Carboxypeptidase C

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

Carboxypeptidase C
Identifiers
EC no.	3.4.16.5
CAS no.	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
Search PMC articles PubMed articles NCBI proteins

This enzyme is a carboxypeptidase with optimum activity at pH 4.5-6.0. It is inhibited by diisopropyl fluorophosphate.

See also

• Cathepsin A

References

1. Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51: 83–128. doi:10.1007/bf02907561.
2. Valls LA, Hunter CP, Rothman JH, Stevens TH (March 1987). "Protein sorting in yeast: the localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide". Cell. 48 (5): 887–97. doi:10.1016/0092-8674(87)90085-7. PMID 3028649.
3. Jackman HL, Morris PW, Deddish PA, Skidgel RA, Erdös EG (February 1992). "Inactivation of endothelin I by deamidase (lysosomal protective protein)". The Journal of Biological Chemistry. 267 (5): 2872–5. PMID 1737744.
4. Miller JJ, Changaris DG, Levy RS (December 1992). "Purification, subunit structure and inhibitor profile of cathepsin A". Journal of Chromatography. 627 (1–2): 153–62. doi:10.1016/0021-9673(92)87195-e. PMID 1487525.

External links

• Carboxypeptidase+C at the U.S. National Library of Medicine Medical Subject Headings (MeSH)