3.4.16.5: carboxypeptidase C

This is an abbreviated version!
For detailed information about carboxypeptidase C, go to the full flat file.

Reaction

release of a C-terminal amino acid with broad specificity =

Synonyms

A-type metallocarboxypeptidase, acidic serine carboxypeptidase, AtCPY, BRS1, carboxypeptidase a, carboxypeptidase A4, carboxypeptidase C, Carboxypeptidase II, carboxypeptidase Y, carboxypeptidase YSCY, carboxypeptidase-Y, Case, CatA, CathA, cathepsin A, CaY, CP-MI, CP-MIII, CP-WIII, CPA4, CPase, CPC, CPD-Y, CPW, CPY, Cpy1p, CTSA, Cxp1, deamidase, EC 3.4.12.1, EC 3.4.16.1, EC 3.4.16.3, hCath A, HPP, lysosomal carboxypeptidase A, lysosomal protective protein, MO54, More, MpiCP-1, MpiCP-2, Phaseolin, PpcA, PRC1, proCPY, protective protein cathepsin A, protective protein/cathepsin A, retinoid-inducible serine carboxypeptidase, SCP, Scpep1, Ser carboxypeptidase, Ser carboxypeptidase-like protein, serine carboxypeptidase, serine carboxypeptidase 1, serine carboxypeptidase I, serine carboxypeptidase Scpep1, SmSCP-1, TcCBP

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.16 Serine-type carboxypeptidases

                3.4.16.5 carboxypeptidase C

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Results	in table
15	Activating Compound
133	AA Sequence
4	Application
1	CAS Registry Number
17	Cloned(Commentary)
1	Cofactor
9	Crystallization (Commentary)
369	Disease/ Diagnostics
1	Expression
10	General Information
8	General Stability
57	IC50 Value
221	Inhibitors
27	Ki Value [mM]
126	KM Value [mM]
28	Localization
22	Metals/Ions
40	Molecular Weight [Da]
7	Natural Substrates/ Products (Substrates)
6	Organic Solvent Stability
204	Organism
23	PDB ID
20	pH Optimum
6	pH Range
20	pH Stability
7	pI Value
24	Posttranslational Modification
77	Protein Variants
25	Purification (Commentary)
1	Reaction
3	Reaction Type
127	Reference
2	Renatured (Commentary)
66	Source Tissue
9	Specific Activity [micromol/min/mg]
2	Storage Stability
269	Substrates and Products (Substrate)
13	Subunits
152	Synonyms
12	Temperature Optimum [°C]
2	Temperature Range [°C]
13	Temperature Stability [°C]
122	Turnover Number [1/s]

Application

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Application on EC 3.4.16.5 - carboxypeptidase C

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

analysis

Saccharomyces cerevisiae

-

application of CPY as sensing element in a biosensor for the direct detection of ochratoxin A and comparison with thermolysin. Thermolysin and CPY both exhibit an optimal activity under the conditions 35 min cross-linking time, working pH of 7 and temperature of 25°C and exhibit comparable analytical performances in the biosensor. Ochratoxin A concentrations can be determined without pretreatment of the sample and no matrix effect is observed

752485

molecular biology

Saccharomyces cerevisiae

P00729

a method is described exploiting the possibility to attach different reactive handles to their C-termini using a reaction catalyzed by CPY. It is possible to attach pairs of reaction handles which can react with each other to each of the peptides to be coupled. In a second step, the two modified peptides can be linked together by a chemical reaction, such as an oxime-forming reaction or a copper(I) catalyzed (2+3)-cycloaddition reaction of an azide with an alkyne

700586

nutrition

Monascus pilosus

-

MpiCP-1 suppresses and reverses the development of the bitterness taste that results from the pepsin hydrolysis of soybean protein by releasing mainly hydrophobic amino acids from the C-termini of the bitter components

665936

synthesis

Saccharomyces cerevisiae

P00729

synthesis of CPY in Pichia pastoris as procarboxypeptidase Y with a yield of about 605 mg/l in shake-flasks after 168 h induction with 1 % (v/v) methanol. This precursor is cleaved by endogenous proteinases of Pichia pastoris and released into the fermentation broth as active carboxypeptidase Y within 2 weeks at 10°C. The recombinant enzyme is optimally active at 30°C and pH 6.0, with an optimal activity of about 305 U/mg

753050