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Literature summary for 3.4.11.21 extracted from
- Proteins of the kidney microvillar membrane. Aspartate aminopeptidase: purification by immunoadsorbent chromatography and properties of the detergent- and proteinase-solubilized forms (1980), Biochem. J., 189, 591-603.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | - |
Sus scrofa |  |
| Cu2+ | strongly inhibitory | Sus scrofa | |
| EDTA | strong inhibitory from 2 mM to 5 mM | Sus scrofa | |
| EGTA | slightly inhibitory from 2 mM to 5 mM | Sus scrofa | |
| Zn2+ | strongly inhibitory | Sus scrofa | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.35 | - |
Glu 2-naphthylamide | - |
Sus scrofa | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| microsome | - |
Sus scrofa | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ba2+ | activation | Sus scrofa | |
| Ca2+ | 4fold activation for Glu 2-naphthylamide at 0.1 mM and above | Sus scrofa | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 270000 | - |
native gel filtration of the proteinase treated form | Sus scrofa |
| 350000 | 400000 | native gel filtration of detergent-treated form | Sus scrofa |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sus scrofa | - |
pig | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| side-chain modification | carbohydrate | Sus scrofa |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 2000fold to homogeneity, Triton X-100 solubilized microsomal fraction, DEAE-cellulose chromatography, immunoadsorbent chromatography | Sus scrofa |
| proteinase solubilized microsomal fraction, DEAE-cellulose chromatography, immunoadsorbent chromatography to homogeneity | Sus scrofa |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| renal cortex | - |
Sus scrofa | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.07 | - |
- |
Sus scrofa |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Arg 2-naphthylamide + H2O | - |
Sus scrofa | Arg + 2-naphthylamine | - |
? | |
| Asp 2-naphthylamide + H2O | attacked more rapidly than 2-naphthylamide derivates of neutral or basic amino acids | Sus scrofa | Asp + 2-naphthylamine | - |
? | |
| Glu 2-naphthylamide + H2O | attacked more rapidly than 2-naphthylamide derivatives of neutral or basic amino acids | Sus scrofa | Glu + 2-naphthylamine | - |
? | |
| Lys 2-naphthylamide + H2O | - |
Sus scrofa | Lys + 2-naphthylamine | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | electron microscopy analysis, 6.5 nm diameter for each monomer | Sus scrofa |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| EC 3.4.11.7 | related | Sus scrofa |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
50% loss of activity in 20 min | Sus scrofa |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 7 | - |
Sus scrofa |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4.5 | 8.5 | outside the range little activity measurable | Sus scrofa |
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