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

Inhibitors

Inhibitors 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.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10 phenanthroline
1,10-phenanthroline
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
-
inactivation by modification of pK 5.8 carboxylate, presence arginine hydroxamate decreases inhibitory potency, hydroxylamine does not recover enzyme activity
1-Phenyl-2-thiourea
-
competitive
2,2'-dipyridyl
-
-
2,3-Dimercaptopropanol
-
-
actinonin
-
-
amastatin
arginine hydroxamate
-
competitive
arphamenine A
-
-
Arphamenine B
-
-
bestatin
captopril
-
-
chymostatin
-
39% residual activity at 0.1 mM
crystal delta-endotoxin from Bacillus thuringiensis
-
-
-
diethyldicarbonate
-
inactivation by modification of an imidazole, presence of arginine hydroxamate decreases inhibitory potency, hydroxylamine partially recovers enzyme activity after inactivation
dipicolinic acid
97% inhibition at 5 mM, Mg2+, Zn2+, and Co2+ partly protect
heavy metals
-
-
-
Hg2+
-
99% inhibition at 1 mM, recombinant enzyme
iodoacetate
-
-
leucinethiol
leuhistin
-
-
matlystatin A
-
-
Methionine hydroxamate
-
competitive
N-(hydroxyethyl)iminodiacetic acid
-
i.e. Himda
N-p-tosyl-L-lysine chloromethyl ketone
-
64% residual activity at 0.1 mM
N-p-tosyl-L-phenylalanine chloromethyl ketone
-
8% residual activity at 0.1 mM
N-tosyl-L-Phe chloromethyl ketone
-
slightly inhibitory
Nalpha-(2-[[(1-amino-3-phenylpropyl)(hydroxy)phosphoryl]methyl]pent-4-ynoyl)-D-phenylalaninamide
potent phosphinic pseudopeptide inhibitor
Ni2+
-
89% inhibition at 1 mM
nitriloacetic acid
-
-
nitrobestatin
-
95.1% inhibition at 0.133 mM
o-phenanthroline
p-chloromercuribenzoate
-
-
phebestin
-
i.e. [(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-valyl]-L-phenylalanine
Phenylglyoxal
-
-
Phenylmethylsulfonylfluoride
-
6% residual activity at 1 mM
probestin
-
-
puromycin
-
-
RB 101(S)
-
-
Tetranitromethane
-
changes the Km of the enzyme without affecting Vmax by modifying a phenol group, presence arginine hydroxamate decreases inhibitory potency
Tris
-
chelated to active site Zn2+
additional information
-