Carboxypeptidase E

Research output: Chapter in Book/Report/Conference proceedingChapter

21 Scopus citations


This chapter examines activity, specificity and structural chemistry of carboxypeptidase E (CPE). CPE removes C-terminal basic residues from a variety of substrates, with no detectable activity towards nonbasic residues. All residues are tolerated in the PI position, although the Pro–Arg bond is cleaved several orders of magnitude more slowly than substrates with other residues in PI. Amongst N-terminally blocked small peptides, CPE shows lower activity with dipeptides than with tri- or tetrapeptides. The optimal pH for CPE activity is 5.0–5.5, and activity falls off dramatically with increasing pH. The sensitivity of CPE to pH over the range 5.5–7 may serve as a mechanism to keep CPE inactive in the Golgi and allow for the activation of CPE in mature secretory vesicles. As found with other metallocarboxypeptidases, CPE is stimulated by millimolar concentrations of Co2+ and inhibited by 1,10-phenanthroline. CPE is potently inhibited by some thiol-directed reagents. CPE is a single-chain protein of 52–56 kDa, with a pi around 5. It is likely that CPE contains lmol of zinc per mol of protein based on the homology between CPE and other metallocarboxypeptidases.

Original languageEnglish (US)
Title of host publicationHandbook of Proteolytic Enzymes, Second Edition
Subtitle of host publicationVolume 1: Aspartic and Metallo Peptidases
Number of pages5
ISBN (Electronic)9780120796113
ISBN (Print)9780124121058
StatePublished - Jan 1 2004

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology


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