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Literature summary for 3.4.23.34 extracted from

  • Abd-Elgaliel, W.R.; Tung, C.H.
    Selective detection of Cathepsin E proteolytic activity (2010), Biochim. Biophys. Acta, 1800, 1002-1008.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.23.34

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.94
-
 (7-methoxycoumarin-4-yl)acetyl-L-Ala-Gly-L-Phe-L-Ser-L-Leu-L-Pro-L-Ala-L-Lys(Dnp)-D-Arg-amide pH 4.0, 27°C Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(7-methoxycoumarin-4-yl)acetyl-L-Ala-Gly-L-Phe-L-Ser-L-Leu-L-Pro-L-Ala-L-Lys(Dnp)-D-Arg-amide + H2O due to the close proximity of a Mca-donor and a Dnp-acceptor, near complete intramolecular quenching effect is achieved in the substrate's intact state. After the proteolytic cleavage of the hydrophobic motif, both Mca and Dnp are further apart, resulting in bright fluorescence Homo sapiens (7-methoxycoumarin-4-yl)acetyl-L-Ala-Gly-L-Phe-L-Ser-L-Leu + L-Pro-L-Ala-L-Lys(Dnp)-D-Arg-amide substrate shows a 265fold difference in the net fluorescence signals between cathepsins E and D. This cathepsin E selectivity is established by having Leu-Pro residues at the scissile peptide bond ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
322.5
-
 (7-methoxycoumarin-4-yl)acetyl-L-Ala-Gly-L-Phe-L-Ser-L-Leu-L-Pro-L-Ala-L-Lys(Dnp)-D-Arg-amide pH 4.0, 27°C Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
167
-
 (7-methoxycoumarin-4-yl)acetyl-L-Ala-Gly-L-Phe-L-Ser-L-Leu-L-Pro-L-Ala-L-Lys(Dnp)-D-Arg-amide pH 4.0, 27°C Homo sapiens