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Literature summary for 3.4.11.22 extracted from

  • Evnouchidou, I.; Papakyriakou, A.; Stratikos, E.
    A new role for Zn(II) aminopeptidases: antigenic peptide generation and destruction (2009), Curr. Pharm. Des., 15, 3656-3670.
    View publication on PubMed
Search for more literature for 3.4.11.22

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline
-
 Mus musculus
actinonin
-
 Mus musculus
amastatin potent inhibitor Mus musculus
arphamenine A
-
 Mus musculus
Arphamenine B
-
 Mus musculus
bestatin very poor inhibitor Mus musculus
captopril
-
 Mus musculus
leucinethiol
-
 Mus musculus
leuhistin
-
 Mus musculus
matlystatin A
-
 Mus musculus
probestin
-
 Mus musculus
puromycin
-
 Mus musculus
RB 101(S)
-
 Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
 Mus musculus 5783
-
microsome
-
 Mus musculus
-
-

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Mus musculus
-
lung
-
 Mus musculus
-
spleen
-
 Mus musculus
-
thymus
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Leu-7-amido-4-methylcoumarin + H2O efficient cleavage Mus musculus L-Leu + 7-amino-4-methylcoumarin
-
 ?
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
-
 ?
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 ?
-
 ?
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

Synonyms Comment Organism
A-LAP
-
 Mus musculus
adipocyte-derived leucine amino-peptidase
-
 Mus musculus
aminopeptidase regulator of TNFR1 shedding
-
 Mus musculus
ARTS-1
-
 Mus musculus
endoplasmic resticulum aminopeptidase associated with antigen processing
-
 Mus musculus
ER aminopeptidase 1
-
 Mus musculus
ERAAP
-
 Mus musculus
ERAP1
-
 Mus musculus
PILS-AP
-
 Mus musculus
puromycin-insensitive leucyl-specific aminopeptidase
-
 Mus musculus

General Information

General Information Comment Organism
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