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Peptidyl-dipeptidase A (None)
- Target
- None
- Molecular classification
- Enzyme, Hydrolase, Peptidase, Metallopeptidase, M2 Metallopeptidases
01
Overview
Peptidyl-dipeptidase A is a membrane-bound, chloride-dependent glycoprotein enzyme that acts as an exopeptidase, catalyzing the release of C-terminal dipeptides from oligopeptides. It is most notable for its role in converting angiotensin I to angiotensin II, a key step in blood pressure regulation. The enzyme does not act on peptide bonds where the penultimate residue (Xaa) is proline or the terminal residue (Yaa) is aspartic acid or glutamic acid. It also inactivates bradykinin. Selective inhibitors targeting peptidyl-dipeptidase A are widely used as antihypertensive agents.
- Other names
- ACEAngiotensin I-converting enzymeDipeptidyl carboxypeptidase IKininase IICarboxycathepsinPeptidyl dipeptidase IKininase ACD143 Antigens
02
Mechanism of action
Inhibition of angiotensin I conversion to angiotensin II, thereby reducing vasoconstriction and blood pressure.
03
Biological functions
Conversion of angiotensin I to angiotensin IIBradykinin inactivationBlood pressure regulationCatalysis of C-terminal dipeptide releaseGlycosidase activity
04
Disease associations
Cardiovascular diseaseHypertension
05
Interacting drugs
ACE inhibitors
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