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Literature summary for 3.4.11.7 extracted from
- Biochemical and enzymatic properties of the M1 family of aminopeptidases involved in the regulation of blood pressure (2007), Heart Fail. Rev., 13, 285-291.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | Ca2+ up- or down-regulates the enzyme activity depending on the substrate tested | Mus musculus |  |
| Ca2+ | Ca2+ up- or down-regulates the enzyme activity depending on the substrate tested | Homo sapiens | |
| Ca2+ | Ca2+ up- or down-regulates the enzyme activity depending on the substrate tested | Rattus norvegicus | |
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | aminopeptidases play an important role in the regulation of blood pressure, and in the regulation of other pathophysiological processes such as angiogenesis, antigen-presentation, and fertility most probably by mediating the metabolism of some peptide substrates | Mus musculus |
| medicine | aminopeptidases play an important role in the regulation of blood pressure, and in the regulation of other pathophysiological processes such as angiogenesis, antigen-presentation, and fertility most probably by mediating the metabolism of some peptide substrates | Homo sapiens |
| medicine | aminopeptidases play an important role in the regulation of blood pressure, and in the regulation of other pathophysiological processes such as angiogenesis, antigen-presentation, and fertility most probably by mediating the metabolism of some peptide substrates | Rattus norvegicus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| angiotensin IV | - |
Homo sapiens | |
| angiotensin IV | - |
Mus musculus | |
| angiotensin IV | - |
Rattus norvegicus | |
| Ca2+ | Ca2+ up- or down-regulates the enzyme activity depending on the substrate tested | Homo sapiens | |
| Ca2+ | Ca2+ up- or down-regulates the enzyme activity depending on the substrate tested | Mus musculus | |
| Ca2+ | Ca2+ up- or down-regulates the enzyme activity depending on the substrate tested | Rattus norvegicus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Mus musculus | 16020 | - |
| membrane | - |
Homo sapiens | 16020 | - |
| membrane | - |
Rattus norvegicus | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | - |
Mus musculus | |
| Zn2+ | - |
Homo sapiens | |
| Zn2+ | - |
Rattus norvegicus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 45000 | - |
only the C-terminal domain of the extracellular domain, obtained by proteolytic fragmentation | Mus musculus |
| 45000 | - |
only the C-terminal domain of the extracellular domain, obtained by proteolytic fragmentation | Homo sapiens |
| 45000 | - |
only the C-terminal domain of the extracellular domain, obtained by proteolytic fragmentation | Rattus norvegicus |
| 107000 | - |
only the catalytic part of the extracellular domain of the membrane-spanning protein | Mus musculus |
| 107000 | - |
only the catalytic part of the extracellular domain of the membrane-spanning protein | Homo sapiens |
| 107000 | - |
only the catalytic part of the extracellular domain of the membrane-spanning protein | Rattus norvegicus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
| Mus musculus | - |
- |
- |
| Rattus norvegicus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Glu-7-amido-4-methylcoumarin + H2O | - |
Mus musculus | Glu + 7-amino-4-methylcoumarin | - |
? | |
| Glu-7-amido-4-methylcoumarin + H2O | - |
Rattus norvegicus | Glu + 7-amino-4-methylcoumarin | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | full-length enzyme forms a dimer via a disulfide bond, this bond is not essential for dimer formation or enzymatic activity | Mus musculus |
| dimer | full-length enzyme forms a dimer via a disulfide bond, this bond is not essential for dimer formation or enzymatic activity | Homo sapiens |
| dimer | full-length enzyme forms a dimer via a disulfide bond, this bond is not essential for dimer formation or enzymatic activity | Rattus norvegicus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| aminopeptidase A | - |
Mus musculus |
| aminopeptidase A | - |
Homo sapiens |
| aminopeptidase A | - |
Rattus norvegicus |
| glutamyl aminopeptidase | - |
Mus musculus |
| glutamyl aminopeptidase | - |
Homo sapiens |
| glutamyl aminopeptidase | - |
Rattus norvegicus |
| hAPA | - |
Homo sapiens |
| mAPA | - |
Mus musculus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
measured with Glu-4-methlcoumaryl-7-amide, Glu-MCA, as a substrate | Mus musculus |
| 7 | - |
measured with Glu-4-methlcoumaryl-7-amide, Glu-MCA, as a substrate | Homo sapiens |
| 7 | - |
measured with Glu-4-methlcoumaryl-7-amide, Glu-MCA, as a substrate | Rattus norvegicus |
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Release 2023.1 (January 2023)
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