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angiotensin + H2O
Asp + des-Asp-angiotensin
angiotensin I + H2O
Asp + Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
angiotensin I + H2O
Asp + des-Asp-angiotensin I
-
-
-
-
?
angiotensin I + H2O
L-Asp + des-Asp-angiotensin I
-
-
-
?
angiotensin II + H2O
Asp + angiotensin III
angiotensin II antipeptide + H2O
?
-
-
-
-
?
angiotensin II antipeptide + H2O
Glu + Gly-Val-Thr-Val-His-Pro-Val
-
i.e. Glu-Gly-Val-Thr-Val-His-Pro-Val
-
-
?
angiotensinogen 1-14 + H2O
?
-
-
-
-
?
angiotensinogen 1-14 + H2O
Asp + Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser, low activity
-
-
?
Arg 2-naphthylamide + H2O
Arg + 2-naphthylamine
-
-
-
?
Asp 2-naphthylamide + H2O
Asp + 2-naphthylamine
Asp-2-naphthylamide + H2O
Asp + 2-naphthylamine
Asp-7-amido-4-methylcoumarin + H2O
Asp + 7-amino-4-methylcoumarin
-
-
-
-
?
Asp-Ala + H2O
Asp + Ala
-
-
-
?
Asp-Ala-Pro-2-naphthylamide + H2O
Asp + Ala-Pro-2-naphthylamide
-
preferring acidic amino acids favouring aspartyl residues, requires a free alpha-amino group
-
?
Asp-Ala-Pro-chromogen + H2O
Asp + Ala-Pro-chromogen
Asp-Ala-Pro-sulfamethoxazole + H2O
Asp + Ala-Pro-sulfamethoxazole
Asp-Lys + H2O
Asp + Lys
-
-
-
?
Asp-Lys-Ala-Leu + H2O
Asp + Lys-Ala-Leu
Asp-p-nitroanilide + H2O
Asp + p-nitroaniline
64% activity
-
-
?
Asp-Xaa + H2O
Asp + Xaa
-
-
-
r
Asp-Xaa-Xaa + H2O
Asp + Xaa-Xaa
-
no activity on oligopeptides larger than tripeptides
-
r
Asp-Xaa-Xaa-Xaa + H2O
Asp + Xaa-Xaa-Xaa
-
neutral or hydrophobic amino acids in P1 position preferred
-
?
aspartyl peptides + H2O
Asp + des-Asp-angiotensin
Glu 2-naphthylamide + H2O
Glu + 2-naphthylamine
Glu-7-amido-4-methylcoumarin + H2O
Glu + 7-amino-4-methylcoumarin
-
-
-
-
?
Glu-Ala-Pro-naphthylamide + H2O
Glu + Ala-Pro-naphthylamide
-
-
-
-
?
Glu-p-nitroanilide + H2O
Glu + p-nitroaniline
100% activity
-
-
?
L-Asp-2-naphthylamide + H2O
L-Asp + 2-naphthylamine
-
-
-
-
?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
L-Asp-7-amido-4-methylcoumarin + H2O
L-Asp + 7-amino-4-methylcoumarin
L-aspartyl-beta-naphthylamide + H2O
L-aspartic acid + beta-naphthylamine
-
-
-
?
L-Glu-4-nitroanilide + H2O
L-Glu + 4-nitroaniline
L-Glu-7-amido-4-methylcoumarin + H2O
L-Glu + 7-amino-4-methylcoumarin
Lys 2-naphthylamide + H2O
Lys + 2-naphthylamine
-
-
-
?
N-(alpha-L-aspartyl)-4-nitroanilide + H2O
L-aspartic acid + 4-nitroaniline
N-(alpha-L-glutamyl)-2-naphthylamide + H2O
L-glutamic acid + 2-naphthylamine
N-(alpha-L-glutamyl)-4-nitroanilide + H2O
L-glutamic acid + 4-nitroaniline
additional information
?
-
angiotensin + H2O
Asp + des-Asp-angiotensin
-
intracellular protein and peptide metabolism
-
?
angiotensin + H2O
Asp + des-Asp-angiotensin
-
metabolism of angiotensin I, angiotensin II, cholecystokinin-8 and neuropeptide, solube and membrane-bound AspAP play different functional roles in the brain
-
?
angiotensin + H2O
Asp + des-Asp-angiotensin
-
intracellular protein and peptide metabolism
-
?
angiotensin + H2O
Asp + des-Asp-angiotensin
-
-
-
?
angiotensin + H2O
Asp + des-Asp-angiotensin
-
intracellular protein and peptide metabolism
-
?
angiotensin I + H2O
?
-
-
-
-
?
angiotensin I + H2O
?
-
-
-
-
?
angiotensin I + H2O
Asp + Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
-
-
?
angiotensin I + H2O
Asp + Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
-
-
?
angiotensin II + H2O
?
-
-
-
-
?
angiotensin II + H2O
?
-
-
-
-
?
angiotensin II + H2O
Asp + angiotensin III
-
-
-
?
angiotensin II + H2O
Asp + angiotensin III
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
Asp + angiotensin III
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
Asp + angiotensin III
-
octapeptides preferred to tetrapeptides
-
?
angiotensin II + H2O
Asp + angiotensin III
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
Asp + angiotensin III
-
aspartyl aminopeptidase and several other aminopeptidases, i.e. angiotensinases, are involved in angiotensin II and cholecystokinin, CCK, metabolism, angiotensin II is the principal effector of the renin-angiotensin-system, RAS, which induces vasoconstriction and increases sodium and water retention thereby leading to increased blood pressure
-
-
?
angiotensin II + H2O
Asp + angiotensin III
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
Asp + angiotensin III
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe, best substrate
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
Asp + angiotensin III
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe, best substrate
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
Asp 2-naphthylamide + H2O
Asp + 2-naphthylamine
-
higher affinity for Asp 2-naphthylamide than for Glu 2-naphthylamide
-
?
Asp 2-naphthylamide + H2O
Asp + 2-naphthylamine
-
-
-
?
Asp 2-naphthylamide + H2O
Asp + 2-naphthylamine
-
attacked more rapidly than 2-naphthylamide derivates of neutral or basic amino acids
-
?
Asp-2-naphthylamide + H2O
Asp + 2-naphthylamine
-
-
-
-
?
Asp-2-naphthylamide + H2O
Asp + 2-naphthylamine
-
-
-
-
?
Asp-2-naphthylamide + H2O
Asp + 2-naphthylamine
-
most susceptible substrate
-
-
?
