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

BRENDA support

3.4.23.5: cathepsin D

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

Word Map on EC 3.4.23.5

Reaction

Specificity similar to, but narrower than, that of pepsin A. Does not cleave the Gln4-His bond in B chain of insulin =

Synonyms

BmCatD, CAD 1, CAD 2, CAD 3, CapD, Cat D, CAT-D, CatD, Cath D, cath-D, cathD, cathepsin D, cathepsin D-like proteinase, cathepsin D1, cathepsin D2, CD1, CTSD, EC 3.4.4.23, matCTSD, PCD, Pep4p, preproCatD, pro-cathepsin, pro-cathepsin D, pro-CD, pro-CtsD, proCat, proCDrec, proCTSD, Proteinase A

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.5 cathepsin D

General Stability

General Stability on EC 3.4.23.5 - cathepsin D

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
not completely stable to freezing. If freezing is followed by lyophilization, 35% loss of activity
-
rapid freezing of the brine at -80 °C does not cause any significant changes in enzyme activity, even after 3 freeze-thaw cycles
-
stable against repetitive freezing and thawing
-
stable upon freezing
-
the addition of progranulin to the proenzyme at a 3:1 molar ratio causes a significant destabilizing effect on the melting temperature of the proenzyme
-
the non-ionic detergents Tween-20 and Triton X-100 stabilize the enzyme activity. The enzyme is active until 2.5 M urea and is resistant to proteolysis by papain and renin. Glycerol (2.5-30% (v/v)) shows no stabilization effect on the activity of the enzyme. In 25% (v/v) methanol, the enzyme retains 100% of the activity
-
the protease is largely pressure stable at room temperature. At 100 MPa a significant stabilisation of the enzyme against temperature-induced inactivation is observed. Pressure drastically inhibits the cleavage by cathepsin D in Bis-Tris buffer (pH 6.0) causing a reduction of the catalytic rate of more than 50% at 100-400 MPa. The enzyme is relatively stable with more than 57% and 40% residual activity after 30 min treatment at 30°C and 300 MPa or 400 MPa, respectively. At higher pressures the enzyme is destabilised rapidly resulting in a residual activity of less than 10% after 30 min treatment at 600 MPa
-