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Literature summary for 3.4.22.15 extracted from

  • Schilling, K.; Körner, A.; Sehmisch, S.; Kreusch, A.; Kleint, R.; Benedix, Y.; Schlabrakowski, A.; Wiederanders, B.
    Selectivity of propeptide-enzyme interaction in cathepsin L-like cysteine proteases (2009), Biol. Chem., 390, 167-174.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information native cathepsin L was completely inhibited by 0.001, 0.004, or 0.01 mM cathepsin L propeptide (10 min, pH 6.5, room temperature) Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Renatured (Commentary)

Renatured (Comment) Organism
the optimum cathepsin L renaturation buffer consists of 50 mM Tris, 4 mM GSH, 0.5 mM GSSG, 300 mM MgSO4, 0.05% (w/v) 3-(3-cholamidopropyl)-dimethylammonio-1-propane sulfonate, 0.04 mM propetide, at pH 7.75 and 16°C Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
-
Homo sapiens benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
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