3.4.23.34: cathepsin E
This is an abbreviated version!
For detailed information about cathepsin E, go to the full flat file.
Word Map on EC 3.4.23.34
-
3.4.23.34
-
cathepsins
-
proteinases
-
pepstatin
-
pepsinogen
-
procathepsin
-
molecular biology
-
gastricsin
-
medicine
-
foveolar
-
non-lysosomal
-
3.4.23.5
- 3.4.23.34
- cathepsins
- proteinases
- pepstatin
- pepsinogen
-
procathepsin
- molecular biology
- gastricsin
- medicine
-
foveolar
-
non-lysosomal
-
3.4.23.5
Reaction
similar to cathepsin D, but slightly broader specificity =
Synonyms
CatE, Cathepsin D-like acid proteinase, cathepsin D-like aspartic proteinase, cathepsin D-like protease, Cathepsin D-type proteinase, cathepsin E, Cathepsin E-like acid proteinase, CE, CTSE, EMAP, erythrocyte membrane acid proteinase, Erythrocyte membrane aspartic proteinase, gastric mucosa non-pepsin acid proteinase, More, Non-pepsin proteinase, slow moving proteinase, Slow-moving proteinase, SMP
ECTree
Advanced search results
Temperature Stability
Temperature Stability on EC 3.4.23.34 - cathepsin E
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
28
-
2 h, enzyme dimer: 60% loss of activity at pH 4, 45% at pH 5, 20% at pH 6 and pH 8.8, stable at pH 7, 10% loss of activity at pH 8, enzyme monomer: 65% loss of activity at pH 4, 55% at pH 5, 20% at pH 6, 10% at pH 7, 50% at pH 7.5, 70% at pH 8 and 95% at pH 8.8
37
55
additional information
-
20 min, inactivation of native enzyme at pH 5.5, only 10% loss of recombinant enzyme activity
55
-
t1/2: 35 min (native enzyme) or 1.7 min (recombinant enzyme) at pH 7.5, t1/2: less than 5 min at pH 8.5
-
no difference in thermostability between recombinant and native enzyme forms
additional information
-
the temperature stability of the mutant monomeric form in alkaline solution is markedly reduced