Reaction: Release of a C-terminal amino acid with broad specificity
Other names: carboxypeptidase Y; serine carboxypeptidase I; cathepsin A; lysosomal protective protein; deamidase; lysosomal carboxypeptidase A; phaseolin
Comments: 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 3.4.12.1 and EC 3.4.21.13, and included in EC 3.4.16.1.
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 9046-67-7
References
1. Breddam, K. Serine carboxypeptidases. A review. Carlsberg Res. Commun. 51 (1986) 83-128
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 (1987) 887-897. [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 (1992) 2872-2875. [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 (1992) 153-162. [PMID: 1487525]