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000028
1-(4-cyanobenzyl)-5-phenyl-1H-imidazole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.00033
1-(4-fluorobenzyl)-1H-imidazole
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000494
1-(4-fluorobenzyl)-1H-imidazole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000709
1-(4-fluorobenzyl)-1H-imidazole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.001799
1-(4-fluorobenzyl)-1H-imidazole
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000011
1-(4-fluorobenzyl)-5-phenyl-1H-imidazole
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000016
1-(4-fluorobenzyl)-5-phenyl-1H-imidazole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000011
1-(4-methoxybenzyl)-5-phenyl-1H-imidazole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000014
1-(4-methoxybenzyl)-5-phenyl-1H-imidazole
Homo sapiens
-
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
Homo sapiens
-
CYP11B2 IC50: 411 nM, recombinant enzymes
0.000763
1-(6-methoxy-3,4-dihydronaphthalen-2-yl)-1H-imidazole
Homo sapiens
-
CYP11B1 IC50: 763 nM
0.0000048
1-benzyl-5-phenyl-1H-imidazole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000011
1-benzyl-5-phenyl-1H-imidazole
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
inhibition of CYP11B2, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.0000059
3,4-difluoro-N-(pyridin-3-yl)benzamide
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
CYP11B2 IC50: 30 nM, recombinant enzymes
0.002117
3-(1-ethyl-3,4-dihydronaphthalen-2-yl)-pyridine
Homo sapiens
-
CYP11B1 IC50: 2117 nM
0.000007
3-(1-methyl-3,4-dihydronaphthalen-2-yl)-pyridine
Homo sapiens
-
CYP11B2 IC50: 7 nM, recombinant enzymes
0.001268
3-(1-methyl-3,4-dihydronaphthalen-2-yl)-pyridine
Homo sapiens
-
CYP11B1 IC50: 1268 nM
0.00039
3-(1H-imidazol-1-ylmethyl)aniline
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.0006
3-(1H-imidazol-1-ylmethyl)aniline
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000007
3-(3,4-dihydronaphthalen-2-yl)pyridine
Homo sapiens
-
CYP11B2 IC50: 7 nM, recombinant enzymes
0.001729
3-(3,4-dihydronaphthalen-2-yl)pyridine
Homo sapiens
-
CYP11B1 IC50: 1729 nM
0.000005
3-(3-methyl-3,4-dihydronaphthalen-2-yl)pyridine
Homo sapiens
-
CYP11B2 IC50: 5 nM, recombinant enzymes
0.000503
3-(3-methyl-3,4-dihydronaphthalen-2-yl)pyridine
Homo sapiens
-
CYP11B1 IC50: 503 nM
0.000176
3-(4-ethyl-3,4-dihydronaphthalen-2-yl)pyridine
Homo sapiens
-
CYP11B2 IC50: 176 nM, recombinant enzymes
0.001615
3-(4-ethyl-3,4-dihydronaphthalen-2-yl)pyridine
Homo sapiens
-
CYP11B1 IC50: 1615 nM
0.000013
3-(4-methyl-3,4-dihydronaphthalen-2-yl)pyridine
Homo sapiens
-
, CYP11B2 IC50: 13 nM, recombinant enzymes
0.001291
3-(4-methyl-3,4-dihydronaphthalen-2-yl)pyridine
Homo sapiens
-
CYP11B1 IC50: 1291 nM
0.000004
3-(6-methoxy-1H-inden-2-yl)pyridine
Homo sapiens
-
CYP11B2 IC50: 4 nM, recombinant enzymes
0.005684
3-(6-methoxy-1H-inden-2-yl)pyridine
Homo sapiens
-
competitive, CYP11B1 IC50: 5684 nM
0.000002
3-(6-methoxy-3,4-dihydronaphthalen-2-yl)pyridine
Homo sapiens
-
CYP11B2 IC50: 2 nM, recombinant enzymes
0.000578
3-(6-methoxy-3,4-dihydronaphthalen-2-yl)pyridine
Homo sapiens
-
competitive, CYP11B1 IC50: 578 nM
0.000288
3-[(Z)-2-phenylvinyl]pyridine
Homo sapiens
-
CYP11B1 IC50: 288 nM
0.000735
3-[(Z)-2-phenylvinyl]pyridine
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
CYP11B1 IC50: 2529 nM
0.002834
4-(6-methoxy-3,4-dihydronaphthalen-2-yl)pyridine
