Crystallization (Comment) | Organism |
---|---|
purified inactivated cathepsin L mutant C25S, method optimization, rod-shaped crystals grow within 2 weeks in 0.1 M bis-Tris-HCl, pH 5.5, and 2 M ammonium sulfate, cube-shaped crystals grow within 2 weeks in 0.11 M HEPES-NaOH, pH 7.5, and 2.14 M ammonium sulfate, X-ray diffraction structure determination and analysis at 1.42 A resolution. The cathepsin L molecule is cleaved autocatalytically, with the cleaved region trapped in the active site cleft of the neighboring molecule demonstrated remaining low levels of catalytic activity | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
C25S | site-directed mutagenesis, almost inactive mutant that still performs autocatalytic cleavage | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
lysosome | - |
Homo sapiens | 5764 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P07711 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | the proenzyme performs autocatalytic cleavage resulting in the mature enzyme | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme performs autocatalytic cleavage | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
cathepsin L1 | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | - |
assay at | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
malfunction | the C25S mutation abolishes the enzyme activity | Homo sapiens |
additional information | cathepsin L's structure reveals the fold of the papain-like enzyme composed of two domains named left (L-) and right (R-). The L-domain is alpha-helical, whereas the R-domain forms a beta-barrel fold. Between the two domains, locates a V-shaped active site cleft on which the L- and R-domain catalytic residues C25 and H163 are positioned | Homo sapiens |
physiological function | cathepsin L is a ubiquitously expressed papain-like cysteine protease involved in the endosomal degradation of proteins and has numerous roles in physiological and pathological processes, such as arthritis, osteoporosis, and cancer | Homo sapiens |