Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Chang, S.C.; Momburg, F.; Bhutani, N.; Goldberg, A.L.
    The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a molecular ruler mechanism (2005), Proc. Natl. Acad. Sci. USA, 102, 17107-17112.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.11.22 additional information
-
 additional information kinetics of peptide trimming, overview Sus scrofa
3.4.11.22 0.09
-
 AYWANATRSGA pH 7.5, 37°C Sus scrofa
3.4.11.22 0.111
-
 QLESIINFEKY pH 7.5, 37°C Sus scrofa
3.4.11.22 0.124
-
 QLESIINFEKL pH 7.5, 37°C Sus scrofa
3.4.11.22 0.124
-
 QLESIINFEKA pH 7.5, 37°C Sus scrofa
3.4.11.22 0.138
-
 QLESIINFEKL-amide pH 7.5, 37°C Sus scrofa
3.4.11.22 0.148
-
 EFAPGNYPAL pH 7.5, 37°C Sus scrofa
3.4.11.22 0.253
-
 AYWANATRSG-D-Ala pH 7.5, 37°C Sus scrofa
3.4.11.22 0.7
-
 QLESIINFEKD pH 7.5, 37°C Sus scrofa
3.4.11.22 0.8
-
 QLESIINFEKK pH 7.5, 37°C Sus scrofa
3.4.11.22 0.91
-
 QLESIINFEKR pH 7.5, 37°C Sus scrofa
3.4.11.22 1.325
-
 EFAPGNYPAD pH 7.5, 37°C Sus scrofa
3.4.11.22 1.5
-
 EFAPGNYPAK pH 7.5, 37°C Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.11.22 endoplasmic reticulum isozymes ERAP1 and ERAP2 Sus scrofa 5783
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.11.22 additional information Sus scrofa the endoplasmic reticulum enzyme ERAP1 trims precursors to lengths of MHC class I peptides by a 'molecular ruler' mechanism, overview, the enzyme is important in antigen presentation, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.22 Sus scrofa
-
 isozyme ERAP1 and ERAP2
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.11.22 further purification of commercial kidney enzyme preparation by affinity and hydrophobic interaction chromatography Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.11.22 commercial preparation from kidney, isozyme ERAP1 Sus scrofa
-
3.4.11.22 kidney isozyme ERAP1 Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.11.22 additional information
-
-
 Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.22 AAEAAG-NH2 + H2O
-
 Sus scrofa L-Ala + AEAAG-NH2
-
 ?
3.4.11.22 AAVVAAG-NH2 + H2O
-
 Sus scrofa L-Ala + AVVAAG-NH2
-
 ?
3.4.11.22 AEAA-NH2 + H2O
-
 Sus scrofa L-Ala + EAA-NH2
-
 ?
3.4.11.22 AYWANATRSG-D-Ala + H2O
-
 Sus scrofa L-Ala + AYWANATRSG-D-Ala
-
 ?
3.4.11.22 AYWANATRSGA + H2O high activity compared to other peptide substrates Sus scrofa L-Ala + YWANATRSGA
-
 ?
3.4.11.22 EAA-NH2 + H2O
-
 Sus scrofa L-Glu + AA-NH2
-
 ?
3.4.11.22 EFAPGNYPAD + H2O low activity compared to other peptide substrates Sus scrofa L-Glu + FAPGNYPAD
-
 ?
3.4.11.22 EFAPGNYPAK + H2O low activity compared to other peptide substrates Sus scrofa L-Glu + FAPGNYPAK
-
 ?
3.4.11.22 EFAPGNYPAL + H2O high activity compared to other peptide substrates Sus scrofa L-Glu + FAPGNYPAL
-
 ?
3.4.11.22 additional information the endoplasmic reticulum enzyme ERAP1 trims precursors to lengths of MHC class I peptides by a 'molecular ruler' mechanism, overview, the enzyme is important in antigen presentation, overview Sus scrofa ?
-
 ?
3.4.11.22 additional information L-amino acid peptide substrate specificity and strongly preferred chain length of 9-16 residues of isozyme ERAP1, overview, no activity with N-acetylQLESIINFEKL Sus scrofa ?
-
 ?
3.4.11.22 QLESIINFEK + H2O low activity compared to other peptide substrates Sus scrofa L-Gln + LESIINFEK
-
 ?
3.4.11.22 QLESIINFEKA + H2O high activity compared to other peptide substrates Sus scrofa L-Gln + LESIINFEKA
-
 ?
3.4.11.22 QLESIINFEKD + H2O low activity compared to other peptide substrates Sus scrofa L-Gln + LESIINFEKD
-
 ?
3.4.11.22 QLESIINFEKK + H2O low activity compared to other peptide substrates Sus scrofa L-Gln + LESIINFEKK
-
 ?
3.4.11.22 QLESIINFEKL + H2O best peptide substrate Sus scrofa L-Gln + LESIINFEKL
-
 ?
3.4.11.22 QLESIINFEKL-amide + H2O high activity compared to other peptide substrates Sus scrofa L-Gln + LESIINFEKL-amide
-
 ?
3.4.11.22 QLESIINFEKR + H2O low activity compared to other peptide substrates Sus scrofa L-Gln + LESIINFEKR
-
 ?
3.4.11.22 QLESIINFEKY + H2O high activity compared to other peptide substrates Sus scrofa L-Gln + LESIINFEKY
-
 ?
3.4.11.22 QLESIINFELK + H2O
-
 Sus scrofa L-Gln + LESIINFELK
-
 ?
3.4.11.22 SIINFEKL + H2O
-
 Sus scrofa L-Ser + IINFEKL
-
 ?
3.4.11.22 TTQRTRALV-NH2 + H2O
-
 Sus scrofa L-Thr + TQRTRALV-NH2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.11.22 aminopeptidase I
-
 Sus scrofa
3.4.11.22 ER aminopeptidase
-
 Sus scrofa
3.4.11.22 ERAP1
-
 Sus scrofa
3.4.11.22 leucine aminopeptidase
-
 Sus scrofa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.11.22 37
-
 assay at Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.11.22 7.5
-
 assay at Sus scrofa