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angiotensin + H2O
Asp + des-Asp-angiotensin
angiotensin I + H2O
Asp + Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
angiotensin I + H2O
Asp + des-Asp-angiotensin I
-
-
-
-
?
angiotensin I + H2O
L-Asp + des-Asp-angiotensin I
-
-
-
?
angiotensin II + H2O
Asp + angiotensin III
angiotensin II antipeptide + H2O
?
-
-
-
-
?
angiotensin II antipeptide + H2O
Glu + Gly-Val-Thr-Val-His-Pro-Val
-
i.e. Glu-Gly-Val-Thr-Val-His-Pro-Val
-
-
?
angiotensinogen 1-14 + H2O
?
-
-
-
-
?
angiotensinogen 1-14 + H2O
Asp + Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser, low activity
-
-
?
Arg 2-naphthylamide + H2O
Arg + 2-naphthylamine
-
-
-
?
Asp 2-naphthylamide + H2O
Asp + 2-naphthylamine
Asp-2-naphthylamide + H2O
Asp + 2-naphthylamine
Asp-7-amido-4-methylcoumarin + H2O
Asp + 7-amino-4-methylcoumarin
-
-
-
-
?
Asp-Ala + H2O
Asp + Ala
-
-
-
?
Asp-Ala-Pro-chromogen + H2O
Asp + Ala-Pro-chromogen
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-Lys + H2O
Asp + Lys
-
-
-
?
Asp-Lys-Ala-Leu + H2O
Asp + Lys-Ala-Leu
Asp-p-nitroanilide + H2O
Asp + p-nitroaniline
64% activity
-
-
?
Asp-Xaa + H2O
Asp + Xaa
-
-
-
r
Asp-Xaa-Xaa + H2O
Asp + Xaa-Xaa
-
no activity on oligopeptides larger than tripeptides
-
r
Asp-Xaa-Xaa-Xaa + H2O
Asp + Xaa-Xaa-Xaa
-
neutral or hydrophobic amino acids in P1 position preferred
-
?
aspartyl peptides + H2O
Asp + des-Asp-angiotensin
Glu 2-naphthylamide + H2O
Glu + 2-naphthylamine
Glu-7-amido-4-methylcoumarin + H2O
Glu + 7-amino-4-methylcoumarin
-
-
-
-
?
Glu-p-nitroanilide + H2O
Glu + p-nitroaniline
100% activity
-
-
?
L-Asp-2-naphthylamide + H2O
L-Asp + 2-naphthylamine
-
-
-
-
?
L-aspartyl-beta-naphthylamide + H2O
L-aspartic acid + beta-naphthylamine
-
-
-
?
Lys 2-naphthylamide + H2O
Lys + 2-naphthylamine
-
-
-
?
N-(alpha-L-aspartyl)-4-nitroanilide + H2O
L-aspartic acid + 4-nitroaniline
N-(alpha-L-glutamyl)-2-naphthylamide + H2O
L-glutamic acid + 2-naphthylamine
N-(alpha-L-glutamyl)-4-nitroanilide + H2O
L-glutamic acid + 4-nitroaniline
additional information
?
-
angiotensin + H2O

Asp + des-Asp-angiotensin
-
intracellular protein and peptide metabolism
-
?
angiotensin + H2O
Asp + des-Asp-angiotensin
-
metabolism of angiotensin I, angiotensin II, cholecystokinin-8 and neuropeptide, solube and membrane-bound AspAP play different functional roles in the brain
-
?
angiotensin + H2O
Asp + des-Asp-angiotensin
-
intracellular protein and peptide metabolism
-
?
angiotensin + H2O
Asp + des-Asp-angiotensin
-
-
-
?
angiotensin + H2O
Asp + des-Asp-angiotensin
-
intracellular protein and peptide metabolism
-
?
Angiotensin I + H2O

