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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

Molecular Weight

Molecular Weight on EC 3.4.11.22 - aminopeptidase I

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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
105000
120000
-
gel permeation chromatography
140000
-
glycosylated active enzyme form, gel filtration
200000
-
SDS-PAGE
27000
-
gel filtration
30000
-
1 * 30000, SDS-PAGE
320000
-
hexameric form, sucrose density gradient centrifugation
36500
-
12 * 36500, heterododecamer with two types of subunits with similar MW, the enzyme shows different hybrid types, overview, the enzymatic activity of the alpha-subunit differs from that of the beta-subunit
37000
x * 37000, SDS-PAGE, x * 41061, amino acid sequence calculation
400000
41061
x * 37000, SDS-PAGE, x * 41061, amino acid sequence calculation
42000
-
1 * 42000, SDS-PAGE
43000
-
gel filtration
44000
-
x * 62000 + x * 44000, SDS-PAGE
44500
-
x * 44500, recombinant enzyme, SDS-PAGE
45000
-
x * 45000, SDS-PAGE
50000
-
12 * 50000, the active enzyme is a homododecameric complex of about 600 kDa, and dissociation into two hexamers leads to loss of enzymatic activity
51000
-
12 * 51000, SDS-PAGE
51950
-
x * 56000, deglycosylated recombinant enzyme, SDS-PAGE, x * 51950, mature enzyme, amino acid sequence calculation
52000
-
gel filtration, non-denaturing PAGE
53000
56000
-
x * 56000, deglycosylated recombinant enzyme, SDS-PAGE, x * 51950, mature enzyme, amino acid sequence calculation
60000
-
SDS-PAGE
610000
-
sucrose density gradient centrifugation
62000
-
x * 62000 + x * 44000, SDS-PAGE
640000
66000
-
x * 66000, SDS-PAGE
71000
-
gel filtration
72000
-
native PAGE
74000
-
native PAGE
84000
-
1 * 84000, SDS-PAGE
85000 - 90000
-
unglycosylated active enzyme form, gel filtration
93000
-
gel filtration
97634
-
1 * 97634, amino acid sequence calculation
98000
-
SDS-PAGE