Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-naphthyl-alanine | - |
Rattus norvegicus | |
4-nitro-L-phenylalanine | inactivation rate is 3.0 mM/min | Rattus norvegicus | |
citrulline | - |
Rattus norvegicus | |
Cys (S-benzyl) | - |
Rattus norvegicus | |
homophenylalanine | - |
Rattus norvegicus | |
leupeptin | leupeptin lacks selectivity since it inhibits both serine and cysteine proteases | Rattus norvegicus | |
additional information | inhibitory potency of a series benzyloxycarbonyl-Phe-X-diazomethylketone, in which Phe promotes binding at S2 while the amino acid X probes S1. The S1 region of cathepsin L also has the ability to accommodate large hydrophobic side chains. In this respect cathepsin L differs from cathepsin B. Thus benzyloxycarbonyl-Phe-Tyr(O-l-butyl)-diazomethylketone, inactivates cathepsin L with higher efficiency compared to cathepsin B | Rattus norvegicus | |
Ser-(O-benzyl) | - |
Rattus norvegicus | |
Thr (O-tert-butyl) | - |
Rattus norvegicus | |
Trp | inactivation rate is 12 mM/min | Rattus norvegicus | |
Tyr-(O-methyl) | inactivation rate is 1.548 mM/min | Rattus norvegicus | |
Tyr-(O-tert-butyl) | inactivation rate is 0.618 mM/min | Rattus norvegicus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
lysosome | - |
Rattus norvegicus | 5764 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | P00787 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | - |
Rattus norvegicus | - |
Synonyms | Comment | Organism |
---|---|---|
cathepsin B | - |
Rattus norvegicus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Rattus norvegicus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.4 | - |
assay at | Rattus norvegicus |
General Information | Comment | Organism |
---|---|---|
additional information | the substrate peptide bond cleaved by cathepsin B (EC 3.4.22.1) and cathepsin L (EC 3.4.22.15) is determined not by the amino acid contributing the carboxyl group to this bond as in the case of serine proteases but rather by the presence of a neighboring amino acid with a large hydrophobic side chain, active center differences between cathepsins L and B in the S1 binding region, overview | Rattus norvegicus |