| EC |
3.4.16.5 |
| Accepted name: |
carboxypeptidase C |
| Reaction: |
Release of a C-terminal amino acid with broad specificity |
| Other name(s): |
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. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, 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. [DOI] [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] |
|
| [EC 3.4.16.5 created 1972 as EC 3.4.12.1, transferred 1978 to EC 3.4.16.1, part transferred 1993 to EC 3.4.16.5 (EC 3.4.16.3 created 1972 as EC 3.4.12.12, transferred 1978 to EC 3.4.16.3, transferred 1992 to EC 3.4.16.1), (EC 3.4.21.13 created 1972, transferred 1978 to EC 3.4.16.1)] |
| |
|
| |
|
Printable version