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Aminopeptidase P (None)
- Target
- None
- Molecular classification
- Enzyme, Metalloprotease, Peptidase subfamily M24B
01
Overview
Aminopeptidase P (APP) is a metalloenzyme that specifically cleaves the N-terminal amino acid from peptides and proteins where the second residue is proline. It exists in both membrane-bound and soluble forms and plays a role in the degradation of bioactive peptides like bradykinin. APP is implicated in various physiological processes and diseases, including cancer, inflammation, and cardiovascular regulation, making it a potential therapeutic target and biomarker.
- Other names
- Aminoacylproline aminopeptidaseCytoplasmic aminopeptidase PCytosolic aminopeptidase PX-Pro aminopeptidase 1Xaa-Pro aminopeptidase 1xpnpep1
02
Mechanism of action
Inhibiting the enzymatic activity of Aminopeptidase P, leading to altered levels of proline-containing peptides such as bradykinin.
03
Biological functions
Peptide degradationKinin metabolismNeuropeptide metabolismHormone processingMyeloid cell differentiation
04
Disease associations
CancerInflammationCardiovascular disease (related to kinin metabolism)Infection (virulence factor in some bacteria)
05
Safety considerations
Altered kinin metabolism may have cardiovascular implications.Potential off-target effects related to proline metabolism.
06
Biomarkers
Overexpression in some cancer cell types as a potential biomarker
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