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

BRENDA support

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

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

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.34 cathepsin E

Cloned

Cloned 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.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of two fusion proteins using chimeric DNAs encoding the cathepsin E propeptide fused to the mature cathepsin D tagged with HA at the COOH terminus and encoding the cathepsin D propeptide fused to the mature cathepsin E
-
expressed in Chinese hamster ovary cells
-
expressed in Escherichia coli BL21(DE3)pLysS
-
expressed in Pichia pastoris cells
-
expression in HEK293T cells of wild-type and mutant form
-
guinea pig
HEK-293 cells are transfected with the full length human cathepsin E gene cloned into pcDNA3.1V5His
-
heterologously expressed in human embryonic kidney 293T cells
-
human
human (gastric adenocarcinoma)
-
human pro-cathepsin E is expressed in Escherichia coli in the form of inclusion bodies. The protein is dissolved in 8 M guanidinium chloride and refolded by dilution/dialysis. The main side products in the refolding reaction were soluble, high molecular mass protein complexes linked most likely due to formation of wrong intra- and intermolecular disulfide bonds. Pro-cathepsin E auto-activates at pH 3.5. The major part of the high molecular mass complexes is easily removed during the auto-activation process as these protein components precipitate during the pH shifts
-
mutants with changed active-site residues and lacking propeptides and N-glycosylation, expressed in human embryonic kidney 293T cells
-
procathepsin E
rabbit
stable expression in human prostate carcinoma cell line ALVA101, product is named ALVA101/hCE
-