Homo sapiens
-
CYP11B2 IC50: 2834 nM, recombinant enzymes
0.000104
4-bromo-N-(pyridin-3-yl)benzamide
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000001
fadrozole
Homo sapiens
-
CYP11B2 IC50: 1 nM
0.00001
fadrozole
Homo sapiens
-
CYP11B1 IC50: 10 nM, recombinant enzymes
0.000081
ketoconazole
Homo sapiens
-
CYP11B2 IC50: 81 nM
0.000224
ketoconazole
Homo sapiens
-
IC50 CYP11B1 IC50: 224 nM, recombinant enzymes
0.000193
methyl 3-(1-benzyl-1H-imidazol-5-yl)-propanoate
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.0000146
Metyrapone
Homo sapiens
-
inhibition of CYP11B1, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.000072
Metyrapone
Homo sapiens
-
inhibition of CYP11B2, substrate 11-deoxycorticosterone, pH not specified in the publication, temperature not specified in the publication
0.000006
R-fadrozole
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000119
R-fadrozole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.00004
S-fadrozole
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.000171
S-fadrozole
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000206
[3-(1H-imidazol-1-ylmethyl)phenyl]methanol
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.001174
[3-(1H-imidazol-1-ylmethyl)phenyl]methanol
Homo sapiens
-
inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
0.000695
[4-(1H-imidazol-1-ylmethyl)phenyl]methanol
Homo sapiens
-
inhibition of CYP11B1, pH not specified in the publication, temperature not specified in the publication
0.001
[4-(1H-imidazol-1-ylmethyl)phenyl]methanol
Homo sapiens
-
above, inhibition of CYP11B2, pH not specified in the publication, temperature not specified in the publication
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Tomkins, G.M.; Michael, P.J.; Curran, J.F.
Studies on the nature of steroid 11-beta hydroxylation
Biochim. Biophys. Acta
23
655-656
1957
Bos taurus, Oryctolagus cuniculus
brenda
Grant, J.K.; Brownie, A.C.
The role of fumarate and TPN in steroid enzymic 11beta-hydroxylation
Biochim. Biophys. Acta
18
433-434
1955
Bos taurus
brenda
Zuidweg, M.H.J.
Hydroxylation of Reichstein's compound S with cell-free preparations from Curvularia lunata
Biochim. Biophys. Acta
152
144-158
1968
Curvularia lunata
brenda
Watanuki, M.; Tilley, B.E.; Hall, P.F.
Purification and properties of cytochrome p-450 (11beta- and 18-hydroxylase) from bovine adrenocortical mitochondria
Biochim. Biophys. Acta
483
236-247
1977
Bos taurus
brenda
Watanuki, M.; Tilley, B.E.; Hall, P.F.
Cytochrome P-450 for 11beta- and 18-hydroxylase activities of bovine adrenocortical mitochondria: one enzyme or two?
Biochemistry
17
127-130
1978
Bos taurus
brenda
Sato, H.; Ashida, N.; Suhara, K.; Itagaki, E.; Takemori, S.; Katagiri, M.
Properties of an adrenal cytochrome P-450 (P-45011beta) for the hydroxylations of corticosteroids
Arch. Biochem. Biophys.
190
307-314
1978
Bos taurus
brenda
Ogishima, T.; Mitani, F.; Ishimura, Y.
Isolation of aldosterone synthase cytochrome P-450 from zona glomerulosa mitochondria of rat adrenal cortex
J. Biol. Chem.
264
10935-10938
1989
Rattus norvegicus
brenda
Cooper, D.Y.; Schleyer, H.; Levin, S.S.; Rosenthal, O.
Studies on the partially purified heme protein P-450 from the adrenal cortex
Ann. N. Y. Acad. Sci.
212
227-242
1973
Bos taurus
brenda
Lombardo, A.; Defaye, G.; Guidicelli, C.; Monnier, N.; Chambaz, E.M.
Integration of purified adrenocortical cytochrome P-45011beta into phospholipid vesicles
Biochem. Biophys. Res. Commun.
