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Literature summary for 3.1.3.2 extracted from
- N-glycosylation influences the latency and catalytic properties of mammalian purple acid phosphatase (2005), Arch. Biochem. Biophys., 435, 147-156.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| stable expression of wild-type enzyme in CHO-K1 cells, expression of wild-type and mutant enzymes in Spodopetra frugiperda Sf9 cells using the baculovirus infection system | Rattus norvegicus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| N128Q | site-directed mutagenesis, reduced N-glycosylation and slightly shifted pH optimum compared to the wild-type enzyme | Rattus norvegicus |
| N97Q | site-directed mutagenesis, reduced N-glycosylation and slightly shifted pH optimum compared to the wild-type enzyme | Rattus norvegicus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the enzyme is tartrate-insensitive | Rattus norvegicus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics, recombinant wild-type and mutant enzymes | Rattus norvegicus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe3+ | activates | Rattus norvegicus |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
Sprague-Dawley rats | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | N-glycosylated, detectable by Galanthus nivalis agglutinin | Rattus norvegicus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme from bone, recombinant enzyme from CHO-K1 cells, recombinant wild-type and mutant enzymes from Sf9 insect cells by cation exchange chromatography, ammonium sulfate fractionation, hydrophobic interaction chromatography, gel filtration, and heparin affinity chromatography | Rattus norvegicus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| bone | - |
Rattus norvegicus | - |
| femur | - |
Rattus norvegicus | - |
| tibia | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenyl phosphate + H2O | - |
Rattus norvegicus | 4-nitrophenol + phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 35000-37000, SDS-PAGE | Rattus norvegicus |
| More | cathepsin L proteolytically cleaved recombinant wild-type and mutant enzymes show two fragment of 16 and 23 kDa | Rattus norvegicus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PAP | - |
Rattus norvegicus |
| purple acid phosphatase | - |
Rattus norvegicus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Rattus norvegicus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 4.8 | 5 | recombinant wild-type and mutant enzymes | Rattus norvegicus |
| 5.8 | 6 | cathepsin L proteolytically cleaved recombinant wild-type and mutant enzymes | Rattus norvegicus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4.3 | 6.7 | - |
Rattus norvegicus |
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Release 2023.1 (January 2023)
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