| 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 | ||||||||
| |||||||||
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.
- ^ Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51: 83–128. doi: 10.1007/bf02907561.
- ^ 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.
- ^ 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.
- ^ 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.
- Carboxypeptidase+C at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| 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 | ||||||||
| |||||||||
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.
- ^ Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51: 83–128. doi: 10.1007/bf02907561.
- ^ 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.
- ^ 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.
- ^ 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.
- Carboxypeptidase+C at the U.S. National Library of Medicine Medical Subject Headings (MeSH)