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Information on EC 3.4.11.2 - membrane alanyl aminopeptidase and Organism(s) Rattus norvegicus and UniProt Accession P15684
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EC Tree
3.4.11.2 membrane alanyl aminopeptidaseSpecify your search results
Word Map
- 3.4.11.2
- bestatin
-
dipeptidyl
- border
-
brush
- endopeptidase
- angiotensin
- carboxypeptidase
- enkephalin
- urinary
- midguts
- thuringiensis
- sucrase
- enterocytes
- jejunum
- maltase
- tripeptides
-
n-acetyl-beta-d-glucosaminidase
- neuropeptides
-
gamma-glutamyl
- metallopeptidases
-
leukotriene
-
brush-border
- enkephalinase
-
nephrotoxicity
-
opioids
-
angiotensin-converting
- phosphoramidon
- gamma-glutamyltransferase
- thiorphan
- captopril
- transpeptidase
- microvillar
- sexta
-
manduca
- coronaviruses
-
ectoenzyme
- sucrase-isomaltase
- p-nitroanilide
-
dipeptidylpeptidase
- disaccharidase
-
3.4.24.11
- arylamidase
- leu-enkephalin
- oxytocinase
-
insulin-regulated
- prolidase
- helveticus
- medicine
- lta4
- dppiv
- gamma-glutamyltranspeptidase
- drug development
- diagnostics
- nutrition
- analysis
- pharmacology
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Release of an N-terminal amino acid, Xaa-/-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide
Synonyms
aminopeptidase, aminopeptidase n, dipeptidase, aminopeptidase m, alanine aminopeptidase, apn/cd13, gp150, aminopeptidase-n, anpep, alanyl aminopeptidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alanine aminopeptidase
-
-
-
-
alanine-specific aminopeptidase
-
-
-
-
alanyl aminopeptidase
-
-
-
-
Alpha-aminoacylpeptide hydrolase
-
-
-
-
amino-oligopeptidase
-
-
-
-
aminopeptidase M
aminopeptidase M II
-
-
-
-
aminopeptidase N
aminopeptidase, microsomal
-
-
-
-
APN1
-
-
-
-
APN2
-
-
-
-
CD13
CryIA(C) receptor
-
-
-
-
GP 130
-
-
-
-
GP150
-
-
-
-
L-alanine aminopeptidase
-
-
-
-
Leukemia antigen CD13
-
-
-
-
Lys-AP
-
-
-
-
Lysyl aminopeptidase
-
-
-
-
Membrane glycoprotein H11
-
-
-
-
Membrane protein p161
-
-
-
-
Microsomal aminopeptidase
-
-
-
-
Myeloid plasma membrane glycoprotein CD13
-
-
-
-
particle-bound aminopeptidase
-
-
-
-
aminopeptidase M
-
-
-
-
aminopeptidase N
-
-
-
-
aminopeptidase N
-
-
CD13
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
9054-63-1
-
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
L-Ala-7-amido-4-carbamoylmethylcoumarin + H2O
L-Ala + 7-amino-4-carbamoylmethylcoumarin
-
-
-
?
L-alanine 4-methylcoumaryl-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarin
Ala-MCA
-
-
?
L-alanyl-L-alanyl-L-7-amido-4-carbamoylmethylcoumarin + H2O
L-alanyl-L-alanine + 7-amino-4-carbamoylmethylcoumarin
substrate for use with tripeptidyl peptidases
-
-
?
L-alanyl-L-alanyl-L-phenylalanine 4-methylcoumaryl-7-amide + H2O
L-alanyl-L-alanyl-L-phenylalanine + 7-amino-4-methylcoumarin
Ala-Ala-Phe-MCA or AAF-MCA
-
-
?
L-arginine 4-methylcoumaryl-7-amide + H2O
L-arginine + 7-amino-4-methylcoumarin
Arg-MCA
-
-
?
L-Leu-7-amido-4-carbamoylmethylcoumarin + H2O
L-Leu + 7-amino-4-carbamoylmethylcoumarin
70% of the activity with L-Ala-7-amido-4-carbamoylmethylcoumarin
-
-
?
