HOME
login
history
all enzymes
BRENDA home
History
Information on EC 3.4.11.21 - aspartyl aminopeptidase
for references in articles please use BRENDA:EC3.4.11.21Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.11.21 aspartyl aminopeptidaseSpecify your search results
Word Map
- 3.4.11.21
-
3.4.11.7
- angiotensin
- aminopeptidases
-
renin-angiotensin
- angiotensinase
- gluap
- amastatin
-
alanyl
- maltase-glucoamylase
-
arylamide
-
3.4.24.11
- aspartyl-aminopeptidase
- pepes
- cysap
- glutamyl-aminopeptidase
-
lactase-phlorizin
- drug development
- synthesis
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAP
Aminopeptidase
angiotensinase
Ape4
Ape4 aspartyl aminopeptidase
Ape4 metalloprotease
Asp-AP
AspAP
aspartyl aminopeptidase
aspartyl(glutamyl)-specific aminopeptidase
aspartyl-AP
DAP
EC 3.4.11.7
glutamyl (aspartyl)-specific aminopeptidase A
M18 aspartyl aminopeptidase
M18AAP
PepA
peptidase E
TgAAP
TGGT1_297970
Yhr113w
additional information
AspAP
-
considered initially an alternative name for glutamyl aminopeptidase
glutamyl (aspartyl)-specific aminopeptidase A
-
additional information
see also EC 3.4.11.7
additional information
-
the enzyme belongs to the peptidase family M18
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate
release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate
-
-
-
-
release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate
the conserved residues His94, His170, and His440 are essential for activity
-
release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate
the conserved residues His94, His170, and His440 are essential for activity
-
release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate
the conserved residues His94, His170, and His440 are essential for activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9074-83-3
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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
-
-
?
Asp-7-amido-4-methylcoumarin + H2O
Asp + 7-amino-4-methylcoumarin
-
-
-
-
?
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-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
-
?
Glu-7-amido-4-methylcoumarin + H2O
Glu + 7-amino-4-methylcoumarin
-
-
-
-
?
Glu-p-nitroanilide + H2O
Glu + p-nitroaniline
100% activity
-
-
?
L-aspartyl-beta-naphthylamide + H2O
L-aspartic acid + beta-naphthylamine
-
-
-
?
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
-
intracellular protein and peptide metabolism
-
?
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
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
-
attacked more rapidly than 2-naphthylamide derivates of neutral or basic amino acids
-
?
Asp-2-naphthylamide + H2O
Asp + 2-naphthylamine
-
most susceptible substrate
-
-
?
Asp-Ala-Pro-sulfamethoxazole + H2O
Asp + Ala-Pro-sulfamethoxazole
-
-
-
?
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
-
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
Lactococcus lactis ssp. lactis DSM 20481
-
-
-
-
?
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
Lactococcus lactis ssp. lactis DSM 20481
-
-
-
-
?
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
?
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
Asp-Xaa + H2O
Asp + Xaa
-
-
-
r
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
-
intracellular protein and peptide metabolism
-
?
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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mn2+
NaCl
a salt-tolerant aspartyl aminopeptidase, the relative activity of the enzyme remains 85% in 3 M NaCl solution for 15 days, Km and Vmax are slightly affected in 3 M NaCl solution. 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
Zn2+
additional information
Zn2+
the catalytic active site harbors two zinc ions bounded by His/Asp, Asp, Glu, Asp/Glu and His
additional information
no or poor effect by Mg2+, Mn2+, and Cu2+ at 1 mM
additional information
-
no or poor effect by Mg2+, Mn2+, and Cu2+ at 1 mM
additional information
Lb-PepA activity decreases significantly with metal salt concentrations above the optimum concentrations determined
additional information
-
Lb-PepA activity decreases significantly with metal salt concentrations above the optimum concentrations determined
additional information
-
Lc-PepA activity decreases only slightly or is almost constant with metal salt concentrations above the optimum concentrations determined
additional information
-
activity is not enhanced by Ca2+, Fe2+, Mg2+, Mn2+, and Ni2+
additional information
AAP is a metalloaminopeptidase, M18 metalloaminopeptidases use metal ions to increase their substrate specificity for N-terminal acidic amino acids, beyond aspartic and glutamic acids
additional information
-
AAP is a metalloaminopeptidase, M18 metalloaminopeptidases use metal ions to increase their substrate specificity for N-terminal acidic amino acids, beyond aspartic and glutamic acids
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
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
-
CID 23724194
a PfM18AAP inhibitor, leads to over 50% inhibition 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-[2-(2-bromo-4,5-dimethoxyphenyl)ethyl]-1,2,3,4-tetrahydroacridin-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
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
-
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
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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
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
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.
