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

BRENDA support

3.4.11.22: aminopeptidase I

This is an abbreviated version!
For detailed information about aminopeptidase I, go to the full flat file.

Word Map on EC 3.4.11.22

Reaction

Release of an N-terminal amino acid, preferably a neutral or hydrophobic one, from a polypeptide. Aminoacyl-arylamides are poor substrates =

Synonyms

A-LAP, AAP, Actinase AS, adipocyte-derived leucine amino-peptidase, Aeromonas proteolytica aminopeptidase, alpha-Aminoacyl-peptide hydrolase, Aminooligopeptidase, Aminopeptidase, aminopeptidase (I), aminopeptidase 1, aminopeptidase ERAP1, aminopeptidase I, aminopeptidase II, Aminopeptidase III, aminopeptidase IV, aminopeptidase regulator of TNFR1 shedding, Aminopeptidase yscI, Aminopeptidase yscII, Aminopeptidase yscXVI, Aminopolypeptidase, Amylorhizin aminopeptidase, Amylorizin, AP, APE1, Ape2 aminopeptidase, API, ARTS-1, Bacillus aminopeptidase I, ColAP, cold-active aminopeptidase, endoplasmic resticulum aminopeptidase associated with antigen processing, endoplasmic reticulum aminopeptidase, endoplasmic reticulum aminopeptidase 1, endoplasmic reticulum aminopeptidase associated with antigen presentation, ER aminopeptidase, ER aminopeptidase 1, ER aminopeptidase associated with antigen processing, ERAAP, ERAP1, Jc-peptidase, L-aminopeptidase, LAP, LAP II, LAP IV, LAP4, LAPase, LAPIV, Leu.AP, Leucin aminopeptidase V, leucine aminopeptidase, leucine aminopeptidase II, Leucine aminopeptidase IV, leucine-aminopeptidase, Leucineaminopeptidase I, Leucyl aminopeptidase, Metallo aminopeptidase, More, non-specific monoaminopeptidase, pApe1p, PILS-AP, Pj-peptidase, Polypeptidase, puromycin-insensitive leucyl-specific aminopeptidase, thermophilic aminopeptidase, vacuolar aminopeptidase 1, vacuolar aminopeptidase I, Yeast aminopeptidase I, YKL103C, yscI

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.22 aminopeptidase I

Crystallization

Crystallization on EC 3.4.11.22 - aminopeptidase I

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular dynamics simulation of mutants K228R, Q730E, R528R/Q730E. The K528R polymorphism has strong effects on the conformational distribution of ERAP1
sitting drop vapor diffusion method
-
to 1.6 A resolution, structure of the closed-conformation of ERAP1 with inhibitor Nalpha-(2-[[(1-amino-3-phenylpropyl)(hydroxy)phosphoryl]methyl]pent-4-ynoyl)-D-phenylalaninamide bound in its active site. Inhibitor Nalpha-(2-[[(1-amino-3-phenylpropyl)(hydroxy)phosphoryl]methyl]pent-4-ynoyl)-D-phenylalaninamide is coordinated to the zinc ion via its phosphinic group with a geometry that imitates a transition state analogue
sitting drop vapour diffusion method with 0.1 M Tris-HCl pH 6.5, 30% polyethylene glycol 400, 0.1 M MgCl2 and 1.1 M NaCl
-
16 mg/ml enzyme complexed with inhibitory Tris, in 10 mM Tris, pH 8.0, 10 mM KSCN, 0.4 NaCl, vapour diffusion method, with precipitant solution containing 100 mM Tris, pH 8.0, 100 mM KSCN, 4.5 M NaCl, 48 h, X-ray diffraction structure determination and analysis at 1.2 A resolution
-