Carboxypeptidase N subunit 2 (CPN2)

Carboxypeptidase N subunit 2 is the high molecular weight, 83 kDa regulatory subunit of the plasma metalloprotease carboxypeptidase N. This subunit binds and stabilizes the smaller, enzymatically active subunits (CPN1), enabling their proper function in the bloodstream. CPN2 plays a crucial role in the regulation of peptide hormones and anaphylatoxins by maintaining carboxypeptidase N activity, which in turn modulates inflammation and innate immune responses. CPN2 itself does not perform catalytic cleavage, but by stabilizing and possibly allosterically modifying CPN1, it indirectly influences the breakdown of peptides such as complement anaphylatoxins and kinins. Note: The molecule is not a receptor, but a regulatory subunit of an enzyme complex important in inflammation and immune regulation. There are no common direct inhibitors or therapeutically approved drugs that target CPN2 specifically; zinc functions as a cofactor for the enzyme complex. Disease roles are mostly inferred from its involvement in inflammation and immune system pathways. If more specific therapeutic targeting emerges in future research, these roles may be updated. Currently, CPN2 is best considered a regulatory enzyme subunit within the broader carboxypeptidase N complex.

Other names

ACBPCarboxypeptidase N 83 kDa chainCarboxypeptidase N large subunitCarboxypeptidase N polypeptide 2Carboxypeptidase N regulatory subunit

Enzyme stabilization (drug cofactors maintain protein stability and activity); Not directly inhibited or modulated by currently approved drugs