?
-
-
-
-
?
Angiotensin I + H2O
?
-
-
-
-
?
angiotensin I + H2O

Asp + Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
-
-
?
angiotensin I + H2O
Asp + Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
-
-
?
Angiotensin II + H2O

?
-
-
-
-
?
Angiotensin II + H2O
?
-
-
-
-
?
angiotensin II + H2O

Asp + angiotensin III
-
-
-
?
angiotensin II + H2O
Asp + angiotensin III
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
Asp + angiotensin III
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
Asp + angiotensin III
-
octapeptides preferred to tetrapeptides
-
?
angiotensin II + H2O
Asp + angiotensin III
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
Asp + angiotensin III
-
aspartyl aminopeptidase and several other aminopeptidases, i.e. angiotensinases, are involved in angiotensin II and cholecystokinin, CCK, metabolism, angiotensin II is the principal effector of the renin-angiotensin-system, RAS, which induces vasoconstriction and increases sodium and water retention thereby leading to increased blood pressure
-
-
?
angiotensin II + H2O
Asp + angiotensin III
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
Asp + angiotensin III
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe, best substrate
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
Asp + angiotensin III
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe, best substrate
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
Asp 2-naphthylamide + H2O

Asp + 2-naphthylamine
-
higher affinity for Asp 2-naphthylamide than for Glu 2-naphthylamide
-
?
Asp 2-naphthylamide + H2O
Asp + 2-naphthylamine
-
-
-
?
Asp 2-naphthylamide + H2O
Asp + 2-naphthylamine
-
attacked more rapidly than 2-naphthylamide derivates of neutral or basic amino acids
-
?
Asp-2-naphthylamide + H2O

Asp + 2-naphthylamine
-
-
-
-
?
Asp-2-naphthylamide + H2O
Asp + 2-naphthylamine
-
-
-
-
?
Asp-2-naphthylamide + H2O
Asp + 2-naphthylamine
-
most susceptible substrate
-
-
?
Asp-Ala-Pro-chromogen + H2O

Asp + Ala-Pro-chromogen
-
-
-
-
?
Asp-Ala-Pro-chromogen + H2O
Asp + Ala-Pro-chromogen
-
-
-
-
?
Asp-Ala-Pro-chromogen + H2O
Asp + Ala-Pro-chromogen
-
-
-
-
?
Asp-Lys-Ala-Leu + H2O

Asp + Lys-Ala-Leu
-
lower activity
-
-
?
Asp-Lys-Ala-Leu + H2O
Asp + Lys-Ala-Leu
-
lower activity
-
-
?
Asp-Lys-Ala-Leu + H2O
Asp + Lys-Ala-Leu
-
lower activity
-
-
?
aspartyl peptides + H2O

Asp + des-Asp-angiotensin
-
catabolism of intracellular proteins, breakdown of abnormal cell proteins, supplement of nutritional sources
-
?
aspartyl peptides + H2O
Asp + des-Asp-angiotensin
-
activation and degradation of several neuropeptides, excitatory Asp and Glu implicated in pathogenesis of different neurogeneratives diseases
-
?
Glu 2-naphthylamide + H2O

Glu + 2-naphthylamine
-
-
-
?
Glu 2-naphthylamide + H2O
Glu + 2-naphthylamine
-
attacked more rapidly than 2-naphthylamide derivatives of neutral or basic amino acids
-
-
?
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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(S)-(+)-apomorphine
Q8I2J3
IC50 value for parasite growth is 0.004 mM
1-amino-1,3-propanediphosphonic acid
-
-
3-amino-3-(P-methylphosphinyl)propionic acid
-
-
3-amino-3-phosphonopropionic acid
-
-
3-amino-3-[P-(2-carboxypropyl)phosphinyl]propionic acid
-
-
4-amino-4-(P-phenylphosphinyl)butyric acid
-
20% inhibition at 1.83 mM
4-amino-4-phosphonobutyric acid
-
-
4-amino-4-[P-(2-carboxypropyl)phosphinyl]butyric acid
-
-
4-[2-(acridin-9-ylamino)ethyl]benzene-1,2-diol
Q8I2J3
IC50 value for parasite growth is 0.0013 mM
5-amino-5-phosphonopentanoic acid
-
-
Cu2+
-
strongly inhibitory
dithiothreitol
-
88% inhibition at 1 mM
EGTA
-
slightly inhibitory from 2 mM to 5 mM
NaCl
about 30% of activity is retained in 20% (w/v) NaCl; about 30% of activity is retained in 20% (w/v) NaCl
p-chloromercuribenzoate
-
-
pyridoxal 5'-phosphate
-
-
1,10-phenanthroline

