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Literature summary extracted from

  • Pereira, H.; Souza, L.; Costa-Neto, C.; Salgado, M.; Oliveira, E.
    Carboxypeptidases A1 and A2 from the perfusate of rat mesenteric arterial bed differentially process angiotensin peptides (2012), Peptides, 33, 67-76.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.17.15 1,10-phenanthroline 1 mM, complete inhibition Rattus norvegicus
3.4.17.15 potato carboxypeptidase inhibitor 10 microM, complete inhibition Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.17.15 0.191
-
 angiotensin II pH 8.1, 37°C Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
3.4.17.15 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.17.15 from mesenteric arterial bed perfusate Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.17.15 artery mesenteric arterial bed, enzyme is identical with its pancreatic counterpart Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.17.15 angiotensin II + H2O
-
 Rattus norvegicus angiotensin-(1-7) + L-Phe
-
 ?
3.4.17.15 angiotensin-(1-12) + H2O
-
 Rattus norvegicus angiotensin I + ? conversion of Ang-(1-12) to Ang I proceeds through stepwise cleavage of C-terminal Tyr and Leu residues ?
3.4.17.15 benzyloxycarbonyl-Val-Phe + H2O
-
 Rattus norvegicus benzyloxycarbonyl-Val + L-Phe
-
 ?