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 number3.4.16.5
CAS number9046-67-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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 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.
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