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Ala-2-naphthylamide + H2O
Ala + 2-naphthylamine
Ala-4-methyl-coumaryl-7-amide + H2O
Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-4-nitroanilide + H2O
?
-
-
-
-
?
Ala-7-amido-4-methylcoumarin
Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala + H2O
Ala + Ala
-
45.4% of the activity with Ala-Trp
-
-
?
Ala-Asp + H2O
Ala + Asp
-
11.4% of the activity with Ala-Trp
-
-
?
Ala-Glu + H2O
Ala + Glu
-
19.0% of the activity with Ala-Trp
-
-
?
Ala-Gly + H2O
Ala + Gly
-
17.8% of the activity with Ala-Trp
-
-
?
Ala-Leu + H2O
Ala + Leu
-
27.1% of the activity with Ala-Trp
-
-
?
Ala-p-nitroanilide + H2O
Ala + p-nitroaniline
-
-
-
-
?
Ala-p-nitroanilide + H2O
L-alanine + p-nitroaniline
Ala-Phe + H2O
Ala + Phe
-
42.8% of the activity with Ala-Trp
-
-
?
Ala-Ser + H2O
Ala + Ser
-
22.5% of the activity with Ala-Trp
-
-
?
Ala-Trp + H2O
Ala + Trp
-
-
-
-
?
Ala-Val + H2O
Ala + Val
-
47.3% of the activity with Ala-Trp
-
-
?
Aplysia insulin D + H2O
?
-
Aplysia insulin D degrades slowly under the effects of mAAP
-
-
?
Arg-2-naphthylamide + H2O
Arg + 2-naphthylamine
Arg-7-amido-4-methylcoumarin
Arg + 7-amino-4-methylcoumarin
-
36% of the activity with Ala-7-amido-4-methylcoumarin
-
-
?
Arg-Arg-7-amido-4-methylcoumarin
?
-
13% of the activity with Ala-7-amido-4-methylcoumarin
-
-
?
CKKQ20KK + H2O
?
-
-
-
-
?
Gly-2-naphthylamide + H2O
Gly + 2-naphthylamine
-
13.7% of the activity with Ala-2-naphthylamide
-
-
?
glycine-4-methyl-coumaryl-7-amide + H2O
glycine + 7-amino-4-methylcoumarin
-
-
-
-
?
Ile-2-naphthylamide + H2O
Ile + 2-naphthylamide
-
-
-
-
?
KKE-(5-[(2-aminoethyl) amino]-naphthalene-1-sulfonic acid)-Q9K-((4'-dimethylaminoazobenzene-4'-sulfonyl))-K + H2O
?
-
-
-
-
?
KKQ30KK + H2O
?
-
-
-
-
?
L-Ala-2-naphthylamide + H2O
L-Ala + 2-naphthylamine
-
-
-
-
?
L-alanine-4-methylcoumaryl-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-enkephalin + H2O
L-Arg + enkephalin
-
-
-
-
?
L-arginine-4-methylcoumaryl-7-amide + H2O
L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-lysine-4-methylcoumaryl-7-amide + H2O
L-lysine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-methionine-4-methylcoumaryl-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-proline-4-methylcoumaryl-7-amide + H2O
L-proline + 7-amino-4-methylcoumarin
-
-
-
-
?
L-tyrosine-4-methylcoumaryl-7-amide + H2O
L-tyrosine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-valine-4-methylcoumaryl-7-amide + H2O
L-valine + 7-amino-4-methylcoumarin
-
-
-
-
?
Leu-(beta-naphthylamine) + H2O
Leu + naphthylamine
-
-
-
-
?
Leu-2-naphthylamide + H2O
Leu + 2-naphthylamine
Leu-4-methyl-coumaryl-7-amide + H2O
Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
Leu-7-amido-4-methylcoumarin
Leu + 7-amino-4-methylcoumarin
-
90% of the activity with Ala-7-amido-4-methylcoumarin
-
-
?
Leu-Ala + H2O
Leu + Ala
-
25.6% of the activity with Ala-Trp
-
-
?
Leu-Gly + H2O
Leu + Gly
-
5.5% of the activity with Ala-Trp
-
-
?
Leu-p-nitroanilide + H2O
Leu + p-nitroaniline
-
-
-
-
?
