Angiotensin-converting enzyme (ACE, aka peptidyl dipeptidase A, carboxycathepsin) cleaves a C-terminal dipeptide from angiotensin I to create the vasoconstrictor peptide, angiotensin II. ACE can also inactivate the vasodilator peptide, bradykinin.
There are two isoforms of ACE, a smaller/single catalytic site enzyme found in the testes and a more widely expressed ~180kDa dual active site isoform. ACE is often membrane bound. In contrast to ACE, the homolog ACE2, has recently been shown to cleave and inactivate angiotensin II to generate the vasodilator Angiotensin (1-7). ACE inhibitors are widely used to treat hypertension and cardiovascular diseases. ACE inhibitors have also been used to slow nephropathy, particularly when it is associated with diabetes.View all products for Angiotensin-Converting Enzyme »
|Gene||Species||Gene Symbol||Gene Accession No.||Protein Accession No.|
|Angiotensin-converting enzyme I||Human||ACE||NM_152830||P22966|
|Angiotensin-converting enzyme 2||Human||ACE2||NM_021804||Q9BYF1|
|View all Angiotensin-Converting Enzyme Gene Data »|
Literature for Angiotensin-Converting Enzyme
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