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Information on EC 3.4.11.14 - cytosol alanyl aminopeptidase
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3.4.11.14 cytosol alanyl aminopeptidaseSpecify your search results
Word Map
- 3.4.11.14
- aminopeptidases
- bestatin
- amastatin
- beta-naphthylamides
- actinonin
-
enkephalin-degrading
-
tau-induced
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
release of an N-terminal amino acid, preferentially alanine, from a wide range of peptides, amides and arylamides
Synonyms
puromycin-sensitive aminopeptidase, mp100, microsomal alanyl aminopeptidase, nucleomorphin, psa/npepps, npepps, alanyl-ap, aap-s, soluble alanyl aminopeptidase, puromycin-sensitive neuron-aminopeptidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAP
AAP-S
-
-
-
-
AlaAP
alanyl aminopeptidase
alanyl-aminopeptidase
aminopeptidase, cytosol alanyl
-
-
-
-
Aminopolypeptidase
-
-
-
-
aminotripeptidase
-
-
-
-
cytyosol aminopeptidase III
-
-
-
-
NAP
NPEPPS
PSA
puromycin-sensitive aminopeptidase
puromycin-sensitive neuron-aminopeptidase
soluble alanyl aminopeptidase
-
-
-
-
tripeptidase
-
-
-
-
tripeptide aminopeptidase
-
-
-
-
alanyl aminopeptidase
-
-
-
-
alanyl aminopeptidase
-
the enzyme selectively degrades peptides lacking a D-amino acid in the second position from the N-terminus
puromycin-sensitive aminopeptidase
-
-
-
-
puromycin-sensitive aminopeptidase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of an N-terminal amino acid, preferentially alanine, from a wide range of peptides, amides and arylamides
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
exopeptidase, release of N-terminal amino acid
-
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CAS REGISTRY NUMBER
COMMENTARY
243859-94-1
-
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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
Aplysia insulin D + H2O
?
-
Aplysia insulin D degrades slowly under the effects of mAAP
-
-
?
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
-
-
?
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
-
-
-
-
?
KKE-(5-[(2-aminoethyl) amino]-naphthalene-1-sulfonic acid)-Q9K-((4'-dimethylaminoazobenzene-4'-sulfonyl))-K + H2O
?
-
-
-
-
?
L-alanine-4-methylcoumaryl-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarin
-
-
-
-
?
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-7-amido-4-methylcoumarin
Leu + 7-amino-4-methylcoumarin
-
90% of the activity with Ala-7-amido-4-methylcoumarin
-
-
?
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
-
-
?
Met-7-amido-4-methylcoumarin
Met + 7-amino-4-methylcoumarin
-
97% of the activity with Ala-7-amido-4-methylcoumarin
-
-
?
Phe-7-amido-4-methylcoumarin
Phe + 7-amino-4-methylcoumarin
-
84% of the activity with Ala-7-amido-4-methylcoumarin
-
-
?
Pro-7-amido-4-methylcoumarin
Pro + 7-amino-4-methylcoumarin
-
39% of the activity with Ala-7-amido-4-methylcoumarin
-
-
?
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
-
-
?
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
-
-
?
Ala-2-naphthylamide + H2O
Ala + 2-naphthylamine
-
-
-
-
?
Arg-2-naphthylamide + H2O
Arg + 2-naphthylamine
-
28% of the activity with Ala-2-naphthylamide
-
-
?
Leu-2-naphthylamide + H2O
Leu + 2-naphthylamine
-
36.4% of the activity with Ala-2-naphthylamide
-
-
?
Lys-2-naphthylamide + H2O
Lys + 2-naphthylamine
-
13.4% of the activity with Ala-2-naphthylamide
-
-
?
Met-2-naphthylamide + H2O
Met + 2-naphthylamine
-
57.5% of the activity with Ala-2-naphthylamide
-
-
?
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Zinc
Co2+
-
2.4fold activation, Co2+ binds loosely in a noncompetitive manner
Zinc
-
the enzyme contains 1 mol of zinc per 113500 g of protein, the zinc is firmly bound
Zinc
-
1 mol Zn2+ for 113500 g protein, firmly bound, not removed by chelating agents
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Leu
-
noncompetitive with Ala-2-naphthylamide, mixed type inhibition with Leu-Leu-Leu, competitive inhibition with Ala-Ala-Ala
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
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
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
-
D-glucose and insulin do not alter enzyme activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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 levels of acid, basic, and neutral peptidase activity and expression in human clear cell renal cell carcinoma.
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
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.
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.27
Ala-p-nitroanilide
-
with 1 mM dithiothreitol, in 10 mM Tris-HCl, pH 7.4, at 37°C
0.25
Leu-p-nitroanilide
-
with 1 mM dithiothreitol, in 10 mM Tris-HCl, pH 7.4, at 37°C
2.2
Lys-p-nitroanilide
-
with 1 mM dithiothreitol, in 10 mM Tris-HCl, pH 7.4, at 37°C
0.8
Met-p-nitroanilide