Carboxypeptidase Z (CPZ)

Carboxypeptidase Z (CPZ) is a secreted zinc-dependent metallocarboxypeptidase enzyme that cleaves substrates containing basic C-terminal residues, particularly arginine. Its structure features an N-terminal cysteine-rich domain (CRD) and a C-terminal catalytic domain. CPZ is involved in the modulation of the Wnt signaling pathway, possibly by direct binding via its CRD domain and enzymatic cleavage of undefined protein substrates, influencing developmental processes such as skeletal element formation and morphogenesis. It is most active at neutral pH and is inhibited by active site-directed inhibitors of metallocarboxypeptidases. Alternative splicing results in several transcript variants and isoforms. Disease associations include Locked-In Syndrome and Epithelial-Stromal Tgfbi Dystrophy. There are currently no directly approved drugs targeting CPZ, nor established clinical biomarkers involving CPZ.

Other names

Carboxypeptidase ZCPZmetallocarboxypeptidase ZCBPZcarboxypeptidase ZCPZ proteinVEZT/CPZ fusionepididymis secretory sperm binding protein

Enzymatic inhibition: drugs or compounds that inhibit metallocarboxypeptidase active sites may reduce CPZ activity