104
1638-1645
1982
Bos taurus
brenda
Yanigabashi, K.; Haniu, M.; Shively, J.E.; Shen, W.H.; Hall, P.
The synthesis of aldosterone by the adrenal cortex. Two zones (fasciculata and glomerulosa) possess one enzyme for 11beta-, 18-hydroxylation, and aldehyde synthesis
J. Biol. Chem.
261
3556-3562
1986
Bos taurus, Sus scrofa
brenda
Ogishima, T.; Mitani, F.; Ishimura, Y
Isolation of two distinct cytochromes P-45011beta with aldosterone synthase activity from bovine adrenocortical mitochondria
J. Biochem.
105
497-499
1989
Bos taurus
brenda
Lauber, M.; Muller, J.
Purification and characterization of two distinct forms of rat adrenal cytochrome P450(11) beta: functional and structural aspects
Arch. Biochem. Biophys.
274
109-119
1989
Rattus norvegicus
brenda
Seybert, D.
Lipid regulation of bovine cytochrome P45011beta activity
Arch. Biochem. Biophys.
279
188-194
1990
Bos taurus
brenda
Tsubaki, M.; Ichikawa, Y.; Fujimoto, Y.; Yu, N.T.; Hori, H.
Active site of bovine adrenocortical cytochrome P-45011beta studied by resonance Raman and electron paramagnetic resonance spectroscopies: distinction from cytochrome P-450scc
Biochemistry
29
8805-8812
1990
Bos taurus
brenda
Yanigabashi, K.; Kobayashi, Y.; Hall, P.F.
Ascorbate as a source of reducing equivalents for the synthesis of aldosterone
Biochem. Biophys. Res. Commun.
170
1256-1262
1990
Bos taurus
brenda
Boon, W.C.; Roche, P.J.; Butkus, A.; McDougall, J.G.; Jeyaseelan, K.; Coghlan, J.P.
Functional and expression analysis of ovine steroid 11beta-hydroxylase (cytochrome P 45011beta)
Endocr. Res.
23
325-347
1997
Ovis aries
brenda
Delorme, C.; Piffeteau, A.; Viger, A.; Marquet, A.
Inhibition of bovine cytochrome P-45011beta by 18-unsaturated progesterone derivatives
Eur. J. Biochem.
232
247-256
1995
Bos taurus
brenda
Delorme, C.; Piffeteau, A.; Sobrio, F.; Marquet, A.
Mechanism-based inactivation of bovine cytochrome P-45011beta by 18-unsaturated progesterone derivatives
Eur. J. Biochem.
248
252-260
1997
Bos taurus
brenda
Davioud, E.; Piffeteau, A.; Delorme, C.; Coustal, S.; Marquet, A.
18-Vinyldeoxycorticosterone: a potent inhibitor of the bovine cytochrome P-45011beta
Bioorg. Med. Chem.
6
1781-1788
1998
Bos taurus
brenda
Ohnishi, T.; Miura, S.; Ichikawa, Y.
Photoaffinity labeling of cytochrome P-45011beta with methyltrienolone as a probe for the substrate binding region
Biochim. Biophys. Acta
1161
257-264
1993
Bos taurus
brenda
Nagamine, S.; Horisaka, E.; Fukuyama, Y.; Maetani, K.; Matsuzawa, R.; Iwakawa, S.; Asada, S.
Stereoselective reductive metabolism of metyrapone and inhibitory activity of metyrapone metabolites, metyrapol enantiomers, on steroid 11beta-hydroxylase in the rat
Biol. Pharm. Bull.
20
188-192
1997
Rattus norvegicus
brenda
Denner, K.; Vogel, R.; Schmalix, W.; Doehmer, J.; Bernhardt, R.
Cloning and stable expression of the human mitochondrial cytochrome P45011B1 cDNA in V79 Chinese hamster cells and their application for testing of potential inhibitors
Pharmacogenetics
5
89-96
1995
Homo sapiens
brenda
Nonaka, Y.; Takemori, H.; Halder, S.K.; Sun, T.; Ohta, M.; Hatano, O.; Takakusu, A.; Okamoto, M.
