Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.4.16.5: carboxypeptidase C

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

Word Map on EC 3.4.16.5

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

General Stability

General Stability on EC 3.4.16.5 - carboxypeptidase C

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
citrus peel enzyme is inactivated upon lyophilization
Citrus sp.
-
orange leaf enzyme is stable to lyophilization
Citrus sp.
-
orange peel enzyme is inactivated upon lyophilization
Citrus sp.
-
pressure-induced denaturation is a process involving at least three transitions. Low pressure, below 150 mPa, induces slight conformational changes characterized by a slight decrease in the center of the spectral mass of intrinsic fluorescence, whereas no changes in 8-anilino-1-naphthalene sulfonic acid binding fluorescence are observed and 80% of the catalytic activity remains. Higher pressure, 150-500 mPa, induce further conformatiinal changes, characterized by a large decrease in the center of the spectral mass of intrinsic fluorescence, a large increase in the 8-anilino-1-naphthalene sulfonic acid binding fluorescence and the loss of all catalytic activity. A further increase in pressure, above 550 mPa induces transition from this first molten globule-like state to a second malten globule-like state. A similar three-transition process is found for unglycosylated carboxypeptidase Y, but the first two transitions clearly occur at lower pressures than those for glycosylated carboxypeptidase Y
-
the carboxypeptidase Y is composed of two structural domains which unfold independently, procarboxypeptidase Y behaves as a single domain, thus ensuring cooperative unfolding. The carbohydrate moiety has a slightly protective role in heat-induced unfolding and highly protective role in pressure-induced unfolding
-
urea, 6 M, about 80% of activity is retained after 1 h
-
when the enzyme is treated at pressures higher than 300 mPa and temperatures lower than -5°C, it undergoes an irreversible inactivation in which nearly 50% of the alpha-helical structure is lost as judged by circular dichroism spectral analysis. When the applied pressure is limited to below 200 mPa, the cold inactivation process appears to be reversible. In the presence of reducing agent, this reversible phenomenon, observed at below 200 mPa, diminishes to give an inactive enzyme
-