Biology:Carboxypeptidase C
From HandWiki
| Carboxypeptidase C | |||||||||
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| 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 | ||||||||
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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.
- ↑ "Protein sorting in yeast: the localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide". Cell 48 (5): 887–97. March 1987. doi:10.1016/0092-8674(87)90085-7. PMID 3028649.
- ↑ "Inactivation of endothelin I by deamidase (lysosomal protective protein)". The Journal of Biological Chemistry 267 (5): 2872–5. February 1992. PMID 1737744.
- ↑ "Purification, subunit structure and inhibitor profile of cathepsin A". Journal of Chromatography 627 (1-2): 153–62. December 1992. 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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