EC - Carboxypeptidase E

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature


Accepted name:
carboxypeptidase E
Other names:
carboxypeptidase H
cobalt-stimulated chromaffin granule carboxypeptidase
enkephalin convertase
enkephalin precursor carboxypeptidase
enkephalin-precursor endopeptidase
insulin granule-associated carboxypeptidase
membrane-bound carboxypeptidase
peptidyl-L-lysine(-L-arginine) hydrolase
Systematic name:




A zinc enzyme, activated by Co2+. Inhibited by 1,10-phenanthroline and other chelating agents. pH optimum 5.6. Located in storage granules of secretory cells, and active in processing of protein hormones and bioactive peptides. In peptidase family M14 (carboxypeptidase A family). Formerly EC, carboxypeptidase H.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Protein domains and families: PROSITE:PDOC00123
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004183
CAS Registry Number: 81876-95-1


  1. Qian, Y.M., Varlamov, O. and Fricker, L.D.
    Glu300 of rat carboxypeptidase E is essential for enzymatic activity but not substrate binding or routing to the regulated secretory pathway.
    J. Biol. Chem. 274: 11582-11586 (1999). [PMID: 10206965]
  2. Fricker, L.D.
    Carboxypeptidase E/H.
    In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.) Handbook of Proteolytic Enzymes, Academic Press, London, 1998, 1341-1344
  3. Fricker, L.D.
    Methods for studying carboxypeptidase E.
    Methods Neurosci. 23: 237-250 (1995).
  4. Manser, E., Fernandez, D., Loo,L., Goh, P.Y., Monfries, C., Hall, C. and Lim,L.
    Human carboxypeptidase E: isolation and characterisaton of the cDNA, sequence conservation, expression and processing in vitro.
    Biochem. J. 267: 517-525 (1990). [PMID: 2334405]
  5. Fricker, L.D.
    Carboxypeptidase E.
    Annu. Rev. Physiol. 50: 309-321 (1988). [PMID: 2897826]

[EC created 1986, modified 2000]