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
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.94
Asp-Xaa
-
overexpressed enzyme
-
1.21
L-Asp-4-nitroanilide
pH 6.0, 60°C, recombinant enzyme
25.2
L-Glu-4-nitroanilide
pH 6.0, 60°C, recombinant enzyme
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.354
Asp-7-amido-4-methylcoumarin
-
at pH 7.5, in the presence of 1 mM Co2+
0.011
Glu-7-amido-4-methylcoumarin
-
at pH 7.5, in the absesence of Co2+
0.33
Glu-7-amido-4-methylcoumarin
-
at pH 7.5, in the presence of 1 mM Co2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
85.66
L-Asp-7-amido-4-methylcoumarin
pH 7.5, 37°C, recombinant enzyme, with Co2+
190.16
L-Glu-7-amido-4-methylcoumarin
pH 7.5, 37°C, recombinant enzyme, with Co2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00339
(S)-(+)-apomorphine
pH 7.5, temperature not specified in the publication
0.183
3-amino-3-[P-(2-carboxypropyl)phosphinyl]propionic acid
-
at pH 7.5
0.0427
4-amino-4-[P-(2-carboxypropyl)phosphinyl]butyric acid
-
at pH 7.5
0.00135
4-[2-(acridin-9-ylamino)ethyl]benzene-1,2-diol
pH 7.5, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.000238
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
0.000154
4-[2-[(1-benzylpiperidin-4-yl)amino]ethyl]benzene-1,2-diol
Plasmodium vivax
pH and temperature not specified in the publication
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
0.001611
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
0.000222
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
0.001663
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00013
additional information
additional information
-
enzyme activities in soluble fractions of heat, kidney, lung, and adrenal gland from PEG-treated rats, acute salt-loaded rats, water-overloaded rats, salt-loaded rats, and water-deprived rats, overview
additional information
-
angiotensin I: 100%, angiotensin II: 144%, angiotensinogen 1-14: 35%, angiotensin II antipeptide: 116%, N-acetyl-angiotensinogen 1-14: 0%, Tyr-bradykinin: 0%, Ile-Ser-bradykinin: 0%, [sar1,ala8] angiotensin II: 0%
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
recombinant enzyme, activity range, profile overview
6 - 9
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
50
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 80
-
recombinant enzyme, activity range, profile overview
20 - 75
recombinant enzyme, activity range, profile overview
30 - 70
20% of maximal activity at 30°C, inactivation above 70°C, maximal activity at 50°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Filobasidiella neoformans var. grubii, serotype A
UniProt
brenda
Cryptococcus neoformans var. grubii ATCC 208821
i.e. Filobasidiella neoformans var. grubii, serotype A
UniProt
brenda
Cryptococcus neoformans var. grubii CBS 10515
i.e. Filobasidiella neoformans var. grubii, serotype A
UniProt
brenda
Cryptococcus neoformans var. grubii FGSC 9487
i.e. Filobasidiella neoformans var. grubii, serotype A
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
29 and 33 months old rats show a 50% decrease of enzymatic activity
brenda
additional information
-
bilateral distribution of aminopeptidases in stress-related areas, overview
brenda
additional information
the APE4 expression pattern is influenced by nitrogen starvation and high temperature, APE4 expression is induced by the combination of nutrient and thermal stress
brenda
additional information
Cryptococcus neoformans var. grubii ATCC 208821
-
the APE4 expression pattern is influenced by nitrogen starvation and high temperature, APE4 expression is induced by the combination of nutrient and thermal stress
brenda
additional information
Cryptococcus neoformans var. grubii CBS 10515
-
the APE4 expression pattern is influenced by nitrogen starvation and high temperature, APE4 expression is induced by the combination of nutrient and thermal stress
brenda
additional information
Cryptococcus neoformans var. grubii FGSC 9487
-
the APE4 expression pattern is influenced by nitrogen starvation and high temperature, APE4 expression is induced by the combination of nutrient and thermal stress
brenda
additional information
the Lb-PepA activity decreases during the stationary growth phase, which is caused by degradation of the enzyme
brenda
additional information
-
the Lb-PepA activity decreases during the stationary growth phase, which is caused by degradation of the enzyme
brenda
additional information
