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Literature summary for 3.4.22.15 extracted from

  • Ma, C.; Liang, K.; Tang, L.; He, S.; Liu, X.; He, M.; Li, Y.
    Identification and characteristics of a cathepsin L-like cysteine protease from Clonorchis sinensis (2019), Parasitol. Res., 118, 829-835 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His6-tagged mature domain of CsCPL (CsCPL-m) in inclusion bodies in Escherichia coli Clonorchis sinensis

Inhibitors

Inhibitors Comment Organism Structure
E-64 complete inhibition Clonorchis sinensis
iodoacetamide complete inhibition Clonorchis sinensis
additional information no inhibition by EDTA Clonorchis sinensis
PMSF low inhibition Clonorchis sinensis
TPCK strong inhibition Clonorchis sinensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00571
-
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin pH 5.5, 37°C, recombinant mature enzyme Clonorchis sinensis

Organism

Organism UniProt Comment Textmining
Clonorchis sinensis B5G4Y8
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant refolded His6-tagged mature domain of CsCPL (CsCPL-m) from inclusion bodies of Escherichia coli Clonorchis sinensis

Renatured (Commentary)

Renatured (Comment) Organism
recombinant His6-tagged mature domain of CsCPL (CsCPL-m) solubilized from Escherichia coli inclusion bodies by dialysis through stepwise dilution of urea (6 to 1 M) in 20 mM Tris-HCl and 5 mM EDTA buffer (pH 8.0). Finally, the urea is removed by dialysis using phosphate-buffered saline, pH 7.4 Clonorchis sinensis

Source Tissue

Source Tissue Comment Organism Textmining
cercaria
-
Clonorchis sinensis
-
metacercaria
-
Clonorchis sinensis
-
additional information the cathepsin L-like protease of Clonorchis sinensis is detected in the cercaria, metacercaria, and adult worm stages by immunolocalization Clonorchis sinensis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
-
Clonorchis sinensis benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
?
Bovine serum albumin + H2O
-
Clonorchis sinensis ?
-
?
Gelatin + H2O
-
Clonorchis sinensis ?
-
?
additional information no activity with benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin. The recombinant CsCPL-m can degrade bovine serum albumin and gelatin, but can not degrade human hemoglobin and human immunoglobulin G Clonorchis sinensis ?
-
?

Synonyms

Synonyms Comment Organism
cathepsin L-like cysteine protease
-
Clonorchis sinensis
CsCPL
-
Clonorchis sinensis
CsCPL-m
-
Clonorchis sinensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
42
-
-
Clonorchis sinensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
-
Clonorchis sinensis

pH Range

pH Minimum pH Maximum Comment Organism
4 8 over 50% of maximal activity within this range, profile overview Clonorchis sinensis

General Information

General Information Comment Organism
evolution cathepsin L-like protease is an important member of the papain-like cysteine protease and plays numerous indispensable roles in the biology of parasitic organisms Clonorchis sinensis
additional information the catalytic triad is formed by conserved residues Cys177, His318, and Asn338 Clonorchis sinensis
physiological function enzyme CsCPL might participate in the catabolism of host proteins for nutrition during the parasitic life cycle of Clonorchis sinensis Clonorchis sinensis