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Literature summary for 3.4.17.2 extracted from
- Carboxypeptidase B2 and carboxypeptidase N in the crosstalk between coagulation, thrombosis, inflammation, and innate immunity (2018), J. Thromb. Haemost., 16, 1474-1486 .
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| DL-mercaptomethyl-3-guanidinoethylthiopropanoic acid | - |
Mus musculus |  |
| EDTA | - |
Mus musculus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
- |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | - |
Mus musculus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| carboxypeptidase B2 | - |
Mus musculus |
| CPB2 | - |
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 C5a, and shows that carboxypeptidase B2 is important in inactivating C5a. Cpn-/- mice are generated by disruption of 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 | the enzyme delays fibrinolysis. CPB2 is important in inactivating C5a | Mus musculus |
| physiological function | the enzyme removes C-terminal basic amino acids from bioactive peptides and proteins, thereby inactivating them | Mus musculus |
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