-
the Lb-PepA activity decreases during the stationary growth phase, which is caused by degradation of the enzyme
brenda
additional information
-
enzyme in visceral organs during alterations in body fluid volume and osmolality, overview
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme is located within parasite cytosol and exported to parasitophorous vacuole
brenda
the enzyme is located within parasite cytosol and exported to parasitophorous vacuole
brenda
Ape4 is localized within the vesicles formed in response to nitrogen starvation and high temperatures. The GFP-Ape4 fusion protein co-localized with intracytoplasmic vesicles during nitrogen depletion
brenda
Cryptococcus neoformans var. grubii ATCC 208821
-
Ape4 is localized within the vesicles formed in response to nitrogen starvation and high temperatures. The GFP-Ape4 fusion protein co-localized with intracytoplasmic vesicles during nitrogen depletion
brenda
Cryptococcus neoformans var. grubii CBS 10515
-
Ape4 is localized within the vesicles formed in response to nitrogen starvation and high temperatures. The GFP-Ape4 fusion protein co-localized with intracytoplasmic vesicles during nitrogen depletion
brenda
Cryptococcus neoformans var. grubii FGSC 9487
-
Ape4 is localized within the vesicles formed in response to nitrogen starvation and high temperatures. The GFP-Ape4 fusion protein co-localized with intracytoplasmic vesicles during nitrogen depletion
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
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
Cryptococcus neoformans var. grubii FGSC 9487
-
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
Cryptococcus neoformans var. grubii ATCC 208821
-
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
Cryptococcus neoformans var. grubii CBS 10515
-
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 var. grubii FGSC 9487
-
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 var. grubii ATCC 208821
-
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 var. grubii CBS 10515
-
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
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
Show AA Sequence and Transmembrane Helices (899 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
440000
508000
recombinant His6-tagged enzyme, gel filtration
55000
680000
680000
-
native enzyme, dodecamer, determined using a Superose 6 column
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dodecamer
homododecamer
homooctamer
oligomer
additional information
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
homododecamer
-
12 * 40000, recombinant His6-tagged enzyme, SDS-PAGE, 12 * 39400, about, sequence calculation
homododecamer
Lactococcus lactis ssp. lactis DSM 20481
-
12 * 40000, recombinant His6-tagged enzyme, SDS-PAGE, 12 * 39400, about, 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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with zinc and substrate analogue aspartate-beta-hydroxamate, to 2.2 A resolution. Structure reveals a dodecameric machinery built by domain-swapped dimers, in agreement with electron microscopy data. For both Asp-Ala and Glu-Ala substrates, the Asp and Glu side chains fit into the P1 substrate pocket without steric constraints, while the main chain is modeled onto the hydroxamate group of aspartate-beta-hydroxamate in a position optimal for hydrolysis. The P1 substrate pocket is created by strand beta15 and the beta16-alpha12 and beta17-alpha13 loops, with the beta17-lpha13 loop lining the wall and restricting the dimensions of the pocket. This limited space disfavours bulky hydrophobic residues
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H352F
-
dramatically reduced activity, destabilization of quarternary structure and dissociation of the native 440000 Da enzyme
additional information
additional information
random insertional mutagenesis, the ape4 mutants are sensitive to high temperature growth. ape4 Mutation affects multiple virulence factors in Cryptococcus neoformans
additional information
Cryptococcus neoformans var. grubii ATCC 208821
-
random insertional mutagenesis, the ape4 mutants are sensitive to high temperature growth. ape4 Mutation affects multiple virulence factors in Cryptococcus neoformans
additional information
Cryptococcus neoformans var. grubii CBS 10515
-
random insertional mutagenesis, the ape4 mutants are sensitive to high temperature growth. ape4 Mutation affects multiple virulence factors in Cryptococcus neoformans
