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

  1. ↑ Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51: 83–128. doi:10.1007/bf02907561.
  2. ↑ Valls, L.A., Hunter, C.P., Rothman, J.H. and 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.
  3. ↑ Jackman, H.L., Morris, P.W., Deddish, P.A., Skidgel, R.A. and Erdös, E.G. (1992). "Inactivation of endothelin I by deamidase (lysosomal protective protein)". J. Biol. Chem. 267: 2872–2875. PMID 1737744.
  4. ↑ Miller, J.J., Changaris, D.G. and 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

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