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Angiotensin I converting enzyme (peptidyl-dipeptidase A) 1
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| PDB rendering based on 1o86. | ||||||||||||||
| Available structures: 1o86, 1o8a, 1uze, 1uzf, 2c6f, 2c6n, 2iul, 2iux, 2oc2 | ||||||||||||||
| Identifiers | ||||||||||||||
| Symbols | ACE; ACE1; CD143; DCP; DCP1; MGC26566 | |||||||||||||
| External IDs | OMIM: 106180 MGI: 87874 HomoloGene: 37351 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
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| 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) |
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| Location | Chr 17: 58.91 - 58.94 Mb | Chr 11: 105.78 - 105.81 Mb | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
Angiotensin I converting enzyme (ACE, EC 3.4.15.1) is an exopeptidase.
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Functions
It has two primary functions:
- it catalyses the conversion of angiotensin I to angiotensin II, a potent vasoconstrictor. [1]
- 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, mainly in the lung, including vascular endothelial cells, epithelial kidney cells, and testicular Leydig cells, whereas the germinal is expressed only in sperm.
See also
References
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. doi:. 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:. 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:. PMID 17103020.
- Castellon R, Hamdi HK (2007). "Demystifying the ACE polymorphism: from genetics to biology". Curr. Pharm. Des. 13 (12): 1191–8. doi:. 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. doi:. PMID 17504232.
External links
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