CPZ (gene)

Carboxypeptidase Z, also known as CPZ, is a human gene.cite web | title = Entrez Gene: CPZ carboxypeptidase Z| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8532| accessdate = ]

PBB_Summary
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summary_text = 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.cite web | title = Entrez Gene: CPZ carboxypeptidase Z| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8532| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Reznik SE, Fricker LD |title=Carboxypeptidases from A to z: implications in embryonic development and Wnt binding. |journal=Cell. Mol. Life Sci. |volume=58 |issue= 12-13 |pages= 1790-804 |year= 2002 |pmid= 11766880 |doi=
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Fan X, Olson SJ, Blevins LS, "et al." |title=Immunohistochemical localization of carboxypeptidases D, E, and Z in pituitary adenomas and normal human pituitary. |journal=J. Histochem. Cytochem. |volume=50 |issue= 11 |pages= 1509-16 |year= 2003 |pmid= 12417617 |doi=
*cite journal | author=Novikova EG, Reznik SE, Varlamov O, Fricker LD |title=Carboxypeptidase Z is present in the regulated secretory pathway and extracellular matrix in cultured cells and in human tissues. |journal=J. Biol. Chem. |volume=275 |issue= 7 |pages= 4865-70 |year= 2000 |pmid= 10671522 |doi=
*cite journal | author=Novikova EG, Fricker LD |title=Purification and characterization of human metallocarboxypeptidase Z. |journal=Biochem. Biophys. Res. Commun. |volume=256 |issue= 3 |pages= 564-8 |year= 1999 |pmid= 10080937 |doi= 10.1006/bbrc.1999.0378
*cite journal | author=Song L, Fricker LD |title=Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidase. |journal=J. Biol. Chem. |volume=272 |issue= 16 |pages= 10543-50 |year= 1997 |pmid= 9099699 |doi=

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