L-leucine 4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
Leu-MCA
-
-
?
L-lysine 4-methylcoumaryl-7-amide + H2O
L-lysine + 7-amino-4-methylcoumarin
Lys-MCA, low activity
-
-
?
L-Met-7-amido-4-carbamoylmethylcoumarin + H2O
L-Met + 7-amino-4-carbamoylmethylcoumarin
99% of the activity with L-Ala-7-amido-4-carbamoylmethylcoumarin
-
-
?
L-methionine 4-methylcoumaryl-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
Met-MCA
-
-
?
L-Phe-7-amido-4-carbamoylmethylcoumarin + H2O
L-Phe + 7-amino-4-carbamoylmethylcoumarin
76% of the activity with L-Ala-7-amido-4-carbamoylmethylcoumarin
-
-
?
L-phenylalanine 4-methylcoumaryl-7-amide + H2O
L-phenylalanine + 7-amino-4-methylcoumarin
Phe-MCA
-
-
?
aminoacyl peptide
?
-
-
-
-
?
enkephalin
?
-
may be involved in enkephalin neurotransmitter inactivation
-
-
?
L-Ala-2-naphthylamide + H2O
L-Ala + 2-naphthylamine
-
-
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-alaninyl 4-methoxy-2-naphthylamide + H2O
L-alanine + 4-methoxy-2-naphthylamine
-
-
-
?
dipeptides + H2O
amino acids
-
not: D-Ala-Gly, Val-Gly, Asp-Gly, Gly-D-Ala, Pro-containing peptides
-
?
dipeptides + H2O
amino acids
-
not: D-Ala-Gly, Val-Gly, Asp-Gly, Gly-D-Ala, Pro-containing peptides
-
?
additional information
?
-
enzyme preferentially cleaves neutral and nonpolar amino acids such as alanine, methionine, leucine, and phenylalanine at the P1 position, substrates with basic amino acids such as lysine and arginine at the P1 position are less cleaved. Pyroglutamic acid, and Bz-Arginine, are not cleaved at all
-
-
?
additional information
?
-
the peptidase that hydrolyzes AAF-MCA is the soluble form of aminopeptidase N/CD13, and caution is required when using AAF-MCA as a substrate for tripeptidyl peptidase assays. No activity with Pyr-MCA and Bz-Arg-MCA
-
-
?
additional information
?
-
-
the enzyme is involved in hematopoiesis and bone growth, increased enzyme expression occurs during angiogenesis associated with cancer development
-
-
?
additional information
?
-
-
substrate specificity, overview, chain length influencs the activity rate, dipeptides are readily hydrolyzed, the enzyme prefers substrates with N-terminal L-Ala residues, the specificity for N-terminal residues is descending order is Ala, Phe, Tyr, Leu, Arg, Thr, Trp, Lys, Ser, Asp, His, Val. Pro- and alpha- or gamma-Glu-derivatives are slowly hydrolyzed, when a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide
-
-
?
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
aminoacyl peptide
?
-
-
-
-
?
enkephalin
?
-
may be involved in enkephalin neurotransmitter inactivation
-
-
?
additional information
?
