3.4.11.21: aspartyl aminopeptidase
This is an abbreviated version!
For detailed information about aspartyl aminopeptidase, go to the full flat file.
Word Map on EC 3.4.11.21
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3.4.11.21
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3.4.11.7
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angiotensin
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aminopeptidases
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renin-angiotensin
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angiotensinase
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gluap
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amastatin
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alanyl
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glutamyl-aminopeptidase
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3.4.24.11
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maltase-glucoamylase
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cysap
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aspartyl-aminopeptidase
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pepes
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arylamide
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drug development
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lactase-phlorizin
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medicine
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synthesis
- 3.4.11.21
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3.4.11.7
- angiotensin
- aminopeptidases
-
renin-angiotensin
- angiotensinase
- gluap
- amastatin
-
alanyl
- glutamyl-aminopeptidase
-
3.4.24.11
- maltase-glucoamylase
- cysap
- aspartyl-aminopeptidase
- pepes
-
arylamide
- drug development
-
lactase-phlorizin
- medicine
- synthesis
Reaction
release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate =
Synonyms
AAP, acid aminopeptidase, acid peptidase, alpha-aspartyl dipeptidase, Aminopeptidase, aminopeptidase A, angiotensinase, APA, Ape4, Ape4 aspartyl aminopeptidase, Ape4 metalloprotease, Asp-AP, AspAP, aspartate aminopeptidase, aspartic aminopeptidase, aspartyl aminopeptidase, aspartyl(glutamyl)-specific aminopeptidase, aspartyl-AP, CNAG_01169, DAP, DNPEP, EC 3.4.11.7, glutamyl (aspartyl)-specific aminopeptidase A, glutamyl aminopeptidase, L-aspartate aminopeptidase, Lb-PepA, Lc-PepA, M18 aspartyl aminopeptidase, M18AAP, More, PepA, peptidase E, PfM18AAP, PvM18AAP, soluble acid aminopeptidase, TgAAP, TGGT1_297970, Yhr113w
ECTree
3.4.11.21 aspartyl aminopeptidaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 3.4.11.21 - aspartyl aminopeptidase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(2S)-3-oxo-3-(7-phenylpyrazolo[1,5-a]pyrimidin-3-yl)-2-(6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]
i.e. ZINC54727336
1-[2-(acridin-9-ylamino)ethyl]-2-methyl-3-phenylmethoxypyridin-4-one
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2-(1,3-benzothiazol-2-ylthio)-N-(5-phenyl-1,3,4-thiadiazol-2-yl)acetamide
i.e. ZINC01158737
2-(3-oxo-[1,2,4]triazolo[4,3-a]pyridin-2-yl)ethyl
i.e. ZINC47767447
2-benzothiazol-2-ylsulfanyl-N-[5-(mtolyl)-1,3,4-thiadiazol-2-yl]-acetamide
i.e. ZINC04174427
3-(5-(H)-[1,2,4]triazino[5,6-b]indol-3-yldisulfanyl)-5-(H)-[1,2,4]triazino[5,6-b]indole
i.e. ZINC06536284
4-[(7-chloroquinolin-4-yl)amino]-2-(diethylamino methyl)phenol
i.e. CHEMBL1506682, 32.65% inhibition
4-[2-(1,2,3,4-tetrahydroacridin-9-ylamino)ethyl]benzene-1,2-diol
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4-[2-(acridin-9-ylamino)ethyl]benzene-1,2-diol
IC50 value for parasite growth is 0.0013 mM
5-phenyl-N-([1,2,4]triazolo[4,3-a]pyridin-3-ylmethyl)-[1,2,4]triazolo[1,5-a]pyrimidin-7-amine
i.e. ZINC78349763
5-phenyl-N-[(1R)-1-([1,2,4]triazolo[4,3-a]pyridin-3-yl)ethyl]-[1,2,4]triazolo[1,5-a]pyrimidin-7-amine
i.e. ZINC72883556
5-phenyl-N-[(1S)-1-([1,2,4]triazolo[4,3-a]pyridin-3-yl)ethyl]-[1,2,4]triazolo[1,5-a]pyrimidin-7-amine
i.e. ZINC72883554
7-chloro-N-[2-(3,4-dimethoxyphenyl)ethyl]-N-methylquinolin-4-amine
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CID 23724194
a PfM18AAP inhibitor, leads to over 50% inhibition at 1 mM
L-Glu
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product inhibition of enzyme Lc-PepA, 8.4% inhibition at 0.1 mM, 17.7% at 10 mM, product inhibition versus substrate L-Asp-4-nitroanilide, and 1.47% inhibition at 0.1 mM, 31.4% at 10 mM, product inhibition versus substrate L-Glu-4-nitroanilide
N-[2-(2-bromo-4,5-dimethoxyphenyl)ethyl]-1,2,3,4-tetrahydroacridin-9-amine
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N-[[8-chloro-6-(trifluoromethyl)-[1,2,4]triazolo[4,3-a]pyridin-3-yl]methyl]-5-methyl-[1,2,4]triazolo
i.e. ZINC32853471
NaCl
about 30% of activity is retained in 20% (w/v) NaCl; about 30% of activity is retained in 20% (w/v) NaCl
1,10-phenanthroline
21% at 1.0 mM, complete inhibition at 10 mM