additional information
Cryptococcus neoformans var. grubii FGSC 9487
-
random insertional mutagenesis, the ape4 mutants are sensitive to high temperature growth. ape4 Mutation affects multiple virulence factors in Cryptococcus neoformans
additional information
knockout of enzyme TgAAP using the CRISPR/Cas9 knockout system, knockout plasmid pCD-TgAAP is constructed by inserting DHFR coding sequence and TgAAP-specific single guide RNA (gRNA) into plasmid pSAG1::CAS9-U6::sgUPRT, which contains Cas9, nuclear localization signal (NLS), and expresses GFP fusion element. The substrate activity is almost completely lost in the DELTATgAAP strain, thus, no other enzyme complements the TgAAP activity
additional information
-
knockout of enzyme TgAAP using the CRISPR/Cas9 knockout system, knockout plasmid pCD-TgAAP is constructed by inserting DHFR coding sequence and TgAAP-specific single guide RNA (gRNA) into plasmid pSAG1::CAS9-U6::sgUPRT, which contains Cas9, nuclear localization signal (NLS), and expresses GFP fusion element. The substrate activity is almost completely lost in the DELTATgAAP strain, thus, no other enzyme complements the TgAAP activity
additional information
-
knockout of enzyme TgAAP using the CRISPR/Cas9 knockout system, knockout plasmid pCD-TgAAP is constructed by inserting DHFR coding sequence and TgAAP-specific single guide RNA (gRNA) into plasmid pSAG1::CAS9-U6::sgUPRT, which contains Cas9, nuclear localization signal (NLS), and expresses GFP fusion element. The substrate activity is almost completely lost in the DELTATgAAP strain, thus, no other enzyme complements the TgAAP activity
additional information
-
knockout of enzyme TgAAP using the CRISPR/Cas9 knockout system, knockout plasmid pCD-TgAAP is constructed by inserting DHFR coding sequence and TgAAP-specific single guide RNA (gRNA) into plasmid pSAG1::CAS9-U6::sgUPRT, which contains Cas9, nuclear localization signal (NLS), and expresses GFP fusion element. The substrate activity is almost completely lost in the DELTATgAAP strain, thus, no other enzyme complements the TgAAP activity
additional information
-
knockout of enzyme TgAAP using the CRISPR/Cas9 knockout system, knockout plasmid pCD-TgAAP is constructed by inserting DHFR coding sequence and TgAAP-specific single guide RNA (gRNA) into plasmid pSAG1::CAS9-U6::sgUPRT, which contains Cas9, nuclear localization signal (NLS), and expresses GFP fusion element. The substrate activity is almost completely lost in the DELTATgAAP strain, thus, no other enzyme complements the TgAAP activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
purified recombinant His-tagged enzyme, over 60% activity remaining after 70 h
45
-
purified recombinant His-tagged enzyme, half-life at 5°C is about 20 h, inactivation within 70 h
50
55
-
purified recombinant His-tagged enzyme, half-life at 65°C is about 4-5 h, inactivation within 65 h
60
60 - 70
AAP is not precipitated by heat treatment for 30 min at 60°C, only less than 10% of AAP protein is precipitated by heating at 70°C
65
-
purified recombinant His-tagged enzyme, half-life at 65°C is about 2 h, inactivation within 10 h
0
purified recombinant His-tagged enzyme, over 80% activity remaining after 70 h
0
-
purified recombinant His-tagged enzyme, completely stable for over 70 h
50
the enzyme remains stabel upt to 50°C and retains about 70% activity after 20 h at 50°C, is inactivated rapidly at temperature in excess of this
50
the enzyme remains stable upt to 50°C and retains about 70% activity after 20 h at 50°C, is inactivated rapidly at temperature in excess of this
50
purified recombinant His-tagged enzyme, over 15% activity remaining after 70 h
50
-
remarkably stable below 50°C, soon inactivated at 60°C
60
purified recombinant His-tagged enzyme, inactivation within 10 h
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2000fold to homogeneity, Triton X-100 solubilized microsomal fraction, DEAE-cellulose chromatography, immunoadsorbent chromatography
-
aspartyl aminopeptidase is purified from yeast cells, using ultracentrifugation, ammonium sulfate fractionating, and chromatography on a Bio-Gel column, on a Mono Q column, and a Superose 6 column
-
DEAE-Sephacel gel filtration and TSK phenyl 5-PW gel filtration
