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
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3.4.23.5
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lysosomal
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pepstatin
-
estrogen
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metastasis
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alzheimer
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proteinases
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aspartyl
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node
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vacuole
-
lymph
-
renin
-
pepsin
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endosomes
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progesterone
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hydrolases
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endocytic
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phagosomes
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amyloid
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beta-glucuronidase
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plasminogen
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mannose
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6-phosphate
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axillary
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autophagosomes
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saposins
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lysosomal-associated
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leupeptin
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plasmepsins
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beta-hexosaminidase
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missorting
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mannose-6-phosphate
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chymosin
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lysotracker
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lipofuscinosis
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lc3-ii
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autophagy-lysosomal
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rab7
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ceroid
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estrogen-regulated
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immunoradiometric
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medicine
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lc3
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lamp-1
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node-negative
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trans-golgi
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upa
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endocytosed
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node-positive
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c-erbb-2
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autolysosomes
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cation-independent
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molecular biology
- 3.4.23.5
- lysosomal
- pepstatin
- estrogen
- metastasis
- alzheimer
- proteinases
-
aspartyl
- node
- vacuole
- lymph
- renin
- pepsin
- endosomes
- progesterone
- hydrolases
-
endocytic
-
phagosomes
-
amyloid
- beta-glucuronidase
- plasminogen
- mannose
- 6-phosphate
-
axillary
-
autophagosomes
-
saposins
-
lysosomal-associated
- leupeptin
-
plasmepsins
- beta-hexosaminidase
-
missorting
- mannose-6-phosphate
- chymosin
-
lysotracker
- lipofuscinosis
-
lc3-ii
-
autophagy-lysosomal
- rab7
-
ceroid
-
estrogen-regulated
-
immunoradiometric
- medicine
- lc3
- lamp-1
-
node-negative
-
trans-golgi
- upa
-
endocytosed
-
node-positive
-
c-erbb-2
-
autolysosomes
-
cation-independent
- molecular biology
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
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Temperature Stability
Temperature Stability on EC 3.4.23.5 - cathepsin D
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20 - 65
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completely stable between 20 and 40°C, thereafter activity decreases continuously, 20% loss of activity at 50°C, 80% loss of activity at 60°C, complete inactivation at 65°C
25 - 60
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the protease is heat stable at ambient pressure up to 300 MPa and 55°C, respectively, causing less than 10% inactivation after 10 min treatment. Cathepsin D is quickly inactivated at temperatures above 60°C
37
40
45 - 55
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the protease begins to thermally unfold above 45°C, with a melting temperature of 53°C. The enzyme is inactivated at 55°C
46
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heat inactivation proceeds linearly with time for the control enzyme but biphasically for the enzyme from animals with experimental neurofibrillary changes
5 - 45
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the enzyme is highly stable at temperatures below 45°C but activity declines rapidly at temperatures exceeding 50°C no activity is detected after incubation at 65°C for 60 min
50
54
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10 min, 13% loss of activity at pH 3.5, complete loss of activity at pH 7.5
55
60
70
60
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10 min, 35% loss of activity at pH 3.5, complete loss of activity at pH 7.5
60
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10 min, pH 3.8 or pH 7.0, loss of a large portion of activity of enzyme form cathepsin D-I and cathepsin D-II
60
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stable in presence of substrate, 95% inactivation after 60 min, in absence of substrate
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complete loss of activity in absence of substrate, 60% loss of activity in presence of substrate