-
-
the enzyme is involved in hematopoiesis and bone growth, increased enzyme expression occurs during angiogenesis associated with cancer development
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zn2+
-
the enzyme contains a typical zinc-binding motif HEXXH, one Zn2+ per subunit
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1-aminohexyl)((2-(methoxycarbonyl)benzyl)carbamothioyl)phosphinic acid
-
-
1-amino-3-methylbutyl(2-(methoxycarbonyl)benzylcarbamothioyl)phosphinic acid
-
-
1-amino-3-phenylpropyl(3-(methylthio)propylcarbamothioyl)phosphinic acid
-
-
1-amino-3-phenylpropyl(4-(ethoxycarbonyl)benzylcarbamothioyl)phosphinic acid
-
-
4-(2-(((1-aminobutyl)(hydroxy)phosphoryl)methanethioamido)ethyl)benzoic acid
-
-
alpha1-amino-3-phenylpropyl(alpha2-hydroxy-3-phenylpropyl)phosphinic acid
-
very potent inhibitor of APN
PC-18
-
inhibition of enzyme in angiotensin type 1 receptor-blocked rats augments the natriuretic response to angiotensin III
[3-[(1-amino-ethyl)-hydroxy-phosphinoyl]-2-phenyl-propionylamino]-phenyl-acetic acid
-
-
2(S)-benzyl-3-[hydroxy(1'(R)-aminoethyl)phosphinyl]propanoyl-L-3-iodotyrosine
-
[125I]-isotope, i.e. [125I]RB 129, highly potent and selective inhibitor, radiolabeled, study of binding properties and kinetics
2(S)-benzyl-3-[hydroxy(1'(R)-aminoethyl)phosphinyl]propanoyl-L-3-iodotyrosine
-
iodinated RB129
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
morphine
-
increase in activity in the striatum by 28% compared to untreated rats, and slightly in the hypothalamus and amygdala, withdrawal of the opioid reduces enzyme activity by 42%, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000203
2(S)-benzyl-3-[hydroxy(1'(R)-aminoethyl)phosphinyl]propanoyl-L-3-iodotyrosine
-
pH 7.4, 35°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0011
(1-amino-2-methylpropyl)(1-hydroxy-3-phenylpropyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0016
(1-amino-2-phenylethyl)(1-hydroxy-3-phenylpropyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00092
(1-amino-3-methylbutyl)(1-hydroxy-3-phenylpropyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0012
(1-aminobutyl)(1-hydroxy-2-phenylethyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0035
(1-aminoethyl)[hydroxy[4-(propan-2-yl)phenyl]methyl]phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.02
(1-aminohexyl)((2-(methoxycarbonyl)benzyl)carbamothioyl)phosphinic acid
Rattus norvegicus
-
IC50 above 0.02 mM, at 37°C in 100 mM Tris-HCl, pH 7.5
0.00046
(1-aminopentyl)(1-hydroxy-2-phenylpropyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00052
(1-aminopentyl)(1-hydroxy-3-phenylpropyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0062
(1-aminopentyl)[hydroxy(4-hydroxyphenyl)methyl]phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0024
(1-aminopropyl)(1-hydroxy-3-phenylpropyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00505
1-amino-2-methylpropyl(hexylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00895
1-amino-2-methylpropyl(isobutylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.02135
1-amino-2-methylpropyl(methylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.02
1-amino-3-methylbutyl(2-(methoxycarbonyl)benzylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
IC50 above 0.02 mM, at 37°C in 100 mM Tris-HCl, pH 7.5
0.0051
1-amino-3-methylbutyl(benzylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0017
1-amino-3-methylbutyl(hexylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0108
1-amino-3-methylbutyl(methylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0054
1-amino-3-methylbutyl(phenethylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00165
1-amino-3-phenylpropyl(3-(methylthio)propylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.02
1-amino-3-phenylpropyl(4-(ethoxycarbonyl)benzylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
IC50 above 0.02 mM, at 37°C in 100 mM Tris-HCl, pH 7.5
0.00265
1-amino-3-phenylpropyl(4-methoxybenzylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0025
1-amino-3-phenylpropyl(benzylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00135
1-amino-3-phenylpropyl(propylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.02
1-aminobutyl(2-(methoxycarbonyl)phenethylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
IC50 above 0.02 mM, at 37°C in 100 mM Tris-HCl, pH 7.5
0.00145
1-aminobutyl(3-(methylthio)propylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.02
1-aminobutyl(4-(ethoxycarbonyl)phenethylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
IC50 above 0.02 mM, at 37°C in 100 mM Tris-HCl, pH 7.5
0.00245
1-aminobutyl(4-methoxyphenethylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0021
1-aminobutyl(benzylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00255
