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Literature summary extracted from

  • Grobe, N.; Weir, N.M.; Leiva, O.; Ong, F.S.; Bernstein, K.E.; Schmaier, A.H.; Morris, M.; Elased, K.M.
    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 .
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.16.2 Z-prolyl-prolinal
-
 Mus musculus
3.4.17.23 Z-prolyl-prolinal
-
 Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
3.4.16.2 Mus musculus
-
-
-
3.4.17.23 Mus musculus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.16.2 kidney
-
 Mus musculus
-
3.4.17.23 kidney
-
 Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.17.23 angiotensin II + H2O
-
 Mus musculus angiotensin-(1-7) + L-phenylalanine
-
 ?

General Information

EC Number General Information Comment Organism
3.4.16.2 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
3.4.17.23 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