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Literature summary extracted from
- A new role for Zn(II) aminopeptidases: antigenic peptide generation and destruction (2009), Curr. Pharm. Des., 15, 3656-3670.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.22 | 1,10-phenanthroline | - |
Mus musculus |  |
| 3.4.11.22 | actinonin | - |
Mus musculus | |
| 3.4.11.22 | amastatin | potent inhibitor | Mus musculus | |
| 3.4.11.22 | arphamenine A | - |
Mus musculus | |
| 3.4.11.22 | Arphamenine B | - |
Mus musculus | |
| 3.4.11.22 | bestatin | very poor inhibitor | Mus musculus | |
| 3.4.11.22 | captopril | - |
Mus musculus | |
| 3.4.11.22 | leucinethiol | - |
Mus musculus | |
| 3.4.11.22 | leuhistin | - |
Mus musculus | |
| 3.4.11.22 | matlystatin A | - |
Mus musculus | |
| 3.4.11.22 | probestin | - |
Mus musculus | |
| 3.4.11.22 | puromycin | - |
Mus musculus | |
| 3.4.11.22 | RB 101(S) | - |
Mus musculus | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.11.22 | endoplasmic reticulum | - |
Mus musculus | 5783 | - |
| 3.4.11.22 | microsome | - |
Mus musculus | - |
- |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.11.22 | Mus musculus | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.11.22 | liver | - |
Mus musculus | - |
| 3.4.11.22 | lung | - |
Mus musculus | - |
| 3.4.11.22 | spleen | - |
Mus musculus | - |
| 3.4.11.22 | thymus | - |
Mus musculus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.11.22 | L-Leu-7-amido-4-methylcoumarin + H2O | efficient cleavage | Mus musculus | L-Leu + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.11.22 | L-Met-7-amido-4-methylcoumarin + H2O | slower cleavage compared to L-Leu-7-amido-4-methylcoumarin | Mus musculus | L-Met + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.11.22 | additional information | ERAP1 does not degrade other substrates of the X-7-amido-4-methylcoumarin form except L-Leu-7-amido-4-methylcoumarin and L-Met-7-amido-4-methylcoumarin | Mus musculus | ? | - |
? | |
| 3.4.11.22 | additional information | ERAP1 trims peptides with length of 10-14 residues very efficiently down to 8-9 residues long while further trimming is practically absent | Mus musculus | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.11.22 | A-LAP | - |
Mus musculus |
| 3.4.11.22 | adipocyte-derived leucine amino-peptidase | - |
Mus musculus |
| 3.4.11.22 | aminopeptidase regulator of TNFR1 shedding | - |
Mus musculus |
| 3.4.11.22 | ARTS-1 | - |
Mus musculus |
| 3.4.11.22 | endoplasmic resticulum aminopeptidase associated with antigen processing | - |
Mus musculus |
| 3.4.11.22 | ER aminopeptidase 1 | - |
Mus musculus |
| 3.4.11.22 | ERAAP | - |
Mus musculus |
| 3.4.11.22 | ERAP1 | - |
Mus musculus |
| 3.4.11.22 | PILS-AP | - |
Mus musculus |
| 3.4.11.22 | puromycin-insensitive leucyl-specific aminopeptidase | - |
Mus musculus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.11.22 | physiological function | intracellular ERAP1 induces angiogenesis through endothelial integrin activation, while the secreted form of the enzyme suppresses angiogenesis through angiotensin II inactivation. ERAP1 participates in the innate immune response by increasing the production of cytokine receptors. ERAP1 is associated with the MHC class I antigen processing and presentation pathway | Mus musculus |
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