Frog cytochrome P-450 (11beta,aldo), a single enzyme involved in the final steps of glucocorticoid and mineralocorticoid biosynthesis
Eur. J. Biochem.
229
249-256
1995
Lithobates catesbeianus
brenda
Suzuki, K.; Sanga, K.i.; Chikaoka, Y.; Itagaki, E.
Purification and properties of cytochrome P-450 (P-450lun) catalyzing steroid 11beta-hydroxylation in Curvularia lunata
Biochim. Biophys. Acta
1203
215-223
1993
Curvularia lunata
brenda
Zhou, M.Y.; Gomez-Sanchez, E.P.; Foecking, M.F.; Gomez-Sanchez, C.E.
Cloning and expression of the rat adrenal cytochrome P-450 11B3 (CYP11B3) enzyme cDNA: preferential 18-hydroxylation over 11beta-hydroxylation of DOC
Mol. Cell. Endocrinol.
114
137-145
1995
Rattus norvegicus
brenda
Kuhn-Velten, W.N.
Norharman (beta-carboline) as a potent inhibitory ligand for steroidogenic cytochromes P450 (CYP11 and CYP17)
Eur. J. Pharmacol.
250
R1-3
1993
Rattus norvegicus
brenda
Wang, G.M.; Ge, R.S.; Latif, S.A.; Morris, D.J.; Hardy, M.P.
Expression of 11beta-hydroxylase in rat Leydig cells
Endocrinology
143
621-626
2002
Rattus norvegicus
brenda
Lloyd-MacGilp, S.A.; Torielli, L.; Bechtel, S.; Tripodi, G.; Gomez-Sanchez, C.E.; Zagato, L.; Bernhardt, R.; Kenyon, C.J.
Mutations in aldosterone synthase gene of Milan hypertensive rats: phenotypic consequences
Am. J. Physiol.
282
E608-617
2002
Rattus norvegicus
brenda
Ulmschneider, S.; Muller-Vieira, U.; Klein, C.D.; Antes, I.; Lengauer, T.; Hartmann, R.W.
Synthesis and evaluation of (pyridylmethylene)tetrahydronaphthalenes/-indanes and structurally modified derivatives: potent and selective inhibitors of aldosterone synthase
J. Med. Chem.
48
1563-1575
2005
Homo sapiens
brenda
Ulmschneider, S.; Muller-Vieira, U.; Mitrenga, M.; Hartmann, R.W.; Oberwinkler-Marchais, S.; Klein, C.D.; Bureik, M.; Bernhardt, R.; Antes, I.; Lengauer, T.
Synthesis and evaluation of imidazolylmethylenetetrahydronaphthalenes and imidazolylmethyleneindanes: potent inhibitors of aldosterone synthase
J. Med. Chem.
48
1796-1805
2005
Homo sapiens
brenda
MacKenzie, S.M.; Lai, M.; Clark, C.J.; Fraser, R.; Gomez-Sanchez, C.E.; Seckl, J.R.; Connell, J.M.; Davies, E.
11beta-hydroxylase and aldosterone synthase expression in fetal rat hippocampal neurons
J. Mol. Endocrinol.
29
319-325
2002
Rattus norvegicus
brenda
Kusakabe, M.; Kobayashi, T.; Todo, T.; Mark Lokman, P.; Nagahama, Y.; Young, G.
Molecular cloning and expression during spermatogenesis of a cDNA encoding testicular 11beta-hydroxylase (P45011beta) in rainbow trout (Oncorhynchus mykiss)
Mol. Reprod. Dev.
62
456-469
2002
Oncorhynchus mykiss
brenda
Ulmschneider, S.; Negri, M.; Voets, M.; Hartmann, R.W.
Development and evaluation of a pharmacophore model for inhibitors of aldosterone synthase (CYP11B2)
Bioorg. Med. Chem. Lett.
16
25-30
2006
Homo sapiens
brenda
Lajer, M.; Schjoedt, K.J.; Jacobsen, P.; Tarnow, L.; Parving, H.H.
Aldosterone synthase (CYP11B2) -344T/C polymorphism is not associated with the initiation and progression of diabetic nephropathy in Caucasian Type 1 diabetic patients
Diabet. Med.