Lys-2-naphthylamide + H2O
Lys + 2-naphthylamine
Lys-7-amido-4-methylcoumarin
Lys + 7-amino-4-methylcoumarin
-
93% of the activity with Ala-7-amido-4-methylcoumarin
-
-
?
Lys-Ala-7-amido-4-methylcoumarin
?
-
79% of the activity with Ala-7-amido-4-methylcoumarin
-
-
?
Lys-p-nitroanilide + H2O
Lys + p-nitroaniline
-
-
-
-
?
Met-2-naphthylamide + H2O
Met + 2-naphthylamine
Met-7-amido-4-methylcoumarin
Met + 7-amino-4-methylcoumarin
-
97% of the activity with Ala-7-amido-4-methylcoumarin
-
-
?
Met-enkephalin + H2O
?
-
-
releases only the N-terminal tyrosine
-
?
Met-Lys-bradykinin + H2O
Met + Lys + bradykinin
-
-
-
?
Met-p-nitroanilide + H2O
Met + p-nitroaniline
-
-
-
-
?
Phe-2-naphthylamide + H2O
Phe + 2-naphthylamine
Phe-7-amido-4-methylcoumarin
Phe + 7-amino-4-methylcoumarin
-
84% of the activity with Ala-7-amido-4-methylcoumarin
-
-
?
Phe-Gly + H2O
Phe + Gly
-
19.2% of the activity with Ala-Trp
-
-
?
poly-Glu peptide + H2O
?
-
capable of rapidly digesting poly-Q sequences
-
-
?
Pro-7-amido-4-methylcoumarin
Pro + 7-amino-4-methylcoumarin
-
39% of the activity with Ala-7-amido-4-methylcoumarin
-
-
?
Pro-p-nitroanilide + H2O
Pro + p-nitroaniline
-
-
-
-
?
Pro-Phe-Arg-7-amido-4-methylcoumarin
?
-
20% of the activity with Ala-7-amido-4-methylcoumarin
-
-
?
Ser-2-naphthylamide + H2O
Ser + 2-naphthylamine
-
6.0% of the activity with Ala-2-naphthylamide
-
-
?
tau protein + H2O
?
-
-
-
-
?
Thr-2-naphthylamide + H2O
Thr + 2-naphthylamine
-
5.7% of the activity with Ala-2-naphthylamide
-
-
?
Trp-2-naphthylamide + H2O
Trp + 2-naphthylamine
-
19.2% of the activity with Ala-2-naphthylamide
-
-
?
Tyr-7-amido-4-methylcoumarin + H2O
Tyr + 7-amino-4-methylcoumarin
-
99% of the activity with Ala-7-amido-4-methylcoumarin
-
-
?
Val-2-naphthylamide + H2O
Val + 2-naphthylamine
-
-
-
-
?
Val-p-nitroanilide + H2O
Val + p-nitroaniline
-
-
-
-
?
additional information
?
-
Ala-2-naphthylamide + H2O
Ala + 2-naphthylamine
-
-
-
-
?
Ala-2-naphthylamide + H2O
Ala + 2-naphthylamine
-
-
-
-
?
Ala-p-nitroanilide + H2O
L-alanine + p-nitroaniline
-
-
-
-
?
Ala-p-nitroanilide + H2O
L-alanine + p-nitroaniline
-
-
-
-
?
Arg-2-naphthylamide + H2O
Arg + 2-naphthylamine
-
-
-
-
?
Arg-2-naphthylamide + H2O
Arg + 2-naphthylamine
-
28% of the activity with Ala-2-naphthylamide
-
-
?
Arg-2-naphthylamide + H2O
Arg + 2-naphthylamine
-
-
-
-
?
Leu-2-naphthylamide + H2O
Leu + 2-naphthylamine
-
-
-
-
?
Leu-2-naphthylamide + H2O
Leu + 2-naphthylamine
-
36.4% of the activity with Ala-2-naphthylamide
-
-
?
Leu-Leu + H2O
Leu + Leu
-
-
-
-
?
Leu-Leu + H2O
Leu + Leu
-
35.9% of the activity with Ala-Trp
-
-
?
Lys-2-naphthylamide + H2O
Lys + 2-naphthylamine
-
-
-
-
?