1-benzyl-N-[2-(3,4-dimethoxyphenyl)ethyl]piperidin-4-amine
i.e. CHEMBL585028, 37.29% inhibition
3-[2-(quinolin-4-ylamino)ethyl]benzene-1,2-diol
i.e. CHEMBL602830, 28.24% inhibition
4-[2-(quinolin-4-ylamino)ethyl]benzene-1,2-diol
i.e. CHEMBL511171, 53.68% inhibition
4-[2-[(7-chloroquinolin-4-yl)amino]ethyl]benzene-1,2-diol
i.e. CHEMBL585601, 55.21% inhibition
4-[3-(acridin-9-ylamino)propyl]benzene-1,2-diol
i.e. CHEMBL586200, 36.43% inhibition
7-chloro-N-[2-(3,4-dimethoxyphenyl)ethyl]quinolin-4-amine
i.e. CHEMBL525132, 75.26% inhibition
Ca2+
57% residual activity at 40 mM; 57% residual activity at 40 mM
dimethylformamide
78.1% inhibition at 4.2% v/v
EDTA
54% residual activity at 20 mM; 54% residual activity at 20 mM
L-Asp
39.5% inhibition at 10 mM, no inhibition at 0.1-1.0 mM, product inhibition versus substrate L-Asp-4-nitroanilide, and 33.8% inhibition at 10 mM and no inhibition at 0.1-1.0 mM, product inhibition versus substrate L-Glu-4-nitroanilide
L-Asp
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21.8% inhibition at 10 mM and no inhibition at 0.1-1.0 mM, product inhibition versus substrate L-Asp-4-nitroanilide, and 24.0% inhibition at 10 mM and no inhibition at 0.1-1.0 mM, product inhibition versus substrate L-Glu-4-nitroanilide
N-[2-(2-bromo-4,5-dimethoxyphenyl)ethyl]quinolin-4-amine
i.e. CHEMBL429, 37.43% inhibition
N-[2-(3,4-dimethoxyphenyl)ethyl]-6-ethoxyquinolin-4-amine
i.e. CHEMBL245416, 31.93% inhibition
N-[2-(3,4-dimethoxyphenyl)ethyl]isoquinolin-4-amine
i.e. CHEMBL66953, 55.6% inhibition
o-phenanthroline
43% residual activity at 5 mM; 43% residual activity at 5 mM
o-phenanthroline
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activity is reduced to 8.3% after incubating with 20 mM o-phenanthroline
SDS
73% at 1.0 mM, complete inhibition at 10 mM
Zn2+
27% residual activity at 0.4 mM; 27% residual activity at 0.4 mM
additional information
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no inhibition by Zn2+ in contrary to glutamyl aminopeptidase, EC 3.4.11.7, no inhibition by Glu-thiol, Asp-thiol, bestatin, amastatin, and puromycin
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additional information
enzyme Lb-PepA is not product-inhibited by L-Glu. Lb-PepA activity decreases significantly with metal salt concentrations above the optimum concentrations determined. Poor inhibition at 1.0 mM 2-mercaptoethanol, no inhibition by pepstatin A at 0.1-10 mM
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additional information
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enzyme Lb-PepA is not product-inhibited by L-Glu. Lb-PepA activity decreases significantly with metal salt concentrations above the optimum concentrations determined. Poor inhibition at 1.0 mM 2-mercaptoethanol, no inhibition by pepstatin A at 0.1-10 mM
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additional information
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no inhibition by Zn2+ in contrary to glutamyl aminopeptidase, EC 3.4.11.7, no inhibition by Glu-thiol, Asp-thiol, bestatin, amastatin, and puromycin
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additional information
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no inhibition by Zn2+ in contrary to glutamyl aminopeptidase, EC 3.4.11.7, no inhibition by Glu-thiol, Asp-thiol, bestatin, amastatin, and puromycin
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additional information
3-dimensional quantitative structure activity relationship (3D QSAR) modeling, pharmacophore modeling, and molecular docking are used to identify potent inhibitors from ChEMBL antimalarial library that bind to M18AAP of Plasmodium falciparum, molecular docking, overview
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additional information
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3-dimensional quantitative structure activity relationship (3D QSAR) modeling, pharmacophore modeling, and molecular docking are used to identify potent inhibitors from ChEMBL antimalarial library that bind to M18AAP of Plasmodium falciparum, molecular docking, overview
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additional information
inhibitor detection using 3-dimensional quantitative structure activity relationship (3D QSAR) modeling, virtual screening and molecular docking studies and interaction analysis, overview. Model evaluation and validation and molecular dynamics analysis
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additional information
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inhibitor detection using 3-dimensional quantitative structure activity relationship (3D QSAR) modeling, virtual screening and molecular docking studies and interaction analysis, overview. Model evaluation and validation and molecular dynamics analysis
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