Aldosterone synthase

CYP11B2
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	4DVQ, 4FDH, 4ZGX
Identifiers
Aliases	CYP11B2, ALDOS, CPN2, CYP11B, CYP11BL, CYPXIB2, P-450C18, P450C18, P450aldo, cytochrome P450 family 11 subfamily B member 2
External IDs	OMIM: 124080; MGI: 88583; HomoloGene: 106948; GeneCards: CYP11B2; OMA:CYP11B2 - orthologs
EC number	1.14.15.4
Gene location (Human)
Chr.	Chromosome 8 (human)
End	142,917,843 bp
Gene location (Mouse)
Chr.	Chromosome 15 (mouse)
End	74,713,492 bp
RNA expression pattern
	Top expressed in
	right adrenal cortex; ; left adrenal gland; ; left adrenal cortex; ; testicle; ; fundus; ; connective tissue; ; adipose tissue; ; heart; ; atrium; ; right atrium;
	Top expressed in
	adrenal gland; ; gastrula; ; decidua; ; belly cord; ; spinal ganglia; ; extraocular muscle; ; upper arm; ; triceps brachii muscle; ; ureter; ; testicle;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	iron ion binding; corticosterone 18-monooxygenase activity; metal ion binding; monooxygenase activity; heme binding; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; oxidoreductase activity; steroid 11-beta-monooxygenase activity; steroid hydroxylase activity;
Cellular component	mitochondrial membranes; membrane; mitochondrion; mitochondrial inner membrane;
Biological process	lipid metabolism; aldosterone biosynthetic process; cortisol biosynthetic process; C21-steroid hormone biosynthetic process; cellular response to hormone stimulus; potassium ion homeostasis; mineralocorticoid biosynthetic process; regulation of blood volume by renal aldosterone; renal water homeostasis; sterol metabolic process; sodium ion homeostasis; cellular response to potassium ion; steroid biosynthetic process; steroid metabolic process; glucocorticoid biosynthetic process; cholesterol metabolic process; cellular response to peptide hormone stimulus; cortisol metabolic process;
	Sources:Amigo / QuickGO
Orthologs
	1585
	110115
	ENSG00000179142
	ENSMUSG00000075604
	P19099
	n/a
	NM_000498
	NM_001033229
	NP_000489
	n/a
	Wikidata
View/Edit Human	View/Edit Mouse

Aldosterone synthase, also called steroid 18-hydroxylase, corticosterone 18-monooxygenase or P450C18, is a steroid hydroxylase cytochrome P450 enzyme involved in the biosynthesis of the mineralocorticoid aldosterone and other steroids. The enzyme catalyzes sequential hydroxylations of the steroid angular methyl group at C18 after initial 11β-hydroxylation (the enzyme has steroid 18-hydroxylase activity as well as steroid 11 beta-hydroxylase activity). It is encoded by the CYP11B2 gene in humans.

Aldosterone synthase is a protein which is only expressed in the zona glomerulosa^[5] of the adrenal cortex and is primarily regulated by the renin–angiotensin system.^[6] It is the sole enzyme capable of synthesizing aldosterone in humans and plays an important role in electrolyte balance and blood pressure.^[7]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000179142 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000075604 – 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.
^ Bassett MH, White PC, Rainey WE (March 2004). "The regulation of aldosterone synthase expression". Molecular and Cellular Endocrinology. 217 (1–2): 67–74. doi:10.1016/j.mce.2003.10.011. PMID 15134803. S2CID 43133280.
^ Peter M, Dubuis JM, Sippell WG (1999). "Disorders of the aldosterone synthase and steroid 11beta-hydroxylase deficiencies". Hormone Research. 51 (5): 211–22. doi:10.1159/000023374 (inactive 10 July 2024). PMID 10559665. S2CID 24182379.{{cite journal}}: CS1 maint: DOI inactive as of July 2024 (link)
^ Strushkevich N, Gilep AA, Shen L, Arrowsmith CH, Edwards AM, Usanov SA, Park HW (February 2013). "Structural insights into aldosterone synthase substrate specificity and targeted inhibition". Molecular Endocrinology. 27 (2): 315–24. doi:10.1210/me.2012-1287. PMC 5417327. PMID 23322723.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000179142 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000075604 – 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.

[Bassett-5] Bassett MH, White PC, Rainey WE (March 2004). "The regulation of aldosterone synthase expression". Molecular and Cellular Endocrinology. 217 (1–2): 67–74. doi:10.1016/j.mce.2003.10.011. PMID 15134803. S2CID 43133280.

[Peter_M-6] Peter M, Dubuis JM, Sippell WG (1999). "Disorders of the aldosterone synthase and steroid 11beta-hydroxylase deficiencies". Hormone Research. 51 (5): 211–22. doi:10.1159/000023374 (inactive 10 July 2024). PMID 10559665. S2CID 24182379.{{cite journal}}: CS1 maint: DOI inactive as of July 2024 (link)

[Structural-7] Strushkevich N, Gilep AA, Shen L, Arrowsmith CH, Edwards AM, Usanov SA, Park HW (February 2013). "Structural insights into aldosterone synthase substrate specificity and targeted inhibition". Molecular Endocrinology. 27 (2): 315–24. doi:10.1210/me.2012-1287. PMC 5417327. PMID 23322723.

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