native enzyme 454.5fold from koji by ammonium sulfate fractionation, dialysis, and ultrafiltration, followed by affinity and anion exchange chromatography, another step of ammonium sulfate fractionation, and gel filtration
native enzyme to homogeneity by ultracentrifugation, ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
-
non-fusion protein expressed in Escherichia coli, 440fold to homogeneity
-
partial, ammonium sulfate fractionation, gel filtration, ion-exchange chromatography
-
proteinase solubilized microsomal fraction, DEAE-cellulose chromatography, immunoadsorbent chromatography to homogeneity
-
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant GST-tagged enzyme from Escherichia coli by glutathione affinity chromatography and dialysis
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography to homogeneity
-
soluble enzyme from brain to homogeneity by affinity chromatography, gel filtration, hydrophobic interaction and hydroxyapatite chromatography
-
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression in Escherichia coli as His6-tagged enzyme
-
expressed in Escherichia coli BL21(DE3), GFP- and hemagglutinin-tagged constructs
-
expression in Escherichia coli
gene ape4, located on chromosome 5, sequence comparisons, recombinant expression of GFP-tagged enzyme in Cryptococcus neoformans
gene pepA, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene TGGT1_297970, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of GST-tagged enzyme in Escherichia coli
gene YHR113W, located on chromosome VIII, DNA and amino acid sequence determination and analysis
-
gene pepA, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene pepA, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APE4 expression is induced by the combination of nutrient and thermal stress
the APE4 expression pattern is influenced by nitrogen starvation and high temperature
APE4 expression is induced by the combination of nutrient and thermal stress
APE4 expression is induced by the combination of nutrient and thermal stress
Cryptococcus neoformans var. grubii FGSC 9487
-
APE4 expression is induced by the combination of nutrient and thermal stress
Cryptococcus neoformans var. grubii ATCC 208821
-
APE4 expression is induced by the combination of nutrient and thermal stress
Cryptococcus neoformans var. grubii CBS 10515
-
the APE4 expression pattern is influenced by nitrogen starvation and high temperature
the APE4 expression pattern is influenced by nitrogen starvation and high temperature
Cryptococcus neoformans var. grubii FGSC 9487
-
the APE4 expression pattern is influenced by nitrogen starvation and high temperature
Cryptococcus neoformans var. grubii ATCC 208821
-
the APE4 expression pattern is influenced by nitrogen starvation and high temperature
Cryptococcus neoformans var. grubii CBS 10515
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
solubilization of inclusion bodies by treatment with 0.6% Triton X-100, pH 10.0, 30 mM NaCl at 40°C for 20 min
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
medicine
-
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
synthesis
-
dipeptide sweeteners aspartame and alitame
drug development
enzyme TgAAP deletion results in inhibition, but not abolition, of invasion and growth of Toxoplasma gondii in cell culture, thus indicating that the enzyme may be a promising adjunct target for anti-toxoplasma drug development
drug development
the M18 aspartyl aminopeptidase is a valid target to develop antimalarial drugs
drug development
the M18 aspartyl aminopeptidase is a valid target to develop antimalarial drugs against the drug resistant strains of malaria parasite
drug development
-
enzyme TgAAP deletion results in inhibition, but not abolition, of invasion and growth of Toxoplasma gondii in cell culture, thus indicating that the enzyme may be a promising adjunct target for anti-toxoplasma drug development
drug development
-
enzyme TgAAP deletion results in inhibition, but not abolition, of invasion and growth of Toxoplasma gondii in cell culture, thus indicating that the enzyme may be a promising adjunct target for anti-toxoplasma drug development
drug development
-
enzyme TgAAP deletion results in inhibition, but not abolition, of invasion and growth of Toxoplasma gondii in cell culture, thus indicating that the enzyme may be a promising adjunct target for anti-toxoplasma drug development
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Danielsen, E.M.; Noren, O.; Sjoestroem, H.; Ingram, J.; Kenny, A.J.
