Cloned (Comment) | Organism |
---|---|
expression of His-tagged or FLAG-tagged wild-type enzyme, and of isolated His- or FLAG-tagged N-terminal, and HA-tagged C-terminal domain in CHO-K1 cells and AtT-20 cells, expression in trans of the separate C- and N-terminal domains rescues enzyme functions, overview | Mus musculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
glutamate phosphonic acid | - |
Mus musculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | integral, cell surface | Mus musculus | 16020 | - |
additional information | deletion of the C-terminal domain abolishes the maturation and enzymatic activity of the N-terminal domain, which remains in the endoplasmic reticulum bound to calnexin as unfolded protein | Mus musculus | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | activates | Mus musculus | |
Zn2+ | monozinc aminopeptidase, binds to the catalytic site | Mus musculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
angiotensin II + H2O | Mus musculus | the enzyme is responsible for the convertion of angiotensin II into angiotensin III in the brain | Asp + angiotensin III | - |
? | |
additional information | Mus musculus | The C-terminal domain of aminopeptidase A is an intramolecular chaperone required for the correct folding, cell surface expression, and activity of the enzyme | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | - |
Mus musculus |
additional information | enzyme maturation, folding, and trafficking, overview | Mus musculus |
proteolytic modification | the enzyme's ectodomain is cleaved in the kidney in to an N-terminal fragment, corresponding to the zinc metallopeptidase domain, and a C-terminal fragment | Mus musculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
brain | - |
Mus musculus | - |
kidney | the enzyme's ectodomain is cleaved in the kidney in to an N-terminal fragment, corresponding to the zinc metallopeptidase domain, and a C-terminal fragment | Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
angiotensin II + H2O | i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe | Mus musculus | Asp + angiotensin III | i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe | ? | |
angiotensin II + H2O | the enzyme is responsible for the convertion of angiotensin II into angiotensin III in the brain | Mus musculus | Asp + angiotensin III | - |
? | |
additional information | The C-terminal domain of aminopeptidase A is an intramolecular chaperone required for the correct folding, cell surface expression, and activity of the enzyme | Mus musculus | ? | - |
? | |
N-(alpha-L-glutamyl)-4-nitroanilide + H2O | - |
Mus musculus | L-glutamic acid + 4-nitroaniline | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the C-terminal domain is required for enzyme maturation, N-terminal domain activation, and cell surface localization, deletion of the C-terminal domain abolishes the maturation and enzymatic activity of the N-terminal domain, which remains in the endoplasmic reticulum bound to calnexin as unfolded protein | Mus musculus |
Synonyms | Comment | Organism |
---|---|---|
aminopeptidase A | - |
Mus musculus |
APA | - |
Mus musculus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Mus musculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Mus musculus |