Reaction: Release of C-terminal arginine or lysine residues from polypeptides
Other names: 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). Formerly EC 3.4.17.10, carboxypeptidase H
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, CAS registry number: 81876-95-1
References
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. [PMID: 10206965]
2. Fricker, L.D. Carboxypeptidase E/H. In Handbook of Proteolytic Enzymes (Barrett, A.J., Rawlings, N.D. and Woessner, J.F. eds), p.1341-1344 (1998) Academic Press, London.
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. [PMID: 2897826]