The Enzyme Database

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Accepted name: carboxypeptidase E
Reaction: Release of C-terminal arginine or lysine residues from polypeptides
Other name(s): carboxypeptidase H; enkephalin convertase; cobalt-stimulated chromaffin granule carboxypeptidase; insulin granule-associated carboxypeptidase; enkephalin convertase; membrane-bound carboxypeptidase; carboxypeptidase E; enkephalin-precursor endopeptidase; enkephalin precursor carboxypeptidase; peptidyl-L-lysine(-L-arginine) hydrolase
Comments: 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).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, 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 (1999) 11582–11586. [DOI] [PMID: 10206965]
2.  Fricker, L.D. Carboxypeptidase E/H. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Ed.), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, pp. 1341–1344.
3.  Fricker, L.D. Methods for studying carboxypeptidase E. Methods Neurosci. 23 (1995) 237–250.
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 (1990) 517–525. [PMID: 2334405]
5.  Fricker, L.D. Carboxypeptidase E. Annu. Rev. Physiol. 50 (1988) 309–321. [DOI] [PMID: 2897826]
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