Carboxypeptidase C Explained
| Carboxypeptidase C |
| Ec Number: | 3.4.16.5 |
| Cas Number: | 9046-67-7 |
Carboxypeptidase C (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
Notes and References
- Serine carboxypeptidases. A review . Breddam, K. . Carlsberg Res. Commun. . 1986 . 51 . 83–128 . 10.1007/bf02907561. free .
- Valls LA, Hunter CP, Rothman JH, Stevens TH . Protein sorting in yeast: the localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide . Cell . 48 . 5 . 887–97 . March 1987 . 3028649 . 10.1016/0092-8674(87)90085-7 .
- Jackman HL, Morris PW, Deddish PA, Skidgel RA, Erdös EG . Inactivation of endothelin I by deamidase (lysosomal protective protein) . The Journal of Biological Chemistry . 267 . 5 . 2872–5 . February 1992 . 1737744 .
- Miller JJ, Changaris DG, Levy RS . Purification, subunit structure and inhibitor profile of cathepsin A . Journal of Chromatography . 627 . 1-2 . 153–62 . December 1992 . 1487525 . 10.1016/0021-9673(92)87195-e .
