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Enzyme Nomenclature
Information on EC 1.14.15.5 - corticosterone 18-monooxygenase
for references in articles please use BRENDA:EC1.14.15.5
Word Map on EC 1.14.15.5
- 1.14.15.5
- aldosterone
- steroid
- 18-hydroxycorticosterone
- cyp11b2
- cortisol
-
glomerulosa
- hypoaldosteronism
-
thrive
- zona
-
18-hydroxylation
-
hyperkalemia
-
hyponatremia
-
salt-wasting
- renin
-
18-oxocortisol
-
18-oh-corticosterone
-
fludrocortisone
-
mineralocorticoid
-
18-hydroxycortisol
-
fasciculata
- 11-deoxycorticosterone
-
salt-losing
- deoxycorticosterone
- furosemide
-
p450aldo
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.15.5
-
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RECOMMENDED NAME
GeneOntology No.
corticosterone 18-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
corticosterone + 2 reduced adrenodoxin + O2 + 2 H+ = 18-hydroxycorticosterone + 2 oxidized adrenodoxin + H2O
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
corticosterone,reduced-adrenal-ferredoxin:oxygen oxidoreductase (18-hydroxylating)
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CAS REGISTRY NUMBER
COMMENTARY
37256-75-0
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
catalyzes a hydroxylation at position C11 of the steroid intermediate deoxycorticosterone yielding corticosterone, reaction of EC 1.14.15.4, followed by a hydroxylation at position C18, reaction of EC 1.14.15.5
UniProt
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
additional information
?
-
-
reduced enzyme activity occurs in hyponatremia and hyperkalemia due to an isolated aldosterone biosynthesis defect, the phenotype can be rescued by a fludrocortisone replacement therapy, overview
-
-
-
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
-
-
-
-
?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
-
reaction in the biosynthesis of aldosterone
-
-
?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
-
-
-
-
?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
-
reaction in the biosynthesis of aldosterone
-
-
?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
-
-
-
-
?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
-
-
-
-
?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
-
reaction in the biosynthesis of aldosterone
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
additional information
?
-
-
reduced enzyme activity occurs in hyponatremia and hyperkalemia due to an isolated aldosterone biosynthesis defect, the phenotype can be rescued by a fludrocortisone replacement therapy, overview
-
-
-
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
-
reaction in the biosynthesis of aldosterone
-
-
?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
-
reaction in the biosynthesis of aldosterone
-
-
?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
-
-
-
-
?
corticosterone + reduced adrenal ferredoxin + O2
18-hydroxycorticosterone + oxidized adrenal ferredoxin + H2O
-
reaction in the biosynthesis of aldosterone
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
activation, no activation by NADH, FAD, FMN, cytochrome c, GSH, dehydroascorbate, in vitro best stimulation by NADPH-regenerating system instead of exogenous NADPH
NADPH
-
activation, no activation by NADH, FAD, FMN, cytochrome c, GSH, dehydroascorbate, in vitro best stimulation by NADPH-regenerating system instead of exogenous NADPH
NADPH
-
activation, no activation by NADH, FAD, FMN, cytochrome c, GSH, dehydroascorbate, in vitro best stimulation by NADPH-regenerating system instead of exogenous NADPH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
lyophilization, mitochondria lose 90% activity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
V386A
the combination of the V386A mutation with the variant CYP11B2 173Arg only slightly reduces the 18-hydroxylase and 18-oxidase activity, whereas the V386A mutation with the CYP11B2 173Lys variant almost abolishes the 18-hydroxylation and 18-oxidation. In both cases the 11-hydroxylase activity is not affected
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.15.5)
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