3.4.23.34: cathepsin E

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

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

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
12	Activating Compound
695	AA Sequence
7	Application
1	CAS Registry Number
34	Cloned(Commentary)
16	Cofactor
1	Crystallization (Commentary)
372	Disease/ Diagnostics
3	Expression
3	General Information
2	General Stability
15	IC50 Value
118	Inhibitors
1	kcat/KM [mM/s]
18	Ki Value [mM]
51	KM Value [mM]
65	Localization
1	Metals/Ions
55	Molecular Weight [Da]
6	Natural Substrates/ Products (Substrates)
70	Organism
2	PDB ID
12	pH Optimum
9	pH Range
18	pH Stability
1	pI Value
18	Posttranslational Modification
13	Protein Variants
25	Purification (Commentary)
1	Reaction
2	Reaction Type
70	Reference
193	Source Tissue
7	Specific Activity [micromol/min/mg]
3	Storage Stability
157	Substrates and Products (Substrate)
35	Subunits
35	Synonyms
19	Temperature Optimum [°C]
10	Temperature Stability [°C]
60	Turnover Number [1/s]

Crystallization

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Crystallization 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.

top print hide Go to Crystallization (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

sitting drop vapor diffusion, crystal structure of an activation intermediate of cathepsin E at 2.35 A resolution. The overall structure follows the general fold of aspartic proteases of the A1 family, and the intermediate shares many features with the intermediate 2 on the proposed activation pathway of aspartic proteases like pepsin C and cathepsin D. The pro-sequence is cleaved from the protease and remains stably associated with the mature enzyme by forming the outermost sixth strand of the interdomain beta-sheet

Homo sapiens

-

669836