Activating Compound | Comment | Organism | Structure |
---|---|---|---|
dithiothreitol | the cathepsins L needed the presence of dithiothreitol to digest IgG1, IgG2, and IgG4 whereas IgG3 was identically cleaved under both reducing and nonreducing conditions | Fasciola hepatica |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Fasciola hepatica | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Fasciola hepatica |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
16.2 | - |
substrate: tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide | Fasciola hepatica |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
human IgG + H2O | both cathepsins L produce similar degradation patterns and cleave all human IgG subclasses at the hinge region, yielding at pH 7.3 and 37°C Fab and Fc fragments in the case of IgG1 and IgG3 or Fab(2) and Fc in IgG2 and IgG4. Both liver fluke cathepsins L cleave the peptide bonds 237His-Thr, 237Glu-Cys, 233Gly-Asp, and 241Ser-Cys of the gamma1, gamma2, gamma3, and gamma4 H chains, respectively. Therefore, the enzymes are interacting with the following P3-P'3 sequences, Lys-Thr-His-Thr-Cys-Pro, Cys-Val-Glu-Asp-Pro-Pro, Pro-Leu-Gly-Asp-Thr-Thr, and Cys-Pro-Ser-Cys-Pro-Ala. The specificity of the liver fluke cathepsins L for peptide bonds in proteins is less defined. The P1 position, for instance, can be occupied by hydrophobic, hydrophilic, acidic, or basic residues. The P3 and P2 positions are occupied by hydrophobic amino acids with the exception of the gamma1 sequence which contains a basic lysine and a hydrophilic threonine, respectively. In addition the specificity between the enzyme and its substrate would depend on which of the amino acids of the substrate can be really exposed to the active site | Fasciola hepatica | ? | - |
? | |
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O | - |
Fasciola hepatica | tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin | - |
? |
Synonyms | Comment | Organism |
---|---|---|
cathepsin L1 | - |
Fasciola hepatica |
CL1 | - |
Fasciola hepatica |