EC - Carboxypeptidase C

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IntEnz Enzyme Nomenclature


Accepted name:
carboxypeptidase C
Other names:
carboxypeptidase Y
cathepsin A
lysosomal carboxypeptidase A
lysosomal protective protein
serine carboxypeptidase I
Systematic name:



A carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents (reviewed in [1]). Widely distributed in eukaryotes. Type example of peptidase family S10. Formerly EC and EC, and included in EC This enzyme is probably also identical to lysosomal tyrosine carboxypeptidase, formerly EC

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Protein domains and families: PROSITE:PDOC00122
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004185
CAS Registry Number: 9046-67-7
UniProtKB/Swiss-Prot: (60) [show] [UniProt]


  1. Breddam, K.
    Serine carboxypeptidases. A review.
    Carlsberg Res. Commun. 51 : 83-128 (1986).
  2. Valls, L.A., Hunter, C.P., Rothman, J.H. and Stevens, T.H.
    Protein sorting in yeast: the localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide.
    Cell 48 : 887-897 (1987). [PMID: 3028649]
  3. Jackman, H.L., Morris, P.W., Deddish, P.A., Skidgel, R.A. and Erdös, E.G.
    Inactivation of endothelin I by deamidase (lysosomal protective protein).
    J. Biol. Chem. 267 : 2872-2875 (1992). [PMID: 1737744]
  4. Miller, J.J., Changaris, D.G. and Levy, R.S.
    Purification, subunit structure and inhibitor profile of cathepsin-A.
    J. Chromatogr. 627 : 153-162 (1992). [PMID: 1487525]

[EC created 1972 as EC, transferred 1978 to EC, part transferred 1993 to EC (EC created 1972 as EC, transferred 1978 to EC, incorporated 1992)]