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Information on EC 3.4.11.21 - aspartyl aminopeptidase
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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
- glutamyl-aminopeptidase
-
3.4.24.11
- maltase-glucoamylase
- cysap
- aspartyl-aminopeptidase
- pepes
-
arylamide
- drug development
-
lactase-phlorizin
- medicine
- synthesis
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
aspartyl aminopeptidase, dnpep, aspap, pfm18aap, peptidase e, acid peptidase, tgaap, m18aap, aspartyl-ap, alpha-aspartyl dipeptidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAP
alpha-aspartyl dipeptidase
-
-
-
-
Aminopeptidase
aminopeptidase A
-
-
-
-
angiotensinase
Ape4
Ape4 aspartyl aminopeptidase
Ape4 metalloprotease
Asp-AP
AspAP
aspartate aminopeptidase
-
-
-
-
aspartic aminopeptidase
-
-
-
-
aspartyl aminopeptidase
aspartyl(glutamyl)-specific aminopeptidase
aspartyl-AP
DAP
EC 3.4.11.7
glutamyl (aspartyl)-specific aminopeptidase A
glutamyl aminopeptidase
-
-
-
-
L-aspartate aminopeptidase
-
-
-
-
M18 aspartyl aminopeptidase
M18AAP
PepA
peptidase E
TgAAP
TGGT1_297970
Yhr113w
additional information
angiotensinase
-
-
-
-
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
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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
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
9074-83-3
-
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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
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-
-
-
?
L-Asp-7-amido-4-methylcoumarin + H2O
L-Asp + 7-amino-4-methylcoumarin
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-
-
?
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
?
-
-
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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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