Literature summary for 3.4.23.34 extracted from

Ostermann, N.; Gerhartz, B.; Worpenberg, S.; Trappe, J.; Eder, J.
Crystal structure of an activation intermediate of cathepsin E (2004), J. Mol. Biol., 342, 889-899.

Search for more literature for 3.4.23.34

Cloned(Commentary)

Cloned (Comment)	Organism
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	Homo sapiens

Cloned (Comment)

Organism

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

Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
DED-[5-[(2-aminoethyl)amino]naphthalene-1-sulfonyl]-KPILFFRLGK-[4-(4-dimethylaminophenylazo)benzoic acid] + H2O	-	Homo sapiens	?	-	?