Angiotensin-converting enzyme

Angiotensin I converting enzyme (peptidyl-dipeptidase A) 1
PDB rendering based on 1o86.
Identifiers
Symbol(s)	ACE; ACE1; CD143; DCP; DCP1; MGC26566
External IDs	OMIM: 106180 MGI: 87874 Homologene: 37351
Gene ontology Molecular Function: • carboxypeptidase activity • peptidyl-dipeptidase A activity • zinc ion binding • hydrolase activity, acting on glycosyl bonds • chloride ion binding • metal ion binding Cellular Component: • membrane fraction • soluble fraction • plasma membrane • membrane • integral to membrane Biological Process: • proteolysis • metabolic process • blood pressure regulation
RNA expression pattern
More reference expression data
Orthologs
	Human	Mouse
Entrez	1636	11421
Ensembl	ENSG00000159640	ENSMUSG00000020681
Uniprot	P12821	Q3TU20
Refseq	NM_000789 (mRNA) NP_000780 (protein)	NM_009598 (mRNA) NP_033728 (protein)
Location	Chr 17: 58.91 - 58.94 Mb	Chr 11: 105.78 - 105.81 Mb
Pubmed search	[1]	[2]

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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [3]

Overview

Angiotensin I converting enzyme (ACE, EC 3.4.15.1) is an exopeptidase.

• Angiotensin-converting enzymes (ACE) are very important to the kallikrein-kinine system and the renin-angiotensin-aldosterone system
• ACE is found in the endothelial cells of the vascular system, primarily in the kidneys and lungs
• Reference range: 8-52 U/l in adults

Functions

It has two primary functions:

• it catalyses the conversion of angiotensin I to angiotensin II, a potent vasoconstrictor.

• it is involved in the inactivation of bradykinin, a potent vasodilator.

These two actions of ACE make it an ideal target in the treatment of conditions such as high blood pressure, heart failure, diabetic nephropathy and type 2 diabetes mellitus. Inhibition of ACE (by ACE inhibitors) results in decreased formation of Angiotensin II (a far more potent vasoconstrictor than Angiotensin I) and decreased inactivation of bradykinin.

Synonyms

ACE is also known as:

• peptidyl dipeptidase A
• carboxycathepsin
• kininase II (kinin-kallikrein system)
• CD 143
• ACE1

Genetics

The ACE gene, ACE, encodes 2 isozymes. The somatic isozyme is expressed in many tissues, including vascular endothelial cells, epithelial kidney cells, and testicular Leydig cells, whereas the germinal is expressed only in sperm.

Differential Diagnosis

Increased

• Alcoholic liver disease
• Allergic alveolitis
• Amyloidosis
• Asbestosis
• Berylliosis
• Biliary Cirrhosis
• Coccidioidomycosis
• Diabetes Mellitus
• Gaucher's Disease
• Hyperparathyroidism
• Hyperthyroidism
• Kidney diseases
• Leprosy
• Multiple Myeloma
• Sarcoidosis
• Silicosis
• Smoker's Bronchitis
• Tuberculosis
• Viral hepatitis

See also

• Renin-angiotensin system
• ACE inhibitors

Further reading

• Niu T, Chen X, Xu X (2002). "Angiotensin converting enzyme gene insertion/deletion polymorphism and cardiovascular disease: therapeutic implications.". Drugs 62 (7): 977-93. PMID 11985486.
• Roĭtberg GE, Tikhonravov AV, Dorosh ZhV (2004). "[Role of angiotensin-converting enzyme gene polymorphism in the development of metabolic syndrome]". Ter. Arkh. 75 (12): 72-7. PMID 14959477.
• Vynohradova SV (2005). "[The role of angiotensin-converting enzyme gene I/D polymorphism in development of metabolic disorders in patients with cardiovascular pathology]". Tsitol. Genet. 39 (1): 63-70. PMID 16018179.
• König S, Luger TA, Scholzen TE (2006). "Monitoring neuropeptide-specific proteases: processing of the proopiomelanocortin peptides adrenocorticotropin and alpha-melanocyte-stimulating hormone in the skin.". Exp. Dermatol. 15 (10): 751-61. doi:10.1111/j.1600-0625.2006.00472.x. PMID 16984256.
• Sabbagh AS, Otrock ZK, Mahfoud ZR, et al. (2007). "Angiotensin-converting enzyme gene polymorphism and allele frequencies in the Lebanese population: prevalence and review of the literature.". Mol. Biol. Rep. 34 (1): 47-52. doi:10.1007/s11033-006-9013-y. PMID 17103020.
• Castellon R, Hamdi HK (2007). "Demystifying the ACE polymorphism: from genetics to biology.". Curr. Pharm. Des. 13 (12): 1191-8. PMID 17504229.
• Lazartigues E, Feng Y, Lavoie JL (2007). "The two fACEs of the tissue renin-angiotensin systems: implication in cardiovascular diseases.". Curr. Pharm. Des. 13 (12): 1231-45. PMID 17504232.

External links

• MeSH Angiotensin+Converting+Enzyme

de:Angiotensin Converting Enzymenl:Angiotensine I converterend enzymsr:АКЕ