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.

References[edit]

^ 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.

External links[edit]

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

Hydrolase: proteases (EC 3.4)

3.4.11-19: Exopeptidase

3.4.11	Aminopeptidase Alanine Arginyl Aspartyl Cystinyl Leucyl Glutamyl Methionyl 1 2 O
3.4.13	Dipeptidase 1 2 3
3.4.14	Dipeptidyl peptidase Cathepsin C Dipeptidyl peptidase-4 Tripeptidyl peptidase Tripeptidyl peptidase I Tripeptidyl peptidase II
3.4.15	Angiotensin-converting enzyme
3.4.16	Serine type carboxypeptidases: Cathepsin A DD-transpeptidase
3.4.17	Metalloexopeptidases Carboxypeptidase A A2 B C E Glutamate II
Other/ungrouped	Metalloexopeptidase

3.4.21-25: Endopeptidase

Other/ungrouped: Amyloid precursor protein secretase

3.4.99: Unknown

Staphylokinase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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