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Literature summary for 3.4.14.1 extracted from

  • Rebernik, M.; Lenarcic, B.; Novinec, M.
    The catalytic domain of cathepsin C (dipeptidyl-peptidase I) alone is a fully functional endoprotease (2019), Protein Expr. Purif., 157, 21-27 .
    View publication on PubMed
Search for more literature for 3.4.14.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information a recombinant form of cathepsin C lacking its exclusion domain is a monomer with endoprotease activity and affinity for hydrophobic residues such as Phe, Leu or Pro, but not Val, in the P2 position Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0023
-
 benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin recombinant truncated cathepsin C, pH 5.5, 25°C Homo sapiens
0.0028
-
 t-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin recombinant truncated cathepsin C, pH 5.5, 25°C Homo sapiens
0.0065
-
 benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin recombinant truncated cathepsin C, pH 5.5, 25°C Homo sapiens
0.028
-
 benzyloxyarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin recombinant truncated cathepsin C, pH 5.5, 25°C Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
NaCl optimal activity between 50 and 200mM NaCl for recombinant truncated cathepsin C. Variant's enzyme activity in the presence of 0.15 mM NaCl is about 55% of optimal activity Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P53634
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyloxyarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
-
 Homo sapiens benzyloxycarbonyl-Gly L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
 ?
benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
-
 Homo sapiens benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
 ?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
-
 Homo sapiens benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
 ?
t-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
-
 Homo sapiens t-butyloxycarbonyl-L-Val-L-Leu-Lys + 7-amino-4-methylcoumarin
-
 ?

Synonyms

Synonyms Comment Organism
CTSC
-
 Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.13
-
 benzyloxyarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin recombinant truncated cathepsin C, pH 5.5, 25°C Homo sapiens
0.16
-
 t-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin recombinant truncated cathepsin C, pH 5.5, 25°C Homo sapiens
0.18
-
 benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin recombinant truncated cathepsin C, pH 5.5, 25°C Homo sapiens
0.23
-
 benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin recombinant truncated cathepsin C, pH 5.5, 25°C Homo sapiens

General Information

General Information Comment Organism
physiological function a recombinant form of cathepsin C lacking its exclusion domain is a monomer with endoprotease activity and affinity for hydrophobic residues such as Phe, Leu or Pro, but not Val, in the P2 position. As opposed to cathepsin C, it does not require chloride ions for its activity. Recombinant truncated cathepsin C has elastolytic and gelatinolytic activity comparable to other cysteine cathepsins Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.6
-
 benzyloxyarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin recombinant truncated cathepsin C, pH 5.5, 25°C Homo sapiens
35
-
 benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin recombinant truncated cathepsin C, pH 5.5, 25°C Homo sapiens
57
-
 t-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin recombinant truncated cathepsin C, pH 5.5, 25°C Homo sapiens
78
-
 benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin recombinant truncated cathepsin C, pH 5.5, 25°C Homo sapiens