23
675-680
2006
Homo sapiens
brenda
Ye, P.; Kenyon, C.J.; MacKenzie, S.M.; Jong, A.S.; Miller, C.; Gray, G.A.; Wallace, A.; Ryding, A.S.; Mullins, J.J.; McBride, M.W.; Graham, D.; Fraser, R.; Connell, J.M.; Davies, E.
The aldosterone synthase (CYP11B2) and 11beta-hydroxylase (CYP11B1) genes are not expressed in the rat heart
Endocrinology
146
5287-5293
2005
Rattus norvegicus
brenda
Lin, T.C.; Chien, S.C.; Hsu, P.C.; Li, L.A.
Mechanistic study of polychlorinated biphenyl 126-induced CYP11B1 and CYP11B2 up-regulation
Endocrinology
147
1536-1544
2006
Homo sapiens
brenda
Kuribayashi, I.; Nomoto, S.; Massa, G.; Oostdijk, W.; Wit, J.M.; Wolffenbuttel, B.H.; Shizuta, Y.; Honke, K.
Steroid 11-beta-hydroxylase deficiency caused by compound heterozygosity for a novel mutation, p.G314R, in one CYP11B1 allele, and a chimeric CYP11B2/CYP11B1 in the other allele
Horm. Res.
63
284-293
2005
Homo sapiens (P15538)
brenda
Peters, C.J.; Nugent, T.; Perry, L.A.; Davies, K.; Morel, Y.; Drake, W.M.; Savage, M.O.; Johnston, L.B.
Cosegregation of a novel homozygous CYP11B1 mutation with the phenotype of non-classical congenital adrenal hyperplasia in a consanguineous family
Horm. Res.
67
189-193
2007
Homo sapiens
brenda
Barr, M.; MacKenzie, S.M.; Friel, E.C.; Holloway, C.D.; Wilkinson, D.M.; Brain, N.J.; Ingram, M.C.; Fraser, R.; Brown, M.; Samani, N.J.; Caulfield, M.; Munroe, P.B.; Farrall, M.; Webster, J.; Clayton, D.; Dominiczak, A.F.; Connell, J.M.; Davies, E.
Polymorphic variation in the 11beta-hydroxylase gene associates with reduced 11-hydroxylase efficiency
Hypertension
49
113-119
2006
Homo sapiens
brenda
Keavney, B.; Mayosi, B.; Gaukrodger, N.; Imrie, H.; Baker, M.; Fraser, R.; Ingram, M.; Watkins, H.; Farrall, M.; Davies, E.; Connell, J.
Genetic variation at the locus encompassing 11-beta hydroxylase and aldosterone synthase accounts for heritability in cortisol precursor (11-deoxycortisol) urinary metabolite excretion
J. Clin. Endocrinol. Metab.
90
1072-1077
2005
Homo sapiens
brenda
Ganapathipillai, S.; Laval, G.; Hoffmann, I.S.; Castejon, A.M.; Nicod, J.; Dick, B.; Frey, F.J.; Frey, B.M.; Cubeddu, L.X.; Ferrari, P.
CYP11B2-CYP11B1 haplotypes associated with decreased 11beta-hydroxylase activity
J. Clin. Endocrinol. Metab.
90
1220-1225
2005
Homo sapiens
brenda
Krone, N.; Riepe, F.G.; Goetze, D.; Korsch, E.; Rister, M.; Commentz, J.; Partsch, C.J.; Groetzinger, J.; Peter, M.; Sippell, W.G.
Congenital adrenal hyperplasia due to 11-hydroxylase deficiency: functional characterization of two novel point mutations and a three-base pair deletion in the CYP11B1 gene
J. Clin. Endocrinol. Metab.
90
3724-3730
2005
Homo sapiens
brenda
Paperna, T.; Gershoni-Baruch, R.; Badarneh, K.; Kasinetz, L.; Hochberg, Z.
Mutations in CYP11B1 and congenital adrenal hyperplasia in Moroccan Jews
J. Clin. Endocrinol. Metab.
90
5463-5465
2005
Homo sapiens
brenda
Imrie, H.; Freel, M.; Mayosi, B.M.; Davies, E.; Fraser, R.; Ingram, M.; Cordell, H.J.; Farrall, M.; Avery, P.J.; Watkins, H.; Keavney, B.; Connell, J.M.
