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Enzyme Nomenclature
Information on EC 3.4.11.21 - aspartyl aminopeptidase
for references in articles please use BRENDA:EC3.4.11.21
Word Map on EC 3.4.11.21
- 3.4.11.21
-
aminopeptidases
- angiotensin
-
renin-angiotensin
-
glutamyl
- gluap
- angiotensinase
-
alanyl
- aspartyl-aminopeptidase
-
glutamyl-aminopeptidase
- cysap
-
arylamides
- medicine
- synthesis
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Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
3.4.11.21
-
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RECOMMENDED NAME
GeneOntology No.
aspartyl aminopeptidase
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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 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
-
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
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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-naphthylamide + H2O
Asp + Ala-Pro-naphthylamine
-
preferring acidic amino acids favouring aspartyl residues, requires a free alpha-amino group
-
?
Asp-Ala-Pro-sulfamethoxazole + H2O
Asp + Ala-Pro-sulfamethoxazole
-
-
-
?
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
-
-
?
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
-
-
?
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
?
-
-
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
?
-
-
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mn2+
91% increase of activity at 0.4 mM; 91% increase of activity at 0.4 mM
additional information
Co2+
294% increase of activity at 0.4 mM; 294% increase of activity at 0.4 mM
additional information
-
activity is not enhanced by Ca2+, Fe2+, Mg2+, Mn2+, and Ni2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-[2-(acridin-9-ylamino)ethyl]benzene-1,2-diol
Q8I2J3
IC50 value for parasite growth is 0.0013 mM
NaCl
about 30% of activity is retained in 20% (w/v) NaCl; about 30% of activity is retained in 20% (w/v) NaCl
Ca2+
57% residual activity at 40 mM; 57% residual activity at 40 mM
EDTA
54% residual activity at 20 mM; 54% residual activity at 20 mM
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
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
-
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.94
Asp-Xaa
-
overexpressed enzyme
-
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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+
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00339
(S)-(+)-apomorphine
Q8I2J3
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
Q8I2J3
pH 7.5, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00013
-
normal healthy rats, soluble fraction of heart, APA; normal healthy rats, soluble fraction of lung, APA
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%
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
29 and 33 months old rats show a 50% decrease of enzymatic activity
additional information
-
bilateral distribution of aminopeptidases in stress-related areas, overview
additional information
-
enzyme in visceral organs during alterations in body fluid volume and osmolality, overview
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54430
calculated from amino acid sequence; calculated from amino acid sequence
55000
440000
680000
-
gel filtration; native enzyme, dodecamer, determined using a Superose 6 column
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dodecamer
homooctamer
-
8 * 65000, SDS-PAGE; 8 * 70000, high performance liquid chromatography
additional information
dodecamer
-
12 * 56000, SDS-PAGE; dodecamer comprising 12 identical units
dodecamer
-
12 * 56000, SDS-PAGE; dodecamer comprising 12 identical units
-
additional information
-
peptide mass fingerprinting by MALDI-TOF MS analysis
additional information
-
peptide mass fingerprinting by MALDI-TOF MS analysis
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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
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; 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
-
remarkably stable below 50°C, soon inactivated at 60°C
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2000fold to homogeneity, Triton X-100 solubilized microsomal fraction, DEAE-cellulose chromatography, immunoadsorbent chromatography; proteinase solubilized microsomal fraction, DEAE-cellulose chromatography, immunoadsorbent chromatography to homogeneity
-
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; native enzyme to homogeneity by ultracentrifugation, ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
-
DEAE-Sephacel gel filtration and TSK phenyl 5-PW gel filtration
Ni-Sepharose 6 Fast Flow column chromatography; Ni-Sepharose 6 Fast Flow column chromatography
non-fusion protein expressed in Escherichia coli, 440fold to homogeneity
-
partial, ammonium sulfate fractionation, gel filtration, ion-exchange chromatography
-
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
-
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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
-
expressed in Escherichia coli; expressed in Escherichia coli
expression in Escherichia coli
gene YHR113W, located on chromosome VIII, DNA and amino acid sequence determination and analysis
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H352F
-
dramatically reduced activity, destabilization of quarternary structure and dissociation of the native 440000 Da enzyme
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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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
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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
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dipeptide sweeteners aspartame and alitame
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LINKS TO OTHER DATABASES (specific for EC-Number 3.4.11.21)
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