Proteins of the kidney microvillar membrane. Aspartate aminopeptidase: purification by immunoadsorbent chromatography and properties of the detergent- and proteinase-solubilized forms
Biochem. J.
189
591-603
1980
Sus scrofa
brenda
Ramirez-Exposito, M.J.; Martinez, J.M.; Prieto, I.; Alba, F.; Ramirez, M.
Comparative distribution of glutamyl and aspartyl aminopeptidase activities in mouse organs
Horm. Metab. Res.
32
161-163
2000
Mus musculus
brenda
Wilk, S.; Wilk, E.; Magnusson, R.P.
Purification, characterization and cloning of a cytosolic aspartyl aminopeptidase
J. Biol. Chem.
273
15961-15970
1998
Oryctolagus cuniculus, Homo sapiens, Rattus sp.
brenda
Iribar, C.; Esteban, M.J.; Martinez, J.M.; Peinado, J.M.
Decrease in cytosolic aspartyl-aminopeptidase but not in alanyl-aminopeptidase activity in the frontal cortex of the aged rat
Brain Res.
687
211-213
1995
Rattus sp.
brenda
Nathan, P.B.; Ahmad, S.I.; Griffin, M.
Identification and characterization of an aspartate-specific peptidase (peptidase E) in Escherichia coli K12
Biochem. Soc. Trans.
17
354
1989
Escherichia coli
-
brenda
Zhang, H.; Zhang, J.; Wang, X.; Yang, W.; Lu, J.
Biochemical characterization of alpha-aspartyl dipeptidase. Cloning and expression of its gene
Ann. N. Y. Acad. Sci.
864
621-625
1998
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Wilk, S.; Wilk, E.; Magnusson, R.P.
Identification of histidine residues important in the catalysis and structure of aspartyl aminopeptidase
Arch. Biochem. Biophys.
407
176-183
2002
Homo sapiens
brenda
Banegas, I.; Prieto, I.; Alba, F.; Vives, F.; Araque, A.; Segarra, A.B.; Duran, R.; de Gasparo, M.; Ramirez, M.
Angiotensinase activity is asymmetrically distributed in the amygdala, hippocampus and prefrontal cortex of the rat
Behav. Brain Res.
156
321-326
2005
Rattus norvegicus
brenda
Yokoyama, R.; Kawasaki, H.; Hirano, H.
Identification of yeast aspartyl aminopeptidase gene by purifying and characterizing its product from yeast cells
FEBS J.
273
192-198
2006
Saccharomyces cerevisiae, Saccharomyces cerevisiae B-8032
brenda
Adang, M.J.
Aminopeptidase A
Handbook of Proteolytic Enzymes (2nd Edition)
1
299-303
2004
Mus musculus
-
brenda
Simmons, W.H.
Aspartyl aminopeptidase
Handbook of Proteolytic Enzymes (2nd Edition)
1
937-939
2004
Oryctolagus cuniculus, Homo sapiens, Mus musculus
-
brenda
Gasparello-Clemente, E.; Casis, L.; Varona, A.; Gil, J.; Irazusta, J.; Silveira, P.F.
Aminopeptidases in visceral organs during alterations in body fluid volume and osmolality
Peptides
24
1367-1372
2003
Rattus norvegicus
brenda
Varona, A.; Blanco, L.; Lopez, J.I.; Gil, J.; Agirregoitia, E.; Irazusta, J.; Larrinaga, G.
Altered levels of acid, basic, and neutral peptidase activity and expression in human clear cell renal cell carcinoma
Am. J. Physiol. Renal Physiol.