Association between aldosterone production and variation in the 11beta-hydroxylase (CYP11B1) gene
J. Clin. Endocrinol. Metab.
91
5051-5056
2006
Homo sapiens
brenda
Voets, M.; Antes, I.; Scherer, C.; Mueller-Vieira, U.; Biemel, K.; Marchais-Oberwinkler, S.; Hartmann, R.W.
Synthesis and evaluation of heteroaryl-substituted dihydronaphthalenes and indenes: potent and selective inhibitors of aldosterone synthase (CYP11B2) for the treatment of congestive heart failure and myocardial fibrosis
J. Med. Chem.
49
2222-2231
2006
Homo sapiens
brenda
Mueller-Vieira, U.; Angotti, M.; Hartmann, R.W.
The adrenocortical tumor cell line NCI-H295R as an in vitro screening system for the evaluation of CYP11B2 (aldosterone synthase) and CYP11B1 (steroid-11beta-hydroxylase) inhibitors
J. Steroid Biochem. Mol. Biol.
96
259-270
2005
Homo sapiens
brenda
Freel, E.M.; Ingram, M.; Wallace, A.M.; White, A.; Fraser, R.; Davies, E.; Connell, J.M.
Effect of variation in CYP11B1 and CYP11B2 on corticosteroid phenotype and hypothalamic-pituitary-adrenal axis activity in hypertensive and normotensive subjects
Clin. Endocrinol. (Oxf.)
68
700-706
2008
Homo sapiens
brenda
Wang, X.G.; Orban, L.
Anti-Muellerian hormone and 11 beta-hydroxylase show reciprocal expression to that of aromatase in the transforming gonad of zebrafish males
Dev. Dyn.
236
1329-1338
2007
Danio rerio (A1XRK1), Danio rerio
brenda
Chen, K.; Tong, W.; Wei, D.; Jiang, W.
The 11beta-hydroxylation of 16,17alpha-epoxyprogesterone and the purification of the 11beta-hydroxylase from Absidia coerulea IBL02
Enzyme Microb. Technol.
41
71-79
2007
Absidia caerulea, Absidia caerulea IBL02
-
brenda
Zoellner, A.; Kagawa, N.; Waterman, M.R.; Nonaka, Y.; Takio, K.; Shiro, Y.; Hannemann, F.; Bernhardt, R.
Purification and functional characterization of human 11beta hydroxylase expressed in Escherichia coli
FEBS J.
275
799-810
2008
Homo sapiens
brenda
Socorro, S.; Martins, R.S.; Deloffre, L.; Mylonas, C.C.; Canario, A.V.
A cDNA for European sea bass (Dicentrarchus labrax) 11beta-hydroxylase: gene expression during the thermosensitive period and gonadogenesis
Gen. Comp. Endocrinol.
150
164-173
2007
Dicentrarchus labrax
brenda
Simm, P.J.; Zacharin, M.R.
Successful pregnancy in a patient with severe 11-beta-hydroxylase deficiency and novel mutations in CYP11B1 gene
Horm. Res.
68
294-297
2007
Homo sapiens
brenda
Peter, M.; Janzen, N.; Sander, S.; Korsch, E.; Riepe, F.G.; Sander, J.
A case of 11beta-hydroxylase deficiency detected in a newborn screening program by second-tier LC-MS/MS
Horm. Res.
69
253-256
2008
Homo sapiens
brenda
Riedl, S.; Nguyen, H.H.; Clausmeyer, S.; Schulze, E.; Waldhauser, F.; Bernhardt, R.
A homozygous L299P mutation in the CYP11B1 gene leads to complete virilization in 46,XX individuals with 11-beta-hydroxylase deficiency
Horm. Res.
70
145-149
2008
Homo sapiens
brenda
Ye, P.; Kenyon, C.J.; Mackenzie, S.M.; Nichol, K.; Seckl, J.R.; Fraser, R.; Connell, J.M.; Davies, E.
Effects of ACTH, dexamethasone, and adrenalectomy on 11beta-hydroxylase (CYP11B1) and aldosterone synthase (CYP11B2) gene expression in the rat central nervous system
J. Endocrinol.
196
305-311
2008
Rattus norvegicus
brenda
Cingoez, S.; Ozkan, B.; Doeneray, H.; Sakizli, M.