Asp-Ala-Pro-chromogen + H2O
Asp + Ala-Pro-chromogen
-
-
-
-
?
Asp-Ala-Pro-chromogen + H2O
Asp + Ala-Pro-chromogen
-
-
-
-
?
Asp-Ala-Pro-chromogen + H2O
Asp + Ala-Pro-chromogen
-
-
-
-
?
Asp-Ala-Pro-sulfamethoxazole + H2O
Asp + Ala-Pro-sulfamethoxazole
-
-
-
-
?
Asp-Ala-Pro-sulfamethoxazole + H2O
Asp + Ala-Pro-sulfamethoxazole
-
-
-
?
Asp-Lys-Ala-Leu + H2O
Asp + Lys-Ala-Leu
-
lower activity
-
-
?
Asp-Lys-Ala-Leu + H2O
Asp + Lys-Ala-Leu
-
lower activity
-
-
?
Asp-Lys-Ala-Leu + H2O
Asp + Lys-Ala-Leu
-
lower activity
-
-
?
aspartyl peptides + H2O
Asp + des-Asp-angiotensin
-
catabolism of intracellular proteins, breakdown of abnormal cell proteins, supplement of nutritional sources
-
?
aspartyl peptides + H2O
Asp + des-Asp-angiotensin
-
activation and degradation of several neuropeptides, excitatory Asp and Glu implicated in pathogenesis of different neurogeneratives diseases
-
?
Glu 2-naphthylamide + H2O
Glu + 2-naphthylamine
-
-
-
?
Glu 2-naphthylamide + H2O
Glu + 2-naphthylamine
-
attacked more rapidly than 2-naphthylamide derivatives of neutral or basic amino acids
-
-
?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
-
-
-
?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
-
-
-
?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
-
-
-
?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
-
-
-
?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
-
-
-
?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
-
-
-
?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
-
-
-
-
?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
-
-
-
-
?
L-Asp-7-amido-4-methylcoumarin + H2O
L-Asp + 7-amino-4-methylcoumarin
-
-
-
?
L-Asp-7-amido-4-methylcoumarin + H2O
L-Asp + 7-amino-4-methylcoumarin
-
-
-
?
L-Asp-7-amido-4-methylcoumarin + H2O
L-Asp + 7-amino-4-methylcoumarin
-
-
-
?
L-Asp-7-amido-4-methylcoumarin + H2O
L-Asp + 7-amino-4-methylcoumarin
-
-
-
?
L-Glu-4-nitroanilide + H2O
L-Glu + 4-nitroaniline
-
-
-
?
L-Glu-4-nitroanilide + H2O
L-Glu + 4-nitroaniline
-
-
-
?
L-Glu-4-nitroanilide + H2O
L-Glu + 4-nitroaniline
-
-
-
?
L-Glu-4-nitroanilide + H2O
L-Glu + 4-nitroaniline
-
-
-
?
L-Glu-4-nitroanilide + H2O
L-Glu + 4-nitroaniline
-
-
-
?
L-Glu-4-nitroanilide + H2O
L-Glu + 4-nitroaniline
-
-
-
?
L-Glu-4-nitroanilide + H2O
L-Glu + 4-nitroaniline
-
-
-
-
?
L-Glu-4-nitroanilide + H2O
L-Glu + 4-nitroaniline
-
-
-
-
?
L-Glu-7-amido-4-methylcoumarin + H2O
L-Glu + 7-amino-4-methylcoumarin
-
-
-
?
L-Glu-7-amido-4-methylcoumarin + H2O
L-Glu + 7-amino-4-methylcoumarin
-
-
-
?
L-Glu-7-amido-4-methylcoumarin + H2O
L-Glu + 7-amino-4-methylcoumarin
-
-
-
?
L-Glu-7-amido-4-methylcoumarin + H2O
L-Glu + 7-amino-4-methylcoumarin
-
-
-
?
N-(alpha-L-aspartyl)-4-nitroanilide + H2O
L-aspartic acid + 4-nitroaniline
-
-
-
-
?
N-(alpha-L-aspartyl)-4-nitroanilide + H2O
L-aspartic acid + 4-nitroaniline
-
-
-
-
?
N-(alpha-L-aspartyl)-4-nitroanilide + H2O
L-aspartic acid + 4-nitroaniline
-
-
-
-
?
N-(alpha-L-glutamyl)-2-naphthylamide + H2O
L-glutamic acid + 2-naphthylamine
-
-
-
-
?
N-(alpha-L-glutamyl)-2-naphthylamide + H2O
L-glutamic acid + 2-naphthylamine
-
-
-
-
?
N-(alpha-L-glutamyl)-2-naphthylamide + H2O
L-glutamic acid + 2-naphthylamine
-
-
-
-
?
N-(alpha-L-glutamyl)-4-nitroanilide + H2O
L-glutamic acid + 4-nitroaniline
-
-
-
-
?
N-(alpha-L-glutamyl)-4-nitroanilide + H2O
L-glutamic acid + 4-nitroaniline
-
-
-
-
?
N-(alpha-L-glutamyl)-4-nitroanilide + H2O
L-glutamic acid + 4-nitroaniline
-
-
-
-
?
additional information
?
-
does not hydrolyze [Asn1, Val5]-angiotensin II, less than 0.5% activity on Ala-p-nitroanilide, Pro-p-nitroanilide, Met-p-nitroanilide, Arg-p-nitroanilide, and Leu-p-nitroanilide
-
-
?
additional information
?
-
does not hydrolyze [Asn1, Val5]-angiotensin II, less than 0.5% activity on Ala-p-nitroanilide, Pro-p-nitroanilide, Met-p-nitroanilide, Arg-p-nitroanilide, and Leu-p-nitroanilide
-
-
?
additional information
?
-
-
does not hydrolyze [Asn1, Val5]-angiotensin II, less than 0.5% activity on Ala-p-nitroanilide, Pro-p-nitroanilide, Met-p-nitroanilide, Arg-p-nitroanilide, and Leu-p-nitroanilide
-
-
?
additional information
?
-
enzyme AAP only hydrolyses Asp-4-nitroanilide and Glu-4-nitroanilide. The activity of AAP against Glu-4-nitroanilide corresponds to 43% of that against Asp-4-nitroanilide, indicating that this AAP is an aspartyl(glutamyl)-specific aminopeptidase
-
-
?
additional information
?
