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Literature summary for 3.4.11.7 extracted from
- Aminopeptidase A (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds) Academic Press, 2nd. Ed. 1, 299-303.
No PubMed abstract available
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 1,10-phenanthroline | - |
Rattus norvegicus |  |
| Cd2+ | complete inhibition at 1 mM | Rattus norvegicus | |
| Cu2+ | complete inhibition at 1 mM | Rattus norvegicus | |
| EC33 | specific inhibition | Rattus norvegicus | |
| EDTA | - |
Rattus norvegicus | |
| EGTA | - |
Rattus norvegicus | |
| Hg2+ | complete inhibition at 1 mM | Rattus norvegicus | |
| Ni2+ | complete inhibition at 1 mM | Rattus norvegicus | |
| RB150 | selective and specific prodrug of the enzyme inhibitor EC33, inhibits the enzyme given i.v. to rats | Rattus norvegicus | |
| Zn2+ | complete inhibition at 1 mM | Rattus norvegicus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytoplasm | the enzyme has cytosolic and transmembrane regions | Rattus norvegicus | 5737 | - |
| membrane | the enzyme has cytosolic and transmembrane regions | Rattus norvegicus | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | activates | Rattus norvegicus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 45000 | 400000 | dependent on the tissue source and purification method | Rattus norvegicus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| brain | - |
Rattus norvegicus | - |
| enterocyte | intestinal, brush border | Rattus norvegicus | - |
| hypothalamus | - |
Rattus norvegicus | - |
| kidney | brush border | Rattus norvegicus | - |
| additional information | broad tissue distribution | Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme catalyzes the hydrolysis of N-(alpha-L-glutamyl)- moieties more efficiently than the hydrolysis of alpha-L-aspartyl derivatives | Rattus norvegicus | ? | - |
? | |
| N-(alpha-L-glutamyl)-4-nitroanilide + H2O | - |
Rattus norvegicus | L-glutamic acid + 4-nitroaniline | - |
? | |
| N-(alpha-L-glutamyl)-beta-naphthylamide + H2O | - |
Rattus norvegicus | L-glutamic acid + beta-naphthylamine | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| acidic alpha-aminopeptidase | - |
Rattus norvegicus |
| aminopeptidase A | - |
Rattus norvegicus |
| angiotensinase A | - |
Rattus norvegicus |
| APA | - |
Rattus norvegicus |
| aspartate aminopeptidase | - |
Rattus norvegicus |
| Ca2+-activated glutamate aminopeptidase | - |
Rattus norvegicus |
| EAP | - |
Rattus norvegicus |
| glutamyl aminopeptidase | - |
Rattus norvegicus |
| membrane aminopeptidase II | - |
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 |
|---|---|---|---|
| 7.2 | - |
approximately | Rattus norvegicus |
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Release 2023.1 (January 2023)
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