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Literature summary for 3.4.17.3 extracted from

  • Leung, L.L.K.; Morser, J.
    Carboxypeptidase B2 and carboxypeptidase N in the crosstalk between coagulation, thrombosis, inflammation, and innate immunity (2018), J. Thromb. Haemost., 16, 1474-1486 .
    View publication on PubMed
Search for more literature for 3.4.17.3

Inhibitors

Inhibitors Comment Organism Structure
DL-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
 Mus musculus
EDTA
-
 Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus Q9JJN5
-
-

Subunits

Subunits Comment Organism
tetramer
-
 Mus musculus

Synonyms

Synonyms Comment Organism
carboxypeptidase N
-
 Mus musculus
CPN
-
 Mus musculus
CPN1
-
 Mus musculus

General Information

General Information Comment Organism
malfunction among mice genetically deficient in either carboxypeptidase B2 (Cpb2) or carboxypeptidase N (Cpn), in a model of hemolytic-uremic syndrome, Cpb2-/- mice have the worst disease, followed by Cpn-/- mice, with wild-type mice being the most protected. This model is driven by complement component C5a, and shows that carboxypeptidase B2 is important in inactivating complement component C5a. Cpn-/- mice are generated by disruption of complement component Cpn1. When mice are challenged acutely with cobra venom factor, the reverse phenotype is observed. Cpn-/- mice have markedly worse disease than Cpb2-/- mice, and wild-type mice are resistant Mus musculus
additional information the enzyme is constitutively active Mus musculus
physiological function carboxypeptidase N is responsible for systemic inactivation of complement component C3a and C5a Mus musculus
physiological function the enzyme removes C-terminal basic amino acids from bioactive peptides and proteins, thereby inactivating them Mus musculus