Angiotensin-Converting Enzyme

Supporting information

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.

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Gene Species Gene Symbol Gene Accession No. Protein Accession No.
Angiotensin-converting enzyme I Human ACE NM_152830 P22966
Mouse Ace NM_207624 P09470
Rat Ace NM_012544 Q8CFN1
Angiotensin-converting enzyme 2 Human ACE2 NM_021804 Q9BYF1
Mouse Ace2 NM_027286 Q8R0I0
Rat Ace2 NM_001012006 Q5EGZ1
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Literature for Angiotensin-Converting Enzyme

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