-
enzyme AAP only hydrolyses Asp-4-nitroanilide and Glu-4-nitroanilide. The activity of AAP against Glu-4-nitroanilide corresponds to 43% of that against Asp-4-nitroanilide, indicating that this AAP is an aspartyl(glutamyl)-specific aminopeptidase
-
-
?
additional information
?
-
-
enzyme AAP only hydrolyses Asp-4-nitroanilide and Glu-4-nitroanilide. The activity of AAP against Glu-4-nitroanilide corresponds to 43% of that against Asp-4-nitroanilide, indicating that this AAP is an aspartyl(glutamyl)-specific aminopeptidase
-
-
?
additional information
?
-
enzyme AAP only hydrolyses Asp-4-nitroanilide and Glu-4-nitroanilide. The activity of AAP against Glu-4-nitroanilide corresponds to 43% of that against Asp-4-nitroanilide, indicating that this AAP is an aspartyl(glutamyl)-specific aminopeptidase
-
-
?
additional information
?
-
enzyme AAP only hydrolyses Asp-4-nitroanilide and Glu-4-nitroanilide. The activity of AAP against Glu-4-nitroanilide corresponds to 43% of that against Asp-4-nitroanilide, indicating that this AAP is an aspartyl(glutamyl)-specific aminopeptidase
-
-
?
additional information
?
-
-
substrate specificity, overview, the substrate chain length is important for activity, the enzyme has little or no activity towards aminoacyl-arylamines, no or little activity towards aspartyl dipeptides with a positively charged residue in the second position
-
-
?
additional information
?
-
-
substrate specificity, overview, the substrate chain length is important for activity, the enzyme has little or no activity towards aminoacyl-arylamines, no or little activity towards aspartyl dipeptides with a positively charged residue in the second position
-
-
?
additional information
?
-
-
the enzyme catalyzes the hydrolysis of N-terminal alpha-L-glutamyl and alpha-L-aspartyl residues
-
-
?
additional information
?
-
-
substrate specificity, overview, the substrate chain length is important for activity, the enzyme has little or no activity towards aminoacyl-arylamines, no or little activity towards aspartyl dipeptides with a positively charged residue in the second position
-
-
?
additional information
?
-
-
no hydrolysis is observed against Leu-7-amido-4-methylcoumarin, Phe-7-amido-4-methylcoumarin, Ala-7-amido-4-methylcoumarin, Pro-7-amido-4-methylcoumarin, Gly-7-amido-4-methylcoumarin, Val-7-amido-4-methylcoumarin, Arg-7-amido-4-methylcoumarin, and Ile-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
M18AAP is an exopeptidase that digests the N-terminal aspartic and glutamic acid which cannot be degraded by any other aminopeptidase
-
-
?
additional information
?
-
-
M18AAP is an exopeptidase that digests the N-terminal aspartic and glutamic acid which cannot be degraded by any other aminopeptidase
-
-
?
additional information
?
-
-
the enzyme is specific for unblocked N-terminal acidic amino acid residues, no activity with N-acetyl-angiotensinogen 1-14, Tyr-bradykinin, Ile-Ser-bradykinin, and [Sar1, Ala8]-angiotensin II, overview
-
-
?
additional information
?
-
-
the enzyme is specific for unblocked N-terminal acidic amino acid residues, no activity with N-acetyl-angiotensinogen 1-14, Tyr-bradykinin, Ile-Ser-bradykinin, and [Sar1, Ala8]-angiotensin II, overview
-
-
?
additional information
?
-
rTgAAP has a strict preference for Asp-7-amido-4-methylcoumarin and Glu-7-amido-4-methylcoumarin, the catalytic efficiency of the enzyme is higher with L-Glu-7-amido-4-methylcoumarin than with L-Asp-7-amido-4-methylcoumarin. No activity with Ala-, Arg-, Cys-, Leu-, Lys, Met-, Phe, Trp-, and Tyr-7-amido-4-methylcoumarin, and poor activity with His-, Ser-, and Pro-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
rTgAAP has a strict preference for Asp-7-amido-4-methylcoumarin and Glu-7-amido-4-methylcoumarin, the catalytic efficiency of the enzyme is higher with L-Glu-7-amido-4-methylcoumarin than with L-Asp-7-amido-4-methylcoumarin. No activity with Ala-, Arg-, Cys-, Leu-, Lys, Met-, Phe, Trp-, and Tyr-7-amido-4-methylcoumarin, and poor activity with His-, Ser-, and Pro-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
rTgAAP has a strict preference for Asp-7-amido-4-methylcoumarin and Glu-7-amido-4-methylcoumarin, the catalytic efficiency of the enzyme is higher with L-Glu-7-amido-4-methylcoumarin than with L-Asp-7-amido-4-methylcoumarin. No activity with Ala-, Arg-, Cys-, Leu-, Lys, Met-, Phe, Trp-, and Tyr-7-amido-4-methylcoumarin, and poor activity with His-, Ser-, and Pro-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
rTgAAP has a strict preference for Asp-7-amido-4-methylcoumarin and Glu-7-amido-4-methylcoumarin, the catalytic efficiency of the enzyme is higher with L-Glu-7-amido-4-methylcoumarin than with L-Asp-7-amido-4-methylcoumarin. No activity with Ala-, Arg-, Cys-, Leu-, Lys, Met-, Phe, Trp-, and Tyr-7-amido-4-methylcoumarin, and poor activity with His-, Ser-, and Pro-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
rTgAAP has a strict preference for Asp-7-amido-4-methylcoumarin and Glu-7-amido-4-methylcoumarin, the catalytic efficiency of the enzyme is higher with L-Glu-7-amido-4-methylcoumarin than with L-Asp-7-amido-4-methylcoumarin. No activity with Ala-, Arg-, Cys-, Leu-, Lys, Met-, Phe, Trp-, and Tyr-7-amido-4-methylcoumarin, and poor activity with His-, Ser-, and Pro-7-amido-4-methylcoumarin
-
-
?
