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Literature summary for 3.4.17.15 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
Search for more literature for 3.4.17.15

Inhibitors

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

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

Source Tissue

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
angiotensin II + H2O
-
 Rattus norvegicus angiotensin-(1-7) + L-Phe
-
 ?
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 ?
benzyloxycarbonyl-Val-Phe + H2O
-
 Rattus norvegicus benzyloxycarbonyl-Val + L-Phe
-
 ?