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Literature summary for 3.4.16.5 extracted from
- Proteolytic activation of human cathepsin A (2014), J. Biol. Chem., 289, 11592-11600.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed as a flagged tagged fusion protein in Tn5 insect cells | Homo sapiens |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure of mature cathepsin A is determined to 2.8 A resolution | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| R262A/R292A | double mutant also undergoes processing to form large and small subunits, suggesting alternative avenues for the maturation of cathepsin A | Homo sapiens |
| S150A/R284A/R298A | triple mutant S150A/R284A/R298A also undergoes cleavage into large and small subunits, comparable with the wildtype cathepsin A, suggesting that these sites are not mandatory for the activation of cathepsin A | Homo sapiens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.04 | - |
CBZ-Phe-Leu | recombinant protein, pH 4.5, 27°C | Homo sapiens |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 51100 | - |
MALDI-TOF, mature protein. Enzymatic activity increases with maturation of Cathepsin A to the 51.1 kDa form | Homo sapiens |
| 54400 | - |
MALDI-TOF, zymogen protein | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P10619 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | the activation of precursor cathepsin A is achieved by proteolytic removal of a larger 3.3-kDa peptide that includes the blocking peptide, bypassing the requirement for conformational changes | Homo sapiens |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| using affinity and ion-exchange chromatography | Homo sapiens |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
enzymatic activity increases with maturation of cathepsin A to the 51.1 kDa form | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| CBZ-Phe-Leu + H2O | - |
Homo sapiens | N-benzyloxycarbonyl-L-Phe + L-leucine | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CatA | - |
Homo sapiens |
| cathepsin A | - |
Homo sapiens |
| CTSA | - |
Homo sapiens |
| HPP | - |
Homo sapiens |
| PpcA | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 27 | - |
assay at | Homo sapiens |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 12.1 | - |
CBZ-Phe-Leu | recombinant protein, pH 4.5, 27°C | Homo sapiens | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 4.5 | - |
assay at | Homo sapiens |
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Release 2023.1 (January 2023)
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