Angiotensin-converting enzyme
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| Angiotensin I converting enzyme PDB [1] | |
| Angiotensin I converting enzyme
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| Identifiers | |
| Symbol(s) | ACE CD143, CD143 |
| Entrez | 1636 |
| OMIM | 106180 |
| RefSeq | NM_000789 |
| UniProt | P12821 |
| Other data | |
| EC number | 3.4.15.1 |
| Locus | Chr. 17 q23 |
Angiotensin I converting enzyme (ACE, EC 3.4.15.1) is an exopeptidase that catalyses the conversion of angiotensin I to angiotensin II, a potent vasoconstrictor. ACE is also 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.
ACE is also known as:
- peptidyl dipeptidase A
- carboxycathepsin
- kininase II (kinin-kallikrein system)
- CD 143
- ACE1
[edit] 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.