1-aminobutyl(phenethylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00345
1-aminoethyl(3-(methylthio)propylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.02
1-aminoethyl(4-(ethoxycarbonyl)benzylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
IC50 above 0.02 mM, at 37°C in 100 mM Tris-HCl, pH 7.5
0.02
1-aminoethyl(4-methoxybenzylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
IC50 above 0.02 mM, at 37°C in 100 mM Tris-HCl, pH 7.5
0.000145
1-aminoethyl(benzylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0087
1-aminoethyl(phenethylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.02
1-aminopentyl(2-(methoxycarbonyl)benzylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
IC50 above 0.02 mM, at 37°C in 100 mM Tris-HCl, pH 7.5
0.00061
1-aminopentyl(3-(methylthio)propylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00105
1-aminopentyl(4-methoxybenzylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0011
1-aminopentyl(benzylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00062
1-aminopentyl(phenethylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0025
1-aminopropyl(3-(methylthio)propylcarbamothioyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.02
4-(2-(((1-aminobutyl)(hydroxy)phosphoryl)methanethioamido)ethyl)benzoic acid
Rattus norvegicus
-
IC50 above 0.02 mM, at 37°C in 100 mM Tris-HCl, pH 7.5
0.0004
alpha1-amino-3-phenylpropyl(alpha2-hydroxy-3-phenylpropyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0047
[amino(phenyl)methyl](1-hydroxy-3-methylbutyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0022
[amino(phenyl)methyl](1-hydroxy-3-phenylpropyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0152
[amino(phenyl)methyl](1-hydroxyethyl)phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00046
[amino(phenyl)methyl][hydroxy(phenyl)methyl]phosphinic acid
Rattus norvegicus
-
at 37°C in 100 mM Tris-HCl, pH 7.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
enzyme activities in membrane 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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
positive staining for the enzyme is limited strictly to the membrane of the hepatocytes that consist of bile canaliculi
additional information
located in brush border of a renal proximal tubule and the small intestine, and the surface membrane of bile canaliculi
renal proximal tubule, no immunoreactivity to the antiserum is found in the glomeruli, in the distal renal tubular epithelial cells, or in the renal tubules in the medulla
located in brush border of a renal proximal tubule and the small intestine, and the surface membrane of bile canaliculi
positive staining for the enzyme is limited strictly to the membrane of the hepatocytes that consist of bile canaliculi, but no signal is seen in the sinusoidal wall. The low expression of the enzyme in the liver might be due to the limited localization on the bile canaliculi
brush border of the epithelium in the small intestine
located in brush border of a renal proximal tubule and the small intestine, and the surface membrane of bile canaliculi
-
cortex and anterior brain, striatum and middle brain, posterior brain, low enzyme activity
-
of fully or partially kindled rats. Aminopeptidase N mRNA levels are decreased at stage II and increased at stage V of kindling, in frontal cortex-olfactory tubercle, and hippocampus. Neprilysin and aminopeptidase N enzymatic activities, follow similar variations to their respective mRNA levels. The coordinated changes of neprilysin and aminopeptidase N expression are opposite to those previously observed for pyroglutamyl peptidaseII mRNA and activity levels in limbic regions
additional information
-
enzyme in visceral organs during alterations in body fluid volume and osmolality, overview
additional information
-
ontogenic and adult whole body distribution of aminopeptidase N, developmental expression pattern in organ compartments, detailed overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
type II integral membrane protein located on the plasma membrane as an ectoenzyme
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
an early high increase in the excretion or activity of the enzyme in supernatant of urine from cisplatin-treated rats are correlated with the extent of renal damage
malfunction
-
amelioration of intrarenal angiotensin II type 2 receptor-mediated natriuresis in prehypertensive spontaneously hypertensive rats is achieved through inhibition of renal APN activity
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AMPN_RAT
965
1
109449
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000
91000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
?