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(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
(S)-(+)-apomorphine
IC50 value for parasite growth is 0.004 mM
1,3-dibenzotriazol-1-yl-3-phenyl-propan-1-ol
i.e. ZINC05489290
1-amino-1,3-propanediphosphonic acid
-
-
1-benzyl-N-[2-(3,4-dimethoxyphenyl)ethyl]piperidin-4-amine
1-[2-(acridin-9-ylamino)ethyl]-2-methyl-3-phenylmethoxypyridin-4-one
-
1-[2-(acridin-9-ylamino)ethyl]-3-phenylmethoxypyridin-4-one
-
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
2-mercaptoethanol
-
58% inhibition at 0.01 mM, 96% at 0.1 mM
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
3-amino-3-(P-methylphosphinyl)propionic acid
-
-
3-amino-3-phosphonopropionic acid
-
-
3-amino-3-[P-(2-carboxypropyl)phosphinyl]propionic acid
-
-
3-[2-(quinolin-4-ylamino)ethyl]benzene-1,2-diol
4-(1-quinolin-4-ylpiperidin-3-yl)benzene-1,2-diol
-
4-(1-quinolin-4-ylpiperidin-4-yl)benzene-1,2-diol
-
4-(1-quinolin-4-ylpyrrolidin-3-yl)benzene-1,2-diol
-
4-amino-4-(P-phenylphosphinyl)butyric acid
-
20% inhibition at 1.83 mM
4-amino-4-phosphonobutyric acid
-
-
4-amino-4-[P-(2-carboxypropyl)phosphinyl]butyric acid
-
-
4-[(7-chloroquinolin-4-yl)amino]-2-(diethylamino methyl)phenol
i.e. CHEMBL1506682, 32.65% inhibition
4-[(7-chloroquinolin-4-yl)amino]-2-(diethylaminomethyl)phenol
-
4-[2-(1,2,3,4-tetrahydroacridin-9-ylamino)ethyl]benzene-1,2-diol
-
4-[2-(3,4-dihydro-1H-isoquinolin-2-yl)ethyl]benzene-1,2-diol
-
4-[2-(acridin-9-ylamino)ethyl]benzene-1,2-diol
IC50 value for parasite growth is 0.0013 mM
4-[2-(acridin-9-ylamino)ethyl]phenol
-
4-[2-(quinolin-4-ylamino)ethyl]benzene-1,2-diol
4-[2-[(1-benzylpiperidin-4-yl)amino]ethyl]benzene-1,2-diol
-
4-[2-[(7-chloroquinolin-4-yl)amino]ethyl]benzene-1,2-diol
4-[2-[(8-methylquinolin-4-yl)amino]ethyl]benzene-1,2-diol
-
4-[2-[methyl(quinolin-4-yl)amino]ethyl]benzene-1,2-diol
-
4-[3-(3,4-dimethoxyphenyl)pyrrolidin-1-yl]quinoline
-
4-[3-(acridin-9-ylamino)propyl]benzene-1,2-diol
5-amino-5-phosphonopentanoic acid
-
-
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
-
7-chloro-N-[2-(3,4-dimethoxyphenyl)ethyl]quinolin-4-amine
bestatin
23.9% inhibition at 0.5 mM
CID 23724194
a PfM18AAP inhibitor, leads to over 50% inhibition at 1 mM
EGTA
-
slightly inhibitory from 2 mM to 5 mM
Fe2+
inhibits 13% at 1 mM
L-Glu
-
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'-acridin-9-ylethane-1,2-diamine
-
N-[(3,4-dimethoxyphenyl)methyl]acridin-9-amine
-
N-[2-(2-bromo-4,5-dimethoxyphenyl)ethyl]-1,2,3,4-tetrahydroacridin-9-amine
-
N-[2-(2-bromo-4,5-dimethoxyphenyl)ethyl]acridin-9-amine
-
N-[2-(2-bromo-4,5-dimethoxyphenyl)ethyl]quinolin-4-amine
N-[2-(3,4-dimethoxyphenyl)ethyl]-6-ethoxyquinolin-4-amine
N-[2-(3,4-dimethoxyphenyl)ethyl]-N-methylacridin-9-amine
-
N-[2-(3,4-dimethoxyphenyl)ethyl]acridin-9-amine
-
N-[2-(3,4-dimethoxyphenyl)ethyl]isoquinolin-4-amine
N-[2-(3-methoxyphenyl)ethyl]acridin-9-amine
-
N-[2-(4-methoxyphenyl)ethyl]acridin-9-amine
-
N-[3-(3,4-dimethoxyphenyl)propyl]acridin-9-amine
-
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
p-chloromercuribenzoate
-
-
pepstatin
10% inhibition at 0.5 mM
pepstatin A
-
slight inhibition
pyridoxal 5'-phosphate
-
-
1,10-phenanthroline
-
complete inhibition
1,10-phenanthroline
21% at 1.0 mM, complete inhibition at 10 mM
1,10-phenanthroline
-
complete inhibition at 1-10 mM
1,10-phenanthroline
-
complete inhibition
1,10-phenanthroline
-
after preincubation total loss of activity
1,10-phenanthroline
-
complete inhibition
1,10-phenanthroline
-
33.5% inhibition at 5 mM
1-benzyl-N-[2-(3,4-dimethoxyphenyl)ethyl]piperidin-4-amine
i.e. CHEMBL585028, 37.29% inhibition
1-benzyl-N-[2-(3,4-dimethoxyphenyl)ethyl]piperidin-4-amine
-
3-[2-(quinolin-4-ylamino)ethyl]benzene-1,2-diol
i.e. CHEMBL602830, 28.24% inhibition
3-[2-(quinolin-4-ylamino)ethyl]benzene-1,2-diol
-
4-[2-(quinolin-4-ylamino)ethyl]benzene-1,2-diol
i.e. CHEMBL511171, 53.68% inhibition
4-[2-(quinolin-4-ylamino)ethyl]benzene-1,2-diol
-
4-[2-[(7-chloroquinolin-4-yl)amino]ethyl]benzene-1,2-diol
i.e. CHEMBL585601, 55.21% inhibition
4-[2-[(7-chloroquinolin-4-yl)amino]ethyl]benzene-1,2-diol
-
4-[3-(acridin-9-ylamino)propyl]benzene-1,2-diol
i.e. CHEMBL586200, 36.43% inhibition
4-[3-(acridin-9-ylamino)propyl]benzene-1,2-diol
-
7-chloro-N-[2-(3,4-dimethoxyphenyl)ethyl]quinolin-4-amine
i.e. CHEMBL525132, 75.26% inhibition
7-chloro-N-[2-(3,4-dimethoxyphenyl)ethyl]quinolin-4-amine
-
acetone
21.5% inhibition at 4.2% v/v
acetone
-
37.2% inhibition at 4.2% v/v
Ca2+
57% residual activity at 40 mM; 57% residual activity at 40 mM
Ca2+
inhibits 10% at 1 mM
Cu2+
-
strongly inhibitory
dimethylformamide
78.1% inhibition at 4.2% v/v
dimethylformamide
-
84.9% inhibition at 4.2% v/v
dithiothreitol
7% inhibition at 0.5 mM
dithiothreitol
-
88% inhibition at 1 mM
DMSO
15.1% inhibition at 4.2% v/v
DMSO
-
13.9% inhibition at 4.2% v/v
DTT
-
high inhibition at 1 mM
DTT
12% inhibition at 0.1 mM
DTT
-
69% inhibition at 0.001 mM, 94% at 0.1 mM
DTT
-
high inhibition at 1 mM
DTT
-
88% inhibition at 1 mM
EDTA
54% residual activity at 20 mM; 54% residual activity at 20 mM
EDTA
inhibits 54% at 5 mM
EDTA
complete inhibition at 1.0 mM
EDTA
-
complete inhibition at 1.0 mM