Lys-2-naphthylamide + H2O
Lys + 2-naphthylamine
-
13.4% of the activity with Ala-2-naphthylamide
-
-
?
Met-2-naphthylamide + H2O
Met + 2-naphthylamine
-
-
-
-
?
Met-2-naphthylamide + H2O
Met + 2-naphthylamine
-
57.5% of the activity with Ala-2-naphthylamide
-
-
?
Phe-2-naphthylamide + H2O
Phe + 2-naphthylamine
-
-
-
-
?
Phe-2-naphthylamide + H2O
Phe + 2-naphthylamine
-
62.8% of the activity with Ala-2-naphthylamide
-
-
?
additional information
?
-
-
there are two active centre ionizable groups with pKa values of approximately 6.0 and 7.5 which are involved in substrate binding or inhibitory amino acid binding
-
-
?
additional information
?
-
-
no activity with: Gly-Pro-7-amido-4-methylcoumarin, butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin, butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin, butyloxycarbonyl-ValPro-Arg-7-amido-4-methylcoumarin,succinyl-Ala-Ala-Ala-7-amido-4-methylcoumarin, succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin, succinyl-Gly-Pro-7-amido-4-methylcoumarin, succinyl-Gly-Pro-Leu-Gly-Pro-7-amido-4-methylcoumarin, succinyl-Ile-Ile-Trp-7-amido-4-methylcoumarin, benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin, acetyl-Asp-Glu-Val-Asp-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
does not digest Asn-Trp-Phe-NH2, Ala-Pro-Arg-Leu-Arg-Phe-Tyr-Ser, and angiotensin I
-
-
?
additional information
?
-
-
mAAP digests amino acids in the following approximate order: Ala > Phe > Tyr > Leu > Arg > Thr > Trp > Lys > Ser > Asp > His > Val
-
-
?
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11-aminoundecanoic acid
-
-
2,2'-bipyridine
-
5.0 mM, 29% inhibition
2,9-Dimethyl-1,10-phenanthroline
-
2.0 mM, 52% inhibition
6-aminopenicillanic acid
-
-
8-hydroxyquinoline
-
2.0 mM, 84% inhibition
acetonitrile
-
20% complete loss of activity
actinonin
-
0.1 mM, complete inactivation
Ala-Ala
-
inhibits hyrolysis of Ala-2-naphthylamide
Ala-Ala-Ala
-
inhibits hyrolysis of Ala-2-naphthylamide
Ala-Ala-Ala-Ala
-
inhibits hyrolysis of Ala-2-naphthylamide
Ala-Ala-Phe-chloromethyl ketone
-
-
anti-PSA immunglobulinb G
-
53.4% residual activity at 0.1 mg/ml
-
antipain
-
0.1 mM, 39% inhibition
Aprotinin
-
82% residual activity at 0.1 mM
arphamenine A
-
0.1 mM, 80% inactivation
azide
-
92% inhibition at 10 mM
benzamidine
-
1 mM, 14% inhibition
benzylpenicillenic acid
-
-
benzylpenicilloic acid
-
-
Cd2+
-
1 mM, complete inhibition
CdCl2
-
6.2% residual activity at 1 mM
chymostatin
-
0.1 mM, 83% inhibition
Co2+
-
1 mM, complete inhibition
Cu2+
-
1 mM, complete inhibition
CuSO4
-
0.6% residual activity at 1 mM
cyanide
-
84% inhibition at 10 mM
E-64
-
27.2% residual activity at 0.015 mM
ethanol
-
inactivation above 30%
Gly-Gly-Ala
-
inhibits hyrolysis of Ala-4-nitroanilide
Gly-Gly-Phe
-
inhibits hyrolysis of Ala-4-nitroanilide
iodoacetamide
-
1 mM, 57% inhibition
iodoacetic acid
-
1 mM, 11% inhibition
KCN
-
10 mM, 84% inhibition
L-arginine
-
19.3% residual activity at 5 mM
L-cysteine
-
non-competitive, 7.3% residual activity at 5 mM
L-isoleucine
-
20.1% residual activity at 5 mM
L-leucine
-
6.9% residual activity at 5 mM
L-phenylalanine
-
21.1% residual activity at 5 mM
L-tryptophan
-
15.5% residual activity at 5 mM
L-valine
-
23.7% residual activity at 5 mM
Leu
-
noncompetitive with Ala-2-naphthylamide, mixed type inhibition with Leu-Leu-Leu, competitive inhibition with Ala-Ala-Ala