x * 137000, enzyme from kidney, SDS-PAGE, x * 110000, enzyme from small intestine, SDS-PAGE, x * 140000, enzyme from liver, SDS-PAGE
additional information
the N-terminal amino acid sequence of the peptidase is x-Ala-Pro-x-Leu-Pro-Gly-Ser-Thr-Ser-Ala-Thr-x-x-Ser, where x indicates undetectable amino acid residues. The undetectable amino acid residues such as threonine or serine might be modified residues that often undergo glycosylation or phosphorylation
additional information
-
the enzyme contains a small cytoplasmic domain, a 24-amino-acid hydrophobic segment close to the N-terminus which serves as membrane anchor, and the bulk domain including the active site as ectodomain
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increase of AlaAp in microvesicular and exosomal fractions from cisplatin-treated rats
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
determination of AlaAp content or its enzymatic activity in microvesicular and exosomal fractions of urine is an early and predictive biomarker of renal dysfunction in cisplatin-induced nephrotoxicity. Nephrotoxic effect of cisplatin over tubular epithelia can be assessed independently of creatinine status or diuresis, overview. It might also be a very useful marker in pathologies where evaluation of early tubular damage takes relevance
medicine
medicine
-
the enzyme might be a therapeutic target in pathological processes, such as tumor proliferation and/or angiogenesis associated with cancer development
medicine
-
inhibition of enzyme in angiotensin type 1 receptor-blocked rats augments the natriuretic response to angiotensin III
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tate, S.S.
Microvillus membrane peptidases that catalyze hydrolysis of cysteinylglycine and its derivatives
Methods Enzymol.
113
471-484
1985
Rattus norvegicus
Gros, C.; Giros, B.; Schwartz, J.C.
Identification of aminopeptidase M as an enkephalin-inactivating enzyme in rat cerebral membranes
Biochemistry
24
2179-2185
1985
Rattus norvegicus
Erickson, R.H.; Kim, Y.S.
Interaction of purified brush-border membrane aminopeptidase N and dipeptidyl peptidase IV with lectin-sepharose derivatives
Biochim. Biophys. Acta
743
37-42
1983
Rattus norvegicus
Kozak, E.M.; Tate, S.S.
Glutathione-degrading enzymes of microvillus membranes
J. Biol. Chem.
257
6322-6327
1982
Rattus norvegicus
Gray, G.M.; Santiago, N.A.
Intestinal surface amino-oligopeptidases. I. Isolation of two weight isomers and their subunits from rat brush border
J. Biol. Chem.
252
4922-4928
1977
Rattus norvegicus
Kim, Y.S.; Brophy, E.J.
Rat intestinal brush border membrane peptidases. I. Solubilization, purification, and physicochemical properties of two different forms of the enzyme
J. Biol. Chem.
251
3199-3205
1976
Rattus norvegicus
Wojnarowska, F.; Gray, G.M.
Intestinal surface peptide hydrolases: identification and characterization of three enzymes from rat brush border
Biochim. Biophys. Acta
403
147-160
1975
Rattus norvegicus
Watt, V.M.; Yip, C.C.
Amino acid sequence deduced from a rat kidney cDNA suggests it encodes the Zn-peptidase aminopeptidase N
J. Biol. Chem.
264
5480-5487
1989
Rattus norvegicus
Malfroy, B.; Kado-Fong, H.; Gros, C.; Giros, B.; Schwartz, J.C.; Hellmiss, R.
Molecular cloning and amino acid sequence of rat kidney aminopeptidase M: a member of a super family of zinc-metallohydrolases
Biochem. Biophys. Res. Commun.
161
236-241
1989
Rattus norvegicus
Noble, F.; Luciani, N.; Da Nacimento, S.; Lai-Kuen, R.; Bischoff, L.; Chen, H.; Fournie-Zaluski, M.C.; Roques, B.P.
Binding propeties of a highly potent and selecive iodinated aminopeptidase N inhibitor appropriate for radioautography
FEBS Lett.
467
81-86
2000
Rattus norvegicus, Sus scrofa
Acartuerk, F.; Parlatan, Z.I.; Saracoglu, O.F.
Comparison of vaginal aminopeptidase enzymatic activities in various animals and in humans
J. Pharm. Pharmacol.
53
1499-1504
2001
Cavia porcellus, Oryctolagus cuniculus, Ovis aries, Homo sapiens, Rattus norvegicus
Irazusta, J.; Larrinaga, G.; Agirregoitia, N.; Varona, A.; Casis, L.