-
complete inhibition
1,10-phenanthroline
-
complete inhibition
1,10-phenanthroline
-
after preincubation total loss of activity
1,10-phenanthroline
-
complete inhibition
1,10-phenanthroline
-
; 33.5% inhibition at 5 mM
Ca2+

57% residual activity at 40 mM; 57% residual activity at 40 mM
DTT

-
high inhibition at 1 mM
DTT
-
high inhibition at 1 mM
DTT
-
88% inhibition at 1 mM
EDTA

54% residual activity at 20 mM; 54% residual activity at 20 mM
EDTA
-
activity is reduced to 14% after incubating with 10 mM EDTA
EDTA
-
; 76.1% inhibition at 20 mM
EDTA
-
strong inhibitory from 2 mM to 5 mM
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
Zn2+
-
50% inhibition at 0.4 M, after preincubation total inhibition
Zn2+
-
Zn2+ abolishes activity at 1 mM
Zn2+
-
strongly inhibitory
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
-
additional information
-
not inhibited by amastatin, bestatin, or EDTA
-
additional information
-
poor inhibition by bestatin at 0.2 mM
-
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Anti-Glomerular Basement Membrane Disease
Chloride Channel ClC-5 Binds to Aspartyl Aminopeptidase to Regulate Renal Albumin Endocytosis.
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.
Hyperthyroidism
Angiotensinase activity in hypothalamus and pituitary of hypothyroid, euthyroid and hyperthyroid adult male rats.
Hyperthyroidism
Atrial angiotensinase activity in hypothyroid, euthyroid, and hyperthyroid rats.
Hyperthyroidism
Influence of thyroid disorders on kidney angiotensinase activity.
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 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
Glutamyl- but not aspartyl-aminopeptidase activity is modified in serum of N-methyl nitrosourea-induced rat mammary tumours.
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.
Proteinuria
Chloride Channel ClC-5 Binds to Aspartyl Aminopeptidase to Regulate Renal Albumin Endocytosis.
Proteinuria
Urinary aminopeptidase activities as early and predictive biomarkers of renal dysfunction in cisplatin-treated rats.
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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
Homo sapiens, Oryctolagus cuniculus, 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
Homo sapiens, Mus musculus, Oryctolagus cuniculus
-
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, Aspergillus oryzae (Q2U9Z9), Aspergillus oryzae (Q2UPZ7)
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.
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Plasmodium falciparum
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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
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Rattus norvegicus
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Banegas, I.; Prieto, I.; Vives, F.; Alba, F.; de Gasparo, M.; Segarra, A.B.; Hermoso, F.; Duran, R.; Ramirez, M.
Brain aminopeptidases and hypertension
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Rattus norvegicus
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Lee, S.; Kim, J.S.; Yun, C.H.; Chae, H.Z.; Kim, K.
Aspartyl aminopeptidase of Schizosaccharomyces pombe has a molecular chaperone function
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Schizosaccharomyces pombe (O36014), Schizosaccharomyces pombe
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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
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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
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Mus musculus (Q9Z2W0)
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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
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Saccharomyces cerevisiae
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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
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Didelphis sp., Rattus norvegicus
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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
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Homo sapiens, Homo sapiens (Q9ULA0)
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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
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Plasmodium falciparum, Plasmodium falciparum (Q8I2J3)
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