Carboxypeptidase Z is an enzyme that in humans is encoded by the CPZgene.[1][2]
This gene encodes a member of the metallocarboxypeptidase family. This enzyme displays carboxypeptidase activity towards substrates with basic C-terminal residues. It is most active at neutral pH and is inhibited by active site-directed inhibitors of metallocarboxypeptidases. Alternative splicing in the coding region results in multiple transcript variants encoding different isoforms.[2]
References
↑Song L, Fricker LD (May 1997). "Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidase". J Biol Chem. 272 (16): 10543–50. doi:10.1074/jbc.272.16.10543. PMID9099699.
Reznik SE, Fricker LD (2002). "Carboxypeptidases from A to z: implications in embryonic development and Wnt binding". Cell. Mol. Life Sci. 58 (12–13): 1790–804. doi:10.1007/PL00000819. PMID11766880.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
Fan X, Olson SJ, Blevins LS, et al. (2003). "Immunohistochemical localization of carboxypeptidases D, E, and Z in pituitary adenomas and normal human pituitary". J. Histochem. Cytochem. 50 (11): 1509–16. doi:10.1177/002215540205001111. PMID12417617.
Novikova EG, Reznik SE, Varlamov O, Fricker LD (2000). "Carboxypeptidase Z is present in the regulated secretory pathway and extracellular matrix in cultured cells and in human tissues". J. Biol. Chem. 275 (7): 4865–70. doi:10.1074/jbc.275.7.4865. PMID10671522.
Novikova EG, Fricker LD (1999). "Purification and characterization of human metallocarboxypeptidase Z.". Biochem. Biophys. Res. Commun. 256 (3): 564–8. doi:10.1006/bbrc.1999.0378. PMID10080937.