EDTA
-
activity is reduced to 14% after incubating with 10 mM EDTA
EDTA
-
76.1% inhibition at 20 mM
EDTA
-
strong inhibitory from 2 mM to 5 mM
ethanol
16.3% inhibition at 4.2% v/v
ethanol
-
25.7% inhibition at 4.2% v/v
Imidazol
34% inhibition at 40 mM
Imidazol
-
21% inhibition at 40 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
-
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-(2-bromo-4,5-dimethoxyphenyl)ethyl]quinolin-4-amine
-
N-[2-(3,4-dimethoxyphenyl)ethyl]-6-ethoxyquinolin-4-amine
i.e. CHEMBL245416, 31.93% inhibition
N-[2-(3,4-dimethoxyphenyl)ethyl]-6-ethoxyquinolin-4-amine
-
N-[2-(3,4-dimethoxyphenyl)ethyl]isoquinolin-4-amine
i.e. CHEMBL66953, 55.6% inhibition
N-[2-(3,4-dimethoxyphenyl)ethyl]isoquinolin-4-amine
-
o-phenanthroline
43% residual activity at 5 mM; 43% residual activity at 5 mM
o-phenanthroline
34.7% inhibition at 0.5 mM
o-phenanthroline
-
activity is reduced to 8.3% after incubating with 20 mM o-phenanthroline
PMSF
7% inhibition at 0.5 mM
PMSF
35% inhibition at 10 mM
PMSF
-
32% inhibition at 10 mM
SDS
73% at 1.0 mM, complete inhibition at 10 mM
SDS
-
63% at 1.0 mM, 97% inhibition at 10 mM
Zn2+
27% residual activity at 0.4 mM; 27% residual activity at 0.4 mM
Zn2+
inhibits 27% at 1 mM
Zn2+
-
50% inhibition at 0.4 M, after preincubation total inhibition
Zn2+
-
Zn2+ abolishes activity at 1 mM
Zn2+
-
strongly inhibitory
additional information
poor inhibition by bacitracin
-
additional information
-
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
-
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
-
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
-
additional information
-
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
-
additional information
-
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
-
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
-
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
-
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
-
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
-
additional information
-
not inhibited by amastatin, bestatin, or EDTA
-
additional information
-
poor inhibition by bestatin at 0.2 mM
-
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Anti-Glomerular Basement Membrane Disease
Chloride Channel ClC-5 Binds to Aspartyl Aminopeptidase to Regulate Renal Albumin Endocytosis.
Astrocytoma
Differential Effects of Doxazosin on Renin-Angiotensin-System-Regulating Aminopeptidase Activities in Neuroblastoma and Glioma Tumoral Cells.
Breast Neoplasms
A PAK5-DNPEP-USP4 axis dictates breast cancer growth and metastasis.
Breast Neoplasms
Aspartyl Aminopeptidase Suppresses Proliferation, Invasion, and Stemness of Breast Cancer Cells via Targeting CD44.
Breast Neoplasms
Neoadjuvant chemotherapy modifies serum angiotensinase activities in women with breast cancer.
Breast Neoplasms
Renin-Angiotensin system-regulating aminopeptidase activities are modified in the pineal gland of rats with breast cancer induced by N-methyl-nitrosourea.
Chagas Disease
[Description of an acidic peptidase, insensitive to classical inhibitors, in protein extracts of Trypanosoma cruzi, from a rural area of Venezuela, where Chagas disease is endemic].
Colorectal Neoplasms
Clinical impact of aspartyl aminopeptidase expression and activity in colorectal cancer.
Coma
Crystal structure of the peptidase domain of Streptococcus ComA, a bifunctional ATP-binding cassette transporter involved in the quorum-sensing pathway.
Hypertension
Angiotensinase A (aminopeptidase A): properties of chromatographically purified isoforms from human kidney.
Hyperthyroidism
Angiotensinase activity in hypothalamus and pituitary of hypothyroid, euthyroid and hyperthyroid adult male rats.
Hyperthyroidism
Atrial angiotensinase activity in hypothyroid, euthyroid, and hyperthyroid rats.
Hyperthyroidism
Influence of thyroid disorders on kidney angiotensinase activity.
Hyperthyroidism
Thyroid Disorders Change the Pattern of Response of Angiotensinase Activities in the Hypothalamus-Pituitary-Adrenal Axis of Male Rats.
Leukemia, Lymphocytic, Chronic, B-Cell
Aspartic Aminopeptidase Is a Novel Biomarker of Aggressive Chronic Lymphocytic Leukemia.
Malaria
Identification of Potent and Selective Inhibitors of the Plasmodium falciparum M18 Aspartyl Aminopeptidase (PfM18AAP) of Human Malaria via High-Throughput Screening.
Malaria
In silico prediction of anti-malarial hit molecules based on machine learning methods.
Malaria
The M18 aspartyl aminopeptidase of Plasmodium falciparum binds to human erythrocyte spectrin in vitro.
Malaria
The M18 aspartyl aminopeptidase of the human malaria parasite Plasmodium falciparum.
Malaria
X-ray Crystal Structure and Specificity of the Plasmodium falciparum Malaria Aminopeptidase PfM18AAP.
Malaria, Falciparum
X-ray Crystal Structure and Specificity of the Plasmodium falciparum Malaria Aminopeptidase PfM18AAP.
Neoplasm Metastasis
A PAK5-DNPEP-USP4 axis dictates breast cancer growth and metastasis.
Neoplasms
Altered glutamyl-aminopeptidase activity and expression in renal neoplasms.
Neoplasms
Aspartic Aminopeptidase Is a Novel Biomarker of Aggressive Chronic Lymphocytic Leukemia.