leuhistin
-
0.1 mM, complete inactivation
Met
-
noncompetitive with Ala-2-naphthylamide
Met-NH2
-
competitive with Ala-2-naphthylamide
methanol
-
inactivation only above 30%
Methyl cellosolve
-
40% loss of activity at 40% solvent
Mg2+
-
1 mM, 20% inhibition
Mn2+
-
1 mM, 69% inhibition
Na2S
-
10 mM, 92% inhibition
NaCl
-
hydrolysis of Ala-4-nitropanilide, competitive inhibition at pH 6.6, inhibition is noncompetitive at pH 5.8, inhibition is mixed type at pH 6.2
NEM
-
1 mM, 43% inhibition
Ni2+
-
1 mM, 90% inhibition
octanoic acid
-
competitive
oxalate
-
50 mM ammonium oxalate, 71% inhibition
p-dioxane
-
inactivation only above 30%
phosphoramidon
-
0.1 mM, 17% inhibition
PMSF
-
1 mM, 40% inhibition; 1 mM, 64% inhibition
puromycin aminonucleoside
-
-
Tyr
-
noncompetitive with Ala-2-naphthylamide, competitive with Ala-Ala-Ala
ZnSO4
-
24% residual activity at 1 mM
1,10-phenanthroline
-
19.4% residual activity at 0.2 mM
1,10-phenanthroline
-
99% inhibition at 0.5 mM; Ki 0.028 mM
1,10-phenanthroline
-
1 mM, complete inhibition
amastatin
-
-
amastatin
-
0.1 mM, complete inactivation
bestatin
-
1.1% residual activity at 0.05 mM
bestatin
-
2.57% residual activity at 0.1 mM
bestatin
-
0.1 mM complete inactivation
EDTA
-
17.5% residual activity at 5 mM, 3,3% residual activity after extensively dialysis against 1 mM, restored by 0.01 mM Zn2+ to 57.8% activity
EDTA
-
98% inhibition at 0.001 mM
EDTA
-
44% residual activity at 0.5 mM
EDTA
-
2 mM, 26% inhibition
EGTA
-
24.3% residual activity at 5 mM
EGTA
-
96% inhibition at 1 mM; Ki 0.012 mM
Leu-Leu-Leu
-
-
Leu-Leu-Leu
-
inhibits hyrolysis of Ala-2-naphthylamide
leupeptin
-
83% residual activity at 0.1 mM
leupeptin
-
0.1 mM, 19% inhibition
Phe
-
-
Phe
-
noncompetitive with Ala-2-naphthylamide
puromycin
-
9.5% residual activity at 0.01 mM
puromycin
-
3.12% residual activity at 0.1 mM
puromycin
-
0.1 mM, complete inactivation, IC50: 0.0006 mM
Zn2+
-
79.4% residual activity at 0.01 mM
Zn2+
-
1 mM, complete inhibition
additional information
-
there are two active centre ionizable groups with pKa values of approximately 6.0 and 7.5 which are involved in substrate binding or inhibitory amino acid binding
-
additional information
-
not inhibited by phenylmethylsulfonylfluoride
-
additional information
-
D-glucose and insulin do not alter enzyme activity
-
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Adenomatous Polyposis Coli
Identification of differentially expressed genes in human pineal parenchymal tumors by microarray analysis.
Amyotrophic Lateral Sclerosis
Cu, Zn-superoxide dismutase 1 (SOD1) is a novel target of Puromycin-sensitive aminopeptidase (PSA/NPEPPS): PSA/NPEPPS is a possible modifier of amyotrophic lateral sclerosis.
Breast Neoplasms
Dictyostelium nucleomorphin is a member of the BRCT-domain family of cell cycle checkpoint proteins.
Cataract
Peptidases play an important role in cataractogenesis: an immunohistochemical study on lenses derived from Shumiya cataract rats.
cytosol alanyl aminopeptidase deficiency
Male reproductive defects caused by puromycin-sensitive aminopeptidase deficiency in mice.
Frontotemporal Dementia
Involvement of puromycin-sensitive aminopeptidase in proteolysis of tau protein in cultured cells, and attenuated proteolysis of frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17) mutant tau.
