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Literature summary for 3.4.16.2 extracted from
- Identification of prolyl carboxypeptidase as an alternative enzyme for processing of renal angiotensin II using mass spectrometry (2013), Am. J. Physiol. Cell Physiol., 304, C945-C953 .
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Z-prolyl-prolinal | - |
Mus musculus |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| kidney | - |
Mus musculus | - |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | at pH values below 6, formation of angiotensin (1-7) in ACE2 knockout mice is similar to that in wild-type mice. The prolyl carboxypeptidase-prolyl endopeptidase inhibitor Z-prolyl-prolinal reduces angiotensin (1-7) formation in ACE2 knockout mice. ACE2 metabolizes angiotensin II in the kidney at neutral and basic pH, while prolyl carboxypeptidase catalyzes the same reaction at acidic pH | Mus musculus |
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Release 2023.1 (January 2023)
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