Purification and characterization of human metallocarboxypeptidase Z

Elena G. Novikova, Lloyd D. Fricker

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


Carboxypeptidase Z (CPZ) is a recently discovered member of the metallocarboxypeptidase gene family that has an N-terminal domain related to the Wnt/wingless binding domain of frizzled receptors and other proteins. To further characterize the enzymatic properties of CPZ, the enzyme was purified using Arg-and heparin-affinity columns. CPZ has a neutral pH optimum, and is inhibited by chelating agents and several divalent cations (Zn2+, Mn2+, Cd2+, Cu2+, Hg2+). Active site-directed inhibitors of several other metallocarboxypeptidases also inhibit CPZ activity with moderate potency. CPZ cleaves substrates with C-terminal Arg residues, preferring peptides with an Ala in the penultimate position. No activity is detected toward substrates with an Ile-Arg or a Pro-Arg sequence. The Km for dansyl-Phe-Ala-Arg and dansyl-Pro-Ala-Arg are both approximately 2 mM. Taken together, these data suggests a selective role for CPZ in the processing of extracellular peptides or proteins.

Original languageEnglish (US)
Pages (from-to)564-568
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Mar 24 1999

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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