Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | the autocatalytic processing of procathepsin B is triggered by proenzyme activity, overview | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
expression of recombinant human procathepsin B and cathepsin B in Escherichia coli | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
K39A/R40A | site-directed mutagenesis, the mutant procathepsin B performs autocatalytic activation 2fold faster compared to the wild-type variant | Homo sapiens |
L41A | site-directed mutagenesis, the mutant procathepsin B performs autocatalytic activation 2fold faster compared to the wild-type variant | Homo sapiens |
additional information | autocatalytic activation of procathepsin B is largely insensitive to mutations in the cleavage site region | Homo sapiens |
R40A | site-directed mutagenesis, the mutant procathepsin B performs autocatalytic activation 2fold faster compared to wild-type variant | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
DCG-04 | an E-64-type inhibitor, inhibits both mature cathepsin B and its zymogen | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | autocatalytic activation of procathepsin B is largely insensitive to mutations in the cleavage site region and can proceed at neutral pH when bound to heparin and other negatively charged surfaces, which may account for an extracellular physiological role of cathepsins | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | the autocatalytic processing of procathepsin B is triggered by proenzyme activity, overview | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | autocatalytic activation of procathepsin B is largely insensitive to mutations in the cleavage site region and can proceed at neutral pH when bound to heparin and other negatively charged surfaces, which may account for an extracellular physiological role of cathepsins | Homo sapiens | ? | - |
? | |
additional information | procathepsin B shows autocatalytic processing triggered by proenzyme activity, identification of cleavage sites and initiation mechanism, overview. A multi-step process, starting with a unimolecular conformational change of the zymogen, which unmasks the active site and, in the presence of negatively charged molecules and/or surfaces, also converts the zymogen into a better substrate, followed by the bimolecular proteolytic removal of the propeptide | Homo sapiens | ? | - |
? | |
N-benzyloxycarbonyl-L-arginyl-L-arginyl-4-methylcoumarin 7-amide + H2O | substrate of mature cathepsin B, also procathepsin B is catalytically active on the synthetic substrate but to a lower extent. The unfolded proenzymeis inactive | Homo sapiens | N-benzyloxycarbonyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
hydrolytic enzyme assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
4.5 | - |
in vitro autocatalytic processing of procathepsin B | Homo sapiens |
7.6 | - |
hydrolytic enzyme assay at | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | autocatalytic activation of procathepsin B can proceed at neutral pH when bound to heparin and other negatively charged surfaces, which may account for an extracellular physiological role of cathepsins | Homo sapiens |