Neoplasms
Aspartyl Aminopeptidase Suppresses Proliferation, Invasion, and Stemness of Breast Cancer Cells via Targeting CD44.
Neoplasms
Changes in cell-surface peptidase activity in papillary renal cell carcinoma.
Neoplasms
Glutamyl- but not aspartyl-aminopeptidase activity is modified in serum of N-methyl nitrosourea-induced rat mammary tumours.
Neoplasms
Ischemia-induced angiogenesis is impaired in aminopeptidase A deficient mice via down-regulation of HIF-1?
Neoplasms
The pro-oxidant buthionine sulfoximine (BSO) reduces tumor growth of implanted Lewis lung carcinoma in mice associated with increased protein carbonyl, tubulin abundance, and aminopeptidase activity.
Neuroblastoma
Differential Effects of Doxazosin on Renin-Angiotensin-System-Regulating Aminopeptidase Activities in Neuroblastoma and Glioma Tumoral Cells.
Proteinuria
Chloride Channel ClC-5 Binds to Aspartyl Aminopeptidase to Regulate Renal Albumin Endocytosis.
Proteinuria
Urinary aminopeptidase activities as early and predictive biomarkers of renal dysfunction in cisplatin-treated rats.
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0.000145
1-benzyl-N-[2-(3,4-dimethoxyphenyl)ethyl]piperidin-4-amine
0.00025
1-[2-(acridin-9-ylamino)ethyl]-2-methyl-3-phenylmethoxypyridin-4-one
Plasmodium vivax
pH and temperature not specified in the publication
0.000213
1-[2-(acridin-9-ylamino)ethyl]-3-phenylmethoxypyridin-4-one
Plasmodium vivax
pH and temperature not specified in the publication
0.000363 - 0.000371
3-[2-(quinolin-4-ylamino)ethyl]benzene-1,2-diol
0.000238
4-(1-quinolin-4-ylpiperidin-3-yl)benzene-1,2-diol
Plasmodium vivax
pH and temperature not specified in the publication
0.000771
4-(1-quinolin-4-ylpiperidin-4-yl)benzene-1,2-diol
Plasmodium vivax
pH and temperature not specified in the publication
0.005248
4-[(7-chloroquinolin-4-yl)amino]-2-(diethylamino methyl)phenol
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.00526
4-[(7-chloroquinolin-4-yl)amino]-2-(diethylaminomethyl)phenol
Plasmodium vivax
pH and temperature not specified in the publication
0.000277
4-[2-(1,2,3,4-tetrahydroacridin-9-ylamino)ethyl]benzene-1,2-diol
Plasmodium vivax
pH and temperature not specified in the publication
0.000127
4-[2-(3,4-dihydro-1H-isoquinolin-2-yl)ethyl]benzene-1,2-diol
Plasmodium vivax
pH and temperature not specified in the publication
0.001429
4-[2-(acridin-9-ylamino)ethyl]phenol
Plasmodium vivax
pH and temperature not specified in the publication
0.000251 - 0.000256
4-[2-(quinolin-4-ylamino)ethyl]benzene-1,2-diol
0.000154
4-[2-[(1-benzylpiperidin-4-yl)amino]ethyl]benzene-1,2-diol
Plasmodium vivax
pH and temperature not specified in the publication
0.001585 - 0.001614
4-[2-[(7-chloroquinolin-4-yl)amino]ethyl]benzene-1,2-diol
0.000213
4-[2-[(8-methylquinolin-4-yl)amino]ethyl]benzene-1,2-diol
Plasmodium vivax
pH and temperature not specified in the publication
0.0002085
4-[2-[methyl(quinolin-4-yl)amino]ethyl]benzene-1,2-diol
Plasmodium vivax
pH and temperature not specified in the publication
0.0005
4-[3-(3,4-dimethoxyphenyl)pyrrolidin-1-yl]quinoline
Plasmodium vivax
pH and temperature not specified in the publication
0.000269 - 0.00027
4-[3-(acridin-9-ylamino)propyl]benzene-1,2-diol
0.001514
7-chloro-N-[2-(3,4-dimethoxyphenyl)ethyl]quinolin-4-amine
0.001611
CHEMBL1535
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.001603
CHEMBL2104009
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.000933
CHEMBL2414638
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.001549
CHEMBL303933
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.001837
CHEMBL339049
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.001578
CHEMBL35228
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.001611
CHEMBL36
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.000776
CHEMBL390368
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.001585
CHEMBL416956
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.000741
CHEMBL465847
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.001556
CHEMBL506
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.000724
CHEMBL528484
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.000708
CHEMBL529157
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.001175
CHEMBL532976
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.000676
CHEMBL587141
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.000525
CHEMBL588000
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.000692
CHEMBL591216
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.000708
CHEMBL601831
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.002427
CHEMBL682
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.001614
CHEMBL76
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.002
N'-acridin-9-ylethane-1,2-diamine
Plasmodium vivax
pH and temperature not specified in the publication
0.000593
N-[(3,4-dimethoxyphenyl)methyl]acridin-9-amine
Plasmodium vivax
pH and temperature not specified in the publication
0.003327
N-[2-(2-bromo-4,5-dimethoxyphenyl)ethyl]acridin-9-amine
Plasmodium vivax
pH and temperature not specified in the publication
0.002188 - 0.002223
N-[2-(2-bromo-4,5-dimethoxyphenyl)ethyl]quinolin-4-amine
0.000708 - 0.000715
N-[2-(3,4-dimethoxyphenyl)ethyl]-6-ethoxyquinolin-4-amine
0.000222
N-[2-(3,4-dimethoxyphenyl)ethyl]-N-methylacridin-9-amine
Plasmodium vivax
pH and temperature not specified in the publication
0.000407
N-[2-(3,4-dimethoxyphenyl)ethyl]acridin-9-amine
Plasmodium vivax
pH and temperature not specified in the publication
0.000219 - 0.000222
N-[2-(3,4-dimethoxyphenyl)ethyl]isoquinolin-4-amine
0.001663
N-[2-(3-methoxyphenyl)ethyl]acridin-9-amine
Plasmodium vivax
pH and temperature not specified in the publication
0.001
N-[2-(4-methoxyphenyl)ethyl]acridin-9-amine
Plasmodium vivax
pH and temperature not specified in the publication
0.000455
N-[3-(3,4-dimethoxyphenyl)propyl]acridin-9-amine
Plasmodium vivax
pH and temperature not specified in the publication
0.000145
1-benzyl-N-[2-(3,4-dimethoxyphenyl)ethyl]piperidin-4-amine
Plasmodium vivax
pH and temperature not specified in the publication
0.000145
1-benzyl-N-[2-(3,4-dimethoxyphenyl)ethyl]piperidin-4-amine
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.000363
3-[2-(quinolin-4-ylamino)ethyl]benzene-1,2-diol
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.000371
3-[2-(quinolin-4-ylamino)ethyl]benzene-1,2-diol
Plasmodium vivax
pH and temperature not specified in the publication
