EC 220.127.116.11 - Carboxypeptidase C
IntEnz Enzyme Nomenclature
lysosomal carboxypeptidase A
lysosomal protective protein
serine carboxypeptidase I
- Release of a C-terminal amino acid with broad specificity.
A carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents (reviewed in ). Widely distributed in eukaryotes. Type example of peptidase family S10. Formerly EC 18.104.22.168 and EC 22.214.171.124, and included in EC 126.96.36.199. This enzyme is probably also identical to lysosomal tyrosine carboxypeptidase, formerly EC 188.8.131.52.
Links to other databases
Serine carboxypeptidases. A review.Carlsberg Res. Commun. 51: 83-128 (1986).
Protein sorting in yeast: the localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide.Cell 48: 887-897 (1987). [PMID: 3028649]
Inactivation of endothelin I by deamidase (lysosomal protective protein).J. Biol. Chem. 267: 2872-2875 (1992). [PMID: 1737744]
Purification, subunit structure and inhibitor profile of cathepsin-A.J. Chromatogr. 627: 153-162 (1992). [PMID: 1487525]
[EC 184.108.40.206 created 1972 as EC 220.127.116.11, transferred 1978 to EC 18.104.22.168, part transferred 1993 to EC 22.214.171.124 (EC 126.96.36.199 created 1972 as EC 188.8.131.52, transferred 1978 to EC 184.108.40.206, incorporated 1992)]