Steroid 11β-hydroxylase

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steroid 11β-monooxygenase
steroid 11β-monooxygenase
Identifiers
EC no.	1.14.15.4
CAS no.	9029-66-7
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

CYP11B1
Identifiers
Aliases	CYP11B1, CPN1, CYP11B, FHI, P450C11, cytochrome P450 family 11 subfamily B member 1
External IDs	OMIM: 610613; MGI: 88584; HomoloGene: 128035; GeneCards: CYP11B1; OMA:CYP11B1 - orthologs
EC number	1.14.15.4
Gene location (Human)
Chr.	Chromosome 8 (human)
End	142,879,846 bp
Gene location (Mouse)
Chr.	Chromosome 15 (mouse)
End	74,728,167 bp
RNA expression pattern
	Top expressed in
	right adrenal cortex; ; left adrenal gland; ; left adrenal cortex; ; testicle; ; pancreatic ductal cell; ; right testis; ; right coronary artery; ; left testis; ; metanephros; ; ectocervix;
	Top expressed in
	adrenal gland; ; lumbar subsegment of spinal cord; ; lumbar spinal ganglion; ; vastus lateralis muscle; ; spermatid; ; carotid body; ; gastrula; ; thoracic diaphragm; ; triceps brachii muscle; ; sternocleidomastoid muscle;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	iron ion binding; corticosterone 18-monooxygenase activity; metal ion binding; monooxygenase activity; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; oxidoreductase activity; steroid 11-beta-monooxygenase activity; heme binding;
Cellular component	membrane; mitochondrial membranes; mitochondrion; mitochondrial inner membrane;
Biological process	glucose homeostasis; lipid metabolism; aldosterone biosynthetic process; cortisol biosynthetic process; regulation of blood pressure; C21-steroid hormone biosynthetic process; cellular response to hormone stimulus; glucocorticoid biosynthetic process; immune response; sterol metabolic process; cellular response to potassium ion; steroid biosynthetic process; steroid metabolic process; cholesterol metabolic process; cellular response to peptide hormone stimulus; cortisol metabolic process;
	Sources:Amigo / QuickGO
Orthologs
	1584
	13072
	ENSG00000160882
	ENSMUSG00000022589
	P15538
	P15539
	NM_000497; NM_001026213
	NM_009991
	NP_000488; NP_001021384
	NP_034121
	Wikidata
View/Edit Human	View/Edit Mouse

Steroid 11β-hydroxylase, also known as steroid 11β-monooxygenase, is a steroid hydroxylase found in the zona glomerulosa and zona fasciculata of the adrenal cortex. Named officially the cytochrome P450 11B1, mitochondrial, it is a protein that in humans is encoded by the CYP11B1 gene.^[5]^[6] The enzyme is involved in the biosynthesis of adrenal corticosteroids^[7] by catalyzing the addition of hydroxyl groups during oxidation reactions.

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000160882 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000022589 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Lifton RP, Dluhy RG, Powers M, Rich GM, Gutkin M, Fallo F, et al. (September 1992). "Hereditary hypertension caused by chimaeric gene duplications and ectopic expression of aldosterone synthase". Nature Genetics. 2 (1): 66–74. doi:10.1038/ng0992-66. hdl:11577/133580. PMID 1303253. S2CID 975796.
^ This article incorporates public domain material from "Entrez Gene: CYP11B1 cytochrome P450, family 11, subfamily B, polypeptide 1". Reference Sequence collection. National Center for Biotechnology Information. Retrieved 30 November 2020. This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the mitochondrial inner membrane and is involved in the conversion of progesterone to cortisol in the adrenal cortex. Mutations in this gene cause congenital adrenal hyperplasia due to 11-beta-hydroxylase deficiency. Transcript variants encoding different isoforms have been noted for this gene. This article incorporates text from this source, which is in the public domain.
^ Zöllner A, Kagawa N, Waterman MR, Nonaka Y, Takio K, Shiro Y, et al. (February 2008). "Purification and functional characterization of human 11beta hydroxylase expressed in Escherichia coli". The FEBS Journal. 275 (4): 799–810. doi:10.1111/j.1742-4658.2008.06253.x. PMID 18215163. S2CID 45997341.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000160882 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000022589 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid1303253-5] Lifton RP, Dluhy RG, Powers M, Rich GM, Gutkin M, Fallo F, et al. (September 1992). "Hereditary hypertension caused by chimaeric gene duplications and ectopic expression of aldosterone synthase". Nature Genetics. 2 (1): 66–74. doi:10.1038/ng0992-66. hdl:11577/133580. PMID 1303253. S2CID 975796.

[entrez-6] This article incorporates public domain material from "Entrez Gene: CYP11B1 cytochrome P450, family 11, subfamily B, polypeptide 1". Reference Sequence collection. National Center for Biotechnology Information. Retrieved 30 November 2020. This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the mitochondrial inner membrane and is involved in the conversion of progesterone to cortisol in the adrenal cortex. Mutations in this gene cause congenital adrenal hyperplasia due to 11-beta-hydroxylase deficiency. Transcript variants encoding different isoforms have been noted for this gene. This article incorporates text from this source, which is in the public domain.

[pmid18215163-7] Zöllner A, Kagawa N, Waterman MR, Nonaka Y, Takio K, Shiro Y, et al. (February 2008). "Purification and functional characterization of human 11beta hydroxylase expressed in Escherichia coli". The FEBS Journal. 275 (4): 799–810. doi:10.1111/j.1742-4658.2008.06253.x. PMID 18215163. S2CID 45997341.

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