Effects of morphine administration and its withdrawal on rat brain aminopeptidase activities
Regul. Pept.
110
225-230
2003
Rattus norvegicus
Jardinaud, F.; Banisadr, G.; Noble, F.; Melik-Parsadaniantz, S.; Chen, H.; Dugave, C.; Laplace, H.; Rostene, W.; Fournie-Zaluski, M.C.; Roques, B.P.; Popovici, T.
Ontogenic and adult whole body distribution of aminopeptidase N in rat investigated by in vitro autoradiography
Biochimie
86
105-113
2004
Rattus norvegicus
Turner, A.J.
Membrane alanyl aminopeptidase
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
289-294
2004
Oryctolagus cuniculus, Homo sapiens, Lactococcus lactis, Lymantria dispar, Rattus norvegicus, Sus scrofa
-
Agirregoitia, N.; Laiz-Carrion, R.; Varona, A.; Rio, M.P.; Mancera, J.M.; Irazusta, J.
Distribution of peptidase activity in teleost and rat tissues
J. Comp. Physiol. B
175
433-444
2005
Oncorhynchus mykiss, Rattus norvegicus, Sparus aurata
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
Banegas, I.; Prieto, I.; Vives, F.; Alba, F.; de Gasparo, M.; Segarra, A.B.; Hermoso, F.; Duran, R.; Ramirez, M.
Brain aminopeptidases and hypertension
J. Renin Angiotensin Aldosterone Syst.
7
129-134
2006
Rattus norvegicus
Padia, S.H.; Kemp, B.A.; Howell, N.L.; Siragy, H.M.; Fournie-Zaluski, M.C.; Roques, B.P.; Carey, R.M.
Intrarenal aminopeptidase N inhibition augments natriuretic responses to angiotensin III in angiotensin type 1 receptor-blocked rats
Hypertension
49
625-630
2007
Rattus norvegicus
de Gortari, P.; Vargas, M.A.; Martinez, A.; Garcia-Vazquez, A.I.; Uribe, R.M.; Chavez-Gutierrez, L.; Magdaleno, V.; Boileau, G.; Charli, J.L.; Joseph-Bravo, P.
Stage-specific modulation of neprilysin and aminopeptidase N in the limbic system during kindling progression
J. Mol. Neurosci.
33
252-261
2007
Rattus norvegicus
Yang, L.E.; Sandberg, M.B.; Can, A.D.; Pihakaski-Maunsbach, K.; McDonough, A.A.
Effects of dietary salt on renal Na+ transporter subcellular distribution, abundance, and phosphorylation status
Am. J. Physiol. Renal Physiol.
295
F1003-F1016
2008
Rattus norvegicus
Timofeeva, N.M.; Egorova, V.V.; Nikitina, A.A.; Dmitrieva, J.V.
Delayed effects of the terms of separation of rat pups from lactating females and low-protein diet on enzyme activity in digestive and non-digestive organs
Bull. Exp. Biol. Med.
145
676-679
2008
Rattus norvegicus
Grzywa, R.; Oleksyszyn, J.; Salvesen, G.S.; Drag, M.
Identification of very potent inhibitor of human aminopeptidase N (CD13)
Bioorg. Med. Chem. Lett.
20
2497-2499
2010
Homo sapiens, Rattus norvegicus, Sus scrofa
Padia, S.H.; Howell, N.L.; Kemp, B.A.; Fournie-Zaluski, M.C.; Roques, B.P.; Carey, R.M.
Intrarenal aminopeptidase N inhibition restores defective angiotensin II type 2-mediated natriuresis in spontaneously hypertensive rats
Hypertension
55
474-480
2010
Rattus norvegicus
Shibata, M.; Koike, M.; Kusumi, S.; Sato, N.; Uchiyama, Y.
A specific tripeptidyl substrate for tripeptidyl peptidase activity is effectively hydrolyzed by alanyl aminopeptidase/aminopeptidase N/CD13 in the rat kidney
Arch. Histol. Cytol.
76
1-8
2016
Rattus norvegicus (P15684), Rattus norvegicus Wistar (P15684)
-
Quesada, A