EC Number   |
General Information |
Reference |
|---|
   3.4.17.2 | 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 |
754517 |
| 3.4.17.2 | malfunction |
anti-CPBAs1 directed antibodies can significantly reduce the mosquito infection rate in the test group compared with the control group |
731910 |
| 3.4.17.2 | malfunction |
Cpb2 knockout mice develop greater cartilage damage than wild-type mice and have a greater number of osteophytes and degree of synovitis |
731233 |
| 3.4.17.2 | metabolism |
CPB activity generates fine-mesh fibrin which is more difficult to lyse by tPA but conversely, CPB and plasmin together can stimulate fibrinolysis |
732935 |
| 3.4.17.2 | metabolism |
nitrone spin-trap 5,5-dimethyl-1-pyrroline N-oxide (DMPO) and a combination of immuno-spin trapping and mass spectrometry is used to identify in vivo products of radical reactions in mice. Dose-dependent production of 5,5-dimethyl-1-pyrroline N-oxide-CPB1 adducts are detected in the spleens of mice treated with lipopolysaccharide and also under normal physiological conditions. Treatments with inhibitors and experiments with knock-out mice indicate that xanthine oxidase and endothelial nitric oxide synthase are important sources of the reactive species that lead to CPB1 adduct formation |
708564 |
| 3.4.17.2 | more |
the enzyme is constitutively active |
754517 |
| 3.4.17.2 | physiological function |
carboxypeptidase B activity is not affected by Zn supplementation |
708891 |
| 3.4.17.2 | physiological function |
in contrast to botulinum neurotoxin carboxypeptidase is not affected by mechanical stirring |
709673 |
| 3.4.17.2 | physiological function |
the enzyme delays fibrinolysis. CPB2 is important in inactivating C5a |
754517 |
| 3.4.17.2 | physiological function |
the enzyme removes C-terminal basic amino acids from bioactive peptides and proteins, thereby inactivating them |
754517 |