0.000251
4-[2-(quinolin-4-ylamino)ethyl]benzene-1,2-diol
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.000256
4-[2-(quinolin-4-ylamino)ethyl]benzene-1,2-diol
Plasmodium vivax
pH and temperature not specified in the publication
0.001585
4-[2-[(7-chloroquinolin-4-yl)amino]ethyl]benzene-1,2-diol
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.001614
4-[2-[(7-chloroquinolin-4-yl)amino]ethyl]benzene-1,2-diol
Plasmodium vivax
pH and temperature not specified in the publication
0.000269
4-[3-(acridin-9-ylamino)propyl]benzene-1,2-diol
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.00027
4-[3-(acridin-9-ylamino)propyl]benzene-1,2-diol
Plasmodium vivax
pH and temperature not specified in the publication
0.001514
7-chloro-N-[2-(3,4-dimethoxyphenyl)ethyl]quinolin-4-amine
Plasmodium vivax
pH and temperature not specified in the publication
0.001514
7-chloro-N-[2-(3,4-dimethoxyphenyl)ethyl]quinolin-4-amine
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.002188
N-[2-(2-bromo-4,5-dimethoxyphenyl)ethyl]quinolin-4-amine
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.002223
N-[2-(2-bromo-4,5-dimethoxyphenyl)ethyl]quinolin-4-amine
Plasmodium vivax
pH and temperature not specified in the publication
0.000708
N-[2-(3,4-dimethoxyphenyl)ethyl]-6-ethoxyquinolin-4-amine
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.000715
N-[2-(3,4-dimethoxyphenyl)ethyl]-6-ethoxyquinolin-4-amine
Plasmodium vivax
pH and temperature not specified in the publication
0.000219
N-[2-(3,4-dimethoxyphenyl)ethyl]isoquinolin-4-amine
Plasmodium falciparum
pH and temperature not specified in the publication, a modeled value
0.000222
N-[2-(3,4-dimethoxyphenyl)ethyl]isoquinolin-4-amine
Plasmodium vivax
pH and temperature not specified in the publication
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evolution
enzyme AAP belongs to the M18 family of peptidases
evolution
the enzyme belongs to the M18 family of proteases
evolution
the enzyme belongs to the M18 family of proteases
evolution
-
enzyme AAP belongs to the M18 family of peptidases
-
evolution
-
enzyme AAP belongs to the M18 family of peptidases
-
evolution
-
enzyme AAP belongs to the M18 family of peptidases
-
malfunction
a Cryptococcus neoformans ape4 knockout mutant does not grow at 37°C, and also has defects in the expression of important virulence factors such as phospholipase production and capsule formation. The ape4 mutants are sensitive to high temperature growth. ape4 Mutation affects multiple virulence factors in Cryptococcus neoformans
malfunction
TgAAP knockout inhibits the attachment/invasion, replication, and substrate-specific activity in Toxoplasma gondii. TgAAP knockout affects the growth of Toxoplasma gondii but does not completely abolish parasite replication and growth
malfunction
-
TgAAP knockout inhibits the attachment/invasion, replication, and substrate-specific activity in Toxoplasma gondii. TgAAP knockout affects the growth of Toxoplasma gondii but does not completely abolish parasite replication and growth
-
malfunction
-
TgAAP knockout inhibits the attachment/invasion, replication, and substrate-specific activity in Toxoplasma gondii. TgAAP knockout affects the growth of Toxoplasma gondii but does not completely abolish parasite replication and growth
-
malfunction
-
a Cryptococcus neoformans ape4 knockout mutant does not grow at 37°C, and also has defects in the expression of important virulence factors such as phospholipase production and capsule formation. The ape4 mutants are sensitive to high temperature growth. ape4 Mutation affects multiple virulence factors in Cryptococcus neoformans
-
malfunction
-
TgAAP knockout inhibits the attachment/invasion, replication, and substrate-specific activity in Toxoplasma gondii. TgAAP knockout affects the growth of Toxoplasma gondii but does not completely abolish parasite replication and growth
-
malfunction
-
a Cryptococcus neoformans ape4 knockout mutant does not grow at 37°C, and also has defects in the expression of important virulence factors such as phospholipase production and capsule formation. The ape4 mutants are sensitive to high temperature growth. ape4 Mutation affects multiple virulence factors in Cryptococcus neoformans
-
malfunction
-
a Cryptococcus neoformans ape4 knockout mutant does not grow at 37°C, and also has defects in the expression of important virulence factors such as phospholipase production and capsule formation. The ape4 mutants are sensitive to high temperature growth. ape4 Mutation affects multiple virulence factors in Cryptococcus neoformans
-
physiological function
aspartyl aminopeptidase is a moonlight protein that has aspartyl aminopeptidase and chaperone activities
physiological function
-
a small portion localizes in the vacuole, but its vacuolar transport is accelerated by nutrient starvation, and it stably resides in the vacuole lumen, it is proposed that cytosolic enzyme is redistributed to the vacuole when yeast cells need more active vacuolar degradation
physiological function
-
aspartyl aminopeptidase immunoprecipitates with beta-actin and tubulin, suggesting a role in cytoskeletal maintenance. Enzyme is not present in the urine of healthy rats, however, it is readily detected in the urine in rat models of mild and heavy proteinuria. Urinary levels correlate with the severity of proteinuria
physiological function
-
aspartyl aminopeptidase interacts with ClC-5, a chloride/proton exchanger that plays an obligate role in albumin uptake by the renal proximal tubule. ClC-5 forms an endocytic complex with the albumin receptor megalin/cubilin. Aspartyl aminopeptidase and ClC-5 associate in cells. The two proteins bind directly to each other. Overexpression of wild-type aspartyl aminopeptidase increases cell-surface levels of ClC-5 and albumin uptake. Overexpression results in significant decrease in the amount of G actin, suggesting a role for aspartyl aminopeptidase in stabilizing the cytoskeleton
physiological function
Cryptococcus neoformans Ape4 activity is required by facultative intracellular pathogen to survive within macrophages, as well as for virulence in an animal model of cryptococcal infection. The enzyme is involved in autophagy. Cryptococcus neoformans autophagy-related genes are modulated during nitrogen starvation and thermal stress, overview The APE4 gene is involved in multi-stress resistance, aspartyl aminopeptidase encoded by APE4 is important during response to osmotic/salt stress
