Carboxypeptidase C
| Carboxypeptidase C | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.16.5 | ||||||||
| CAS number | 9046-67-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Carboxypeptidase C (EC 3.4.16.5, carboxypeptidase Y, serine carboxypeptidase I, cathepsin A, lysosomal protective protein, deamidase, lysosomal carboxypeptidase A, phaseolin) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Release of a C-terminal amino acid with broad specificity
This enzyme is a carboxypeptidase with optimum activity at pH 4.5-6.0. It is inhibited by diisopropyl fluorophosphate.
See also
References
- ↑ Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51: 83–128. doi:10.1007/bf02907561.
- ↑ Valls, L.A.; Hunter, C.P.; Rothman, J.H.; Stevens, T.H. (1987). "Protein sorting in yeast: the localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide". Cell. 48: 887–897. doi:10.1016/0092-8674(87)90085-7. PMID 3028649.
- ↑ Jackman, H.L.; Morris, P.W.; Deddish, P.A.; Skidgel, R.A.; Erdös, E.G. (1992). "Inactivation of endothelin I by deamidase (lysosomal protective protein)". J. Biol. Chem. 267: 2872–2875. PMID 1737744.
- ↑ Miller, J.J.; Changaris, D.G.; Levy, R.S. (1992). "Purification, subunit structure and inhibitor profile of cathepsin-A". J. Chromatogr. 627: 153–162. doi:10.1016/0021-9673(92)87195-e. PMID 1487525.
External links
- Carboxypeptidase C at the US National Library of Medicine Medical Subject Headings (MeSH)
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