Familial pericentric inversion chromosome 3 and R448C mutation of CYP11B1 gene in Turkish kindred with 11beta-hydroxylase deficiency
J. Endocrinol. Invest.
30
285-291
2007
Homo sapiens
brenda
Tonetto-Fernandes, V.; Lemos-Marini, S.H.; De Mello, M.P.; Ribeiro-Neto, L.M.; Kater, C.E.
21-hydroxylase deficiency transiently mimicking combined 21- and 11beta-hydroxylase deficiency
J. Pediatr. Endocrinol. Metab.
21
487-494
2008
Homo sapiens
brenda
Atabek, M.E.; Pirgon, O.; Sert, A.
Hypokalemic rhabdomyolysis in a child with 11-hydroxylase deficiency
J. Pediatr. Endocrinol. Metab.
21
93-96
2008
Homo sapiens
brenda
Nimkarn, S.; New, M.I.
Steroid 11beta-hydroxylase deficiency congenital adrenal hyperplasia
Trends Endocrinol. Metab.
19
96-99
2008
Homo sapiens
brenda
Zhao, L.Q.; Han, S.; Tian, H.M.
Progress in molecular-genetic studies on congenital adrenal hyperplasia due to 11beta-hydroxylase deficiency
World J. Pediatr.
4
85-90
2008
Homo sapiens
brenda
Miura, S.; Horiguchi, R.; Nakamura, M.
Immunohistochemical evidence for 11beta-hydroxylase (P45011beta) and androgen production in the gonad during sex differentiation and in adults in the protandrous anemonefish Amphiprion clarkii
Zool. Sci.
25
212-219
2008
Amphiprion clarkii
brenda
LaSala, D.; Shibanaka, Y.; Jeng, A.Y.
Coexpression of CYP11B2 or CYP11B1 with adrenodoxin and adrenodoxin reductase for assessing the potency and selectivity of aldosterone synthase inhibitors
Anal. Biochem.
394
56-61
2009
Homo sapiens (P15538), Homo sapiens (P19099), Homo sapiens
brenda
Imachi, H.; Murao, K.; Cao, W.M.; Muraoka, T.; Nishiuchi, T.; Dobashi, H.; Hosomi, N.; Iwama, H.; Ishida, T.
The prolactin regulatory element-binding regulates of the 11beta-hydroxylase gene
Biochem. Biophys. Res. Commun.
376
531-535
2008
Mus musculus
brenda
Liu, J.F.; Guiguen, Y.; Liu, S.J.
Aromatase (P450arom) and 11beta-hydroxylase (P45011beta) genes are differentially expressed during the sex change process of the protogynous rice field eel, Monopterus albus
Fish Physiol. Biochem.
35
511-518
2009
Monopterus albus (Q2I128), Monopterus albus
brenda
Zhang, W.L.; Zhou, L.Y.; Senthilkumaran, B.; Huang, B.F.; Sudhakumari, C.C.; Kobayashi, T.; Nagahama, Y.; Wang, D.S.
Molecular cloning of two isoforms of 11beta-hydroxylase and their expressions in the Nile tilapia, Oreochromis niloticus
Gen. Comp. Endocrinol.
165
34-41
2010
Oreochromis niloticus
brenda
Adams, C.M.; Hu, C.W.; Jeng, A.Y.; Karki, R.; Ksander, G.; Lasala, D.; Leung-Chu, J.; Liang, G.; Liu, Q.; Meredith, E.; Rao, C.; Rigel, D.F.; Shi, J.; Smith, S.; Springer, C.; Zhang, C.
The discovery of potent inhibitors of aldosterone synthase that exhibit selectivity over 11-beta-hydroxylase
Bioorg. Med. Chem. Lett.
20
4324-4327
2010
Homo sapiens
brenda
Zimmer, C.; Hafner, M.; Zender, M.; Ammann, D.; Hartmann, R.W.; Vock, C.A.
N-(Pyridin-3-yl)benzamides as selective inhibitors of human aldosterone synthase (CYP11B2)
Bioorg. Med. Chem. Lett.
