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]

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RENATURED/Commentary

ORGANISM

UNIPROT

LITERATURE

efficient folding of carboxypeptidase Y is dependent on the presence of the proregion. Thus denatured pro-carboxypeptidase Y, in contrast to the mature enzyme, refolds efficiently in vitro in low ionic strength buffers. Under these conditions denatured mature carboxypeptidase Y forms an inactive, soluble folding intermediate

Saccharomyces cerevisiae

-

647196

the denatured His-tagged carboxypeptidase propeptide is refolded by dilution 1:60 into the renaturation buffer, 50 mM Tris-HCl containing 0.5 M NaCl and 3 mM EDTA, pH 8.0. The denatured carboxypeptidase is refolded by dilution 1:60 into the reanturation buffer containing containing His-tagged carboxypeptidase propeptide at various concentrations. Increasing the molar ratio of His-tagged carboxypeptidase propeptide to carboxypeptidase results in an increase in the carboxypeptidase refolding yield, indicating that the His-tagged carboxypeptidase propeptide plays a chaperone-like role in in vitro folding of the carboxypeptidase. When refolding is carried out in the presence of 10 molar equivalent His-tagged carboxypeptidase propeptide the specific activity, N-(2-furanacryloyl)-Phe-Phe hydrolysis activity per mg of protein, is 63% of that of the native enzyme

Saccharomyces cerevisiae

-

647225