Infections
Identification and characterization of microRNA in the lung tissue of pigs with different susceptibilities to PCV2 infection.
Infertility, Female
Puromycin-sensitive aminopeptidase is essential for the maternal recognition of pregnancy in mice.
Neoplasms
Altered Activity and Expression of Cytosolic Peptidases in Colorectal Cancer.
Neoplasms
Altered levels of acid, basic, and neutral peptidase activity and expression in human clear cell renal cell carcinoma.
Neoplasms
Positioning of aminopeptidase inhibitors in next generation cancer therapy.
Neuroblastoma
cDNA cloning and molecular characterization of human brain metalloprotease MP100: a beta-secretase candidate?
Neuroblastoma
Puromycin-sensitive aminopeptidase (PSA/NPEPPS) impedes development of neuropathology in hPSA/TAUP301L double-transgenic mice.
Neurodegenerative Diseases
Brain-Specific Aminopeptidase: From Enkephalinase to Protector Against Neurodegeneration.
Pancreatic Neoplasms
Autophagy creates a CTL epitope that mimics tumor-associated antigens.
Pancreatic Neoplasms
Identification of a Ubiquitination-Related Gene Risk Model for Predicting Survival in Patients With Pancreatic Cancer.
Parkinsonian Disorders
Involvement of puromycin-sensitive aminopeptidase in proteolysis of tau protein in cultured cells, and attenuated proteolysis of frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17) mutant tau.
Stroke
Hemodynamic effects of epinephrine in rats: evaluation by impedance cardiography.
Stroke
The effects of whole body vibration combined computerized postural control training on the lower extremity muscle activity and cerebral cortex activity in stroke patients.
Tauopathies
A genomic screen for modifiers of tauopathy identifies puromycin-sensitive aminopeptidase as an inhibitor of tau-induced neurodegeneration.
Uremia
Enzyme cytochemistry of rat organs after uremia with special reference to proteases.
Virus Diseases
Puromycin-sensitive aminopeptidase limits MHC class I presentation in dendritic cells but does not affect CD8 T cell responses during viral infections.
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Starnes, W.L.; Szechinski, J.; Behal, F.J.
Human-liver alanine aminopeptidase. A kinin-converting enzyme sensitive to beta-lactam antibiotics
Eur. J. Biochem.
124
363-370
1982
Homo sapiens
brenda
Yamamoto, Y.; Li, Y.H.; Huang, K.; Ohkubo, I.; Nishi, K.
Isolation and characterization of an alanyl aminopeptidase from rat liver cytosol as a puromycin-sensitive enkephalin-degrading aminopeptidase
Biol. Chem.
379
711-719
1998
Rattus norvegicus
brenda
Garner, C.W.; Behal, F.J.
Hydrophobic binding sites of human liver alanine aminopeptidase
Arch. Biochem. Biophys.
182
667-673
1977
Homo sapiens
brenda
Little, G.H.; Starnes, W.L.; Behal, F.J.
Human liver aminopeptidase
Methods Enzymol.
45
495-503
1976
Homo sapiens
brenda
Garner, C.W.; Behal, F.J.
Effect of pH on substrate and inhibitor kinetic constants of human liver alanine aminopeptidase. Evidence for two ionizable active center groups
Biochemistry
14
5084-5088
1975
Homo sapiens
brenda
Garner, C.W.; Behal, F.J.
Human liver alanine aminopeptidase. Inhibition by amino acids
Biochemistry
14
3208-3212
1975
Homo sapiens
brenda
Starnes, W.L.; Behal, F.J.
A human liver aminopeptidase. The amino acid and carbohydrate content, and some physical properties of a sialic acid containing glycoprotein
Biochemistry
13
3221-3227
1974
Homo sapiens
brenda
Garner, C.W.; Behal, F.J.
Human liver aminopeptidase. Role of metal ions in mechanism of action
Biochemistry
13
3227-3233
1974
Homo sapiens
brenda
Kao, Y.J.; Starnes, W.L.; Behal, F.J.
Human kidney alanine aminopeptidase: physical and kinetic properties of a sialic acid containing glycoprotein
Biochemistry
17
2990-2994
1978
Homo sapiens
brenda
Fricke, B.; Aurich, H.
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