physiological function
the enzyme functions at the terminal stage of hemoglobin degradation of host and completes the hydrolysis process. M18AAP is an exopeptidase that digests the N-terminal aspartic and glutamic acid which cannot be degraded by any other aminopeptidase
physiological function
the only aspartyl aminopeptidase in Plasmodium falciparum, PfM18AAP, is essential for the survival of the organism. PfM18AAP enzyme performs various functions in the parasite and the erythrocytic host such as hemoglobin digestion, erythrocyte invasion, parasite growth and parasite escape from the host cell
physiological function
-
Cryptococcus neoformans Ape4 activity is required by facultative intracellular pathogen to survive within macrophages, as well as for virulence in an animal model of cryptococcal infection. The enzyme is involved in autophagy. Cryptococcus neoformans autophagy-related genes are modulated during nitrogen starvation and thermal stress, overview The APE4 gene is involved in multi-stress resistance, aspartyl aminopeptidase encoded by APE4 is important during response to osmotic/salt stress
-
physiological function
-
Cryptococcus neoformans Ape4 activity is required by facultative intracellular pathogen to survive within macrophages, as well as for virulence in an animal model of cryptococcal infection. The enzyme is involved in autophagy. Cryptococcus neoformans autophagy-related genes are modulated during nitrogen starvation and thermal stress, overview The APE4 gene is involved in multi-stress resistance, aspartyl aminopeptidase encoded by APE4 is important during response to osmotic/salt stress
-
physiological function
-
Cryptococcus neoformans Ape4 activity is required by facultative intracellular pathogen to survive within macrophages, as well as for virulence in an animal model of cryptococcal infection. The enzyme is involved in autophagy. Cryptococcus neoformans autophagy-related genes are modulated during nitrogen starvation and thermal stress, overview The APE4 gene is involved in multi-stress resistance, aspartyl aminopeptidase encoded by APE4 is important during response to osmotic/salt stress
-
additional information
enzyme structure homology modelling, molecular dynamics simulation, secondary structure, acidic residues and hydrophobicity of interior residues demonstrate that aspartyl aminopeptidase has a greater stability than non-salttolerant protease in high salinity. Higher contents of ordered secondary structures, more salt bridges between hydrated surface acidic residues and specific basic residues, and stronger hydrophobicity of interior residues are the salt-tolerance mechanisms of aspartyl aminopeptidase
additional information
-
enzyme structure homology modelling, molecular dynamics simulation, secondary structure, acidic residues and hydrophobicity of interior residues demonstrate that aspartyl aminopeptidase has a greater stability than non-salttolerant protease in high salinity. Higher contents of ordered secondary structures, more salt bridges between hydrated surface acidic residues and specific basic residues, and stronger hydrophobicity of interior residues are the salt-tolerance mechanisms of aspartyl aminopeptidase
-
additional information
-
enzyme structure homology modelling, molecular dynamics simulation, secondary structure, acidic residues and hydrophobicity of interior residues demonstrate that aspartyl aminopeptidase has a greater stability than non-salttolerant protease in high salinity. Higher contents of ordered secondary structures, more salt bridges between hydrated surface acidic residues and specific basic residues, and stronger hydrophobicity of interior residues are the salt-tolerance mechanisms of aspartyl aminopeptidase
-
additional information
-
enzyme structure homology modelling, molecular dynamics simulation, secondary structure, acidic residues and hydrophobicity of interior residues demonstrate that aspartyl aminopeptidase has a greater stability than non-salttolerant protease in high salinity. Higher contents of ordered secondary structures, more salt bridges between hydrated surface acidic residues and specific basic residues, and stronger hydrophobicity of interior residues are the salt-tolerance mechanisms of aspartyl aminopeptidase
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dimer
-
electron microscopy analysis, 6.5 nm diameter for each monomer
octamer
-
8 * 55000, SDS-PAGE, 8 * 52428, amino acid sequence calculation
?
x * 57000, about, SDS-PAGE, x * 56763, sequence calculation
?
-
x * 57000, about, SDS-PAGE, x * 56763, sequence calculation
-
?
-
x * 57000, about, SDS-PAGE, x * 56763, sequence calculation
-
?
-
x * 57000, about, SDS-PAGE, x * 56763, sequence calculation
-
?
-
x * 55000, immunoblot analysis
dodecamer
-
12 * 56000, SDS-PAGE
dodecamer
-
dodecamer comprising 12 identical units
dodecamer
-
12 * 56000, SDS-PAGE
-
dodecamer
-
dodecamer comprising 12 identical units
-
homododecamer
12 * 41000, recombinant His6-tagged enzyme, SDS-PAGE, 12 * 41100, about, sequence calculation
homododecamer
-
12 * 41000, recombinant His6-tagged enzyme, SDS-PAGE, 12 * 41100, about, sequence calculation
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homododecamer
-
12 * 40000, recombinant His6-tagged enzyme, SDS-PAGE, 12 * 39400, about, sequence calculation
homododecamer
-
12 * 40000, recombinant His6-tagged enzyme, SDS-PAGE, 12 * 39400, about, sequence calculation
-
homooctamer
-
8 * 65000, SDS-PAGE
homooctamer
-
8 * 70000, high performance liquid chromatography
oligomer
x * 80000, recombinant GST-tagged enzyme, SDS-PAGE, x * 56000, about, untagged enzyme, sequence calculation
oligomer
-
x * 80000, recombinant GST-tagged enzyme, SDS-PAGE, x * 56000, about, untagged enzyme, sequence calculation
-
oligomer
-
x * 80000, recombinant GST-tagged enzyme, SDS-PAGE, x * 56000, about, untagged enzyme, sequence calculation
-
oligomer
-
x * 80000, recombinant GST-tagged enzyme, SDS-PAGE, x * 56000, about, untagged enzyme, sequence calculation
-
additional information
enzyme tertiary structure prediction and validation, primary sequence analysis
additional information
-
enzyme tertiary structure prediction and validation, primary sequence analysis
additional information
-
peptide mass fingerprinting by MALDI-TOF MS analysis
additional information
-
peptide mass fingerprinting by MALDI-TOF MS analysis
-
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