21
186-190
2011
Homo sapiens
brenda
Parajes, S.; Loidi, L.; Reisch, N.; Dhir, V.; Rose, I.T.; Hampel, R.; Quinkler, M.; Conway, G.S.; Castro-Feijoo, L.; Araujo-Vilar, D.; Pombo, M.; Dominguez, F.; Williams, E.L.; Cole, T.R.; Kirk, J.M.; Kaminsky, E.; Rumsby, G.; Arlt, W.; Krone, N.
Functional consequences of seven novel mutations in the CYP11B1 gene: four mutations associated with nonclassic and three mutations causing classic 11beta-hydroxylase deficiency
J. Clin. Endocrinol. Metab.
95
779-788
2010
Homo sapiens
brenda
Roumen, L.; Peeters, J.W.; Emmen, J.M.; Beugels, I.P.; Custers, E.M.; de Gooyer, M.; Plate, R.; Pieterse, K.; Hilbers, P.A.; Smits, J.F.; Vekemans, J.A.; Leysen, D.; Ottenheijm, H.C.; Janssen, H.M.; Hermans, J.J.
Synthesis, biological evaluation, and molecular modeling of 1-benzyl-1H-imidazoles as selective inhibitors of aldosterone synthase (CYP11B2)
J. Med. Chem.
53
1712-1725
2010
Homo sapiens
brenda
Lucas, S.; Negri, M.; Heim, R.; Zimmer, C.; Hartmann, R.W.
Fine-tuning the selectivity of aldosterone synthase inhibitors: structure-activity and structure-selectivity insights from studies of heteroaryl substituted 1,2,5,6-tetrahydropyrrolo[3,2,1-ij]quinolin-4-one derivatives
J. Med. Chem.
54
2307-2319
2011
Homo sapiens
brenda
Saha, S.; Bornstein, S.R.; Graessler, J.; Kopprasch, S.
Very-low-density lipoprotein mediates transcriptional regulation of aldosterone synthase in human adrenocortical cells through multiple signaling pathways
Cell Tissue Res.
348
71-80
2012
Homo sapiens
brenda
Hobler, A.; Kagawa, N.; Hutter, M.C.; Hartmann, M.F.; Wudy, S.A.; Hannemann, F.; Bernhardt, R.
Human aldosterone synthase: recombinant expression in E. coli and purification enables a detailed biochemical analysis of the protein on the molecular level
J. Steroid Biochem. Mol. Biol.
132
57-65
2012
Homo sapiens (P19099), Homo sapiens
brenda
Strushkevich, N.; Gilep, A.A.; Shen, L.; Arrowsmith, C.H.; Edwards, A.M.; Usanov, S.A.; Park, H.W.
Structural insights into aldosterone synthase substrate specificity and targeted inhibition
Mol. Endocrinol.
27
315-324
2013
Homo sapiens (P15538), Homo sapiens (P19099), Homo sapiens
brenda
Adams, B.P.; Bose, H.S.
Alteration in accumulated aldosterone synthesis as a result of N-terminal cleavage of aldosterone synthase
Mol. Pharmacol.
81
465-474
2012
Homo sapiens
brenda
Vecchiola, A.; Lagos, C.F.; Fuentes, C.A.; Allende, F.; Campino, C.; Valdivia, C.; Tapia-Castillo, A.; Ogishima, T.; Mukai, K.; Owen, G.; Solari, S.; Carvajal, C.A.; Fardella, C.E.
Different effects of progesterone and estradiol on chimeric and wild type aldosterone synthase in vitro
Reprod. Biol. Endocrinol.
11
76
2013
Homo sapiens
brenda
Neunzig, J.; Khatri, Y.; Bernhardt, R.
The impact of the clinical CYP11B2 mutation V386A strongly depends on the enzymes genetic background
Endocr. J.
64
457-461
2017
Homo sapiens (P19099), Homo sapiens
brenda
van Rooyen, D.; Gent, R.; Barnard, L.; Swart, A.C.
The in vitro metabolism of 11beta-hydroxyprogesterone and 11-ketoprogesterone to 11-ketodihydrotestosterone in the backdoor pathway
J. Steroid Biochem. Mol. Biol.
178
203-212
2018
Homo sapiens (P15538), Homo sapiens (P19099), Homo sapiens
brenda