292
F780-F788
2007
Homo sapiens
brenda
Watanabe, J.; Tanaka, H.; Akagawa, T.; Mogi, Y.; Yamazaki, T.
Characterization of Aspergillus oryzae aspartyl aminopeptidase expressed in Escherichia coli
Biosci. Biotechnol. Biochem.
71
2557-2560
2007
Aspergillus oryzae (Q2U9Z9), Aspergillus oryzae (Q2UPZ7), Aspergillus oryzae
brenda
Banegas, I.; Barrero, F.; Duran, R.; Morales, B.; Luna, J.D.; Prieto, I.; Ramirez, M.; Alba, F.; Vives, F.
Plasma aminopeptidase activities in Parkinsons disease
Horm. Metab. Res.
38
758-760
2006
Homo sapiens
brenda
Teuscher, F.; Lowther, J.; Skinner-Adams, T.S.; Spielmann, T.; Dixon, M.W.; Stack, C.M.; Donnelly, S.; Mucha, A.; Kafarski, P.; Vassiliou, S.; Gardiner, D.L.; Dalton, J.P.; Trenholme, K.R.
The M18 aspartyl aminopeptidase of the human malaria parasite Plasmodium falciparum
J. Biol. Chem.
282
30817-30826
2007
Plasmodium falciparum
brenda
Segarra, A.B.; Wangensteen, R.; Ramirez, M.; Banegas, I.; Hermoso, F.; Vargas, F.; Vives, F.; Duran, R.; Alba, F.; de Gasparo, M.; Prieto, I.
Atrial angiotensinase activity in hypothyroid, euthyroid, and hyperthyroid rats
J. Cardiovasc. Pharmacol.
48
117-120
2006
Rattus norvegicus
brenda
Banegas, I.; Prieto, I.; Vives, F.; Alba, F.; de Gasparo, M.; Segarra, A.B.; Hermoso, F.; Duran, R.; Ramirez, M.
Brain aminopeptidases and hypertension
J. Renin Angiotensin Aldosterone Syst.
7
129-134
2006
Rattus norvegicus
brenda
Lee, S.; Kim, J.S.; Yun, C.H.; Chae, H.Z.; Kim, K.
Aspartyl aminopeptidase of Schizosaccharomyces pombe has a molecular chaperone function
BMB Rep.
42
812-816
2009
Schizosaccharomyces pombe (O36014), Schizosaccharomyces pombe
brenda
Trenholme, K.R.; Brown, C.L.; Skinner-Adams, T.S.; Stack, C.; Lowther, J.; To, J.; Robinson, M.W.; Donnelly, S.M.; Dalton, J.P.; Gardiner, D.L.
Aminopeptidases of malaria parasites: new targets for chemotherapy
Infect. Disord. Drug Targets
10
217-225
2010
Plasmodium falciparum
brenda
Cai, W.W.; Wang, L.; Chen, Y.
Aspartyl aminopeptidase, encoded by an evolutionarily conserved syntenic gene, is colocalized with its cluster in secretory granules of pancreatic islet cells
Biosci. Biotechnol. Biochem.
74
2050-2055
2010
Mus musculus (Q9Z2W0)
brenda
Yuga, M.; Gomi, K.; Klionsky, D.J.; Shintani, T.
Aspartyl aminopeptidase is imported from the cytoplasm to the vacuole by selective autophagy in Saccharomyces cerevisiae
J. Biol. Chem.
286
13704-13713
2011
Saccharomyces cerevisiae
brenda
Lee, A.; Slattery, C.; Nikolic-Paterson, D.J.; Hryciw, D.H.; Wilk, S.; Wilk, E.; Zhang, Y.; Valova, V.A.; Robinson, P.J.; Kelly, D.J.; Poronnik, P.
Chloride channel ClC-5 binds to aspartyl aminopeptidase to regulate renal albumin endocytosis
Am. J. Physiol. Renal Physiol.
308
F784-F792
2015
Rattus norvegicus, Didelphis sp.
brenda
Chaikuad, A.; Pilka, E.; De Riso, A.; Von Delft, F.; Kavanagh, K.; Venien-Bryan, C.; Oppermann, U.; Yue, W.
Structure of human aspartyl aminopeptidase complexed with substrate analogue: Insight into catalytic mechanism, substrate specificity and M18 peptidase family
BMC Struct. Biol.
12
14
2012
Homo sapiens (Q9ULA0), Homo sapiens
brenda
Spicer, T.; Fernandez-Vega, V.; Chase, P.; Scampavia, L.; To, J.; Dalton, J.P.; Da Silva, F.L.; Skinner-Adams, T.S.; Gardiner, D.L.; Trenholme, K.R.; Brown, C.L.; Ghosh, P.; Porubsky, P.; Wang, J.L.; Whipple, D.A.; Schoenen, F.J.; Hodder, P.
Identification of potent and selective inhibitors of the Plasmodium falciparum M18 aspartyl aminopeptidase (PfM18AAP) of human malaria via high-throughput screening
J. Biomol. Screen.
19
1107-1115
2014
Plasmodium falciparum (Q8I2J3), Plasmodium falciparum
brenda
Rout, S.; Mahapatra, R.K.
In silico study of M18 aspartyl amino peptidase (M18AAP) of Plasmodium vivax as an antimalarial drug target
Bioorg. Med. Chem.
27
2553-2571
2019
Plasmodium vivax (A0A1G4HB34), Plasmodium vivax
brenda
Kumari, M.; Chandra, S.; Tiwari, N.; Subbarao, N.
3D QSAR, pharmacophore and molecular docking studies of known inhibitors and designing of novel inhibitors for M18 aspartyl aminopeptidase of Plasmodium falciparum
BMC Struct. Biol.
16
12
2016
Plasmodium falciparum (Q8I2J3), Plasmodium falciparum
brenda
Gao, X.; Yin, Y.; Zhou, C.
Purification, characterisation and salt-tolerance molecular mechanisms of aspartyl aminopeptidase from Aspergillus oryzae 3.042
Food Chem.
240
377-385
2018
Aspergillus oryzae (Q2UPZ7), Aspergillus oryzae, Aspergillus oryzae 3.042 (Q2UPZ7), Aspergillus oryzae 3.042, Aspergillus oryzae ATCC 42149 (Q2UPZ7), Aspergillus oryzae RIB 40 (Q2UPZ7)
brenda
Stressler, T.; Ewert, J.; Merz, M.; Funk, J.; Claassen, W.; Lutz-Wahl, S.; Schmidt, H.; Kuhn, A.; Fischer, L.
A novel glutamyl (aspartyl)-specific aminopeptidase A from Lactobacillus delbrueckii with promising properties for application
PLoS ONE
11
e0152139
2016
Lactococcus lactis ssp. lactis, Lactobacillus delbrueckii subsp. lactis (F0HXE4), Lactobacillus delbrueckii subsp. lactis, Lactobacillus delbrueckii subsp. lactis DSM 20072 (F0HXE4), Lactococcus lactis ssp. lactis DSM 20481
brenda
Gontijo, F.A.; de Melo, A.T.; Pascon, R.C.; Fernandes, L.; Paes, H.C.; Alspaugh, J.A.; Vallim, M.A.
The role of aspartyl aminopeptidase (Ape4) in Cryptococcus neoformans virulence and authophagy
PLoS ONE
12
e0177461
2017
Cryptococcus neoformans var. grubii (J9VNI6), Cryptococcus neoformans var. grubii FGSC 9487 (J9VNI6), Cryptococcus neoformans var. grubii ATCC 208821 (J9VNI6), Cryptococcus neoformans var. grubii CBS 10515 (J9VNI6)
brenda
Zheng, J.; Cheng, Z.; Jia, H.; Zheng, Y.
Characterization of aspartyl aminopeptidase from Toxoplasma gondii
Sci. Rep.
6
34448
2016
Toxoplasma gondii (S7UJV5), Toxoplasma gondii, Toxoplasma gondii GT1 (S7UJV5), Toxoplasma gondii RH (S7UJV5), Toxoplasma gondii ATCC 50853 (S7UJV5)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.4.11.21)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
