From Wikipedia, the free encyclopedia
Carboxypeptidase Z is an enzyme that in humans is encoded by the CPZ gene .[ 5] [ 6]
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 .[ 6]
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Further reading
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 . PMID 11766880 .
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)" . Genome Res . 14 (10B): 2121–7. doi :10.1101/gr.2596504 . PMC 528928 . PMID 15489334 .
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 . PMID 14702039 .
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences" . Proc. Natl. Acad. Sci. U.S.A . 99 (26): 16899–903. doi :10.1073/pnas.242603899 . PMC 139241 . PMID 12477932 .
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 . PMID 12417617 .
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 . PMID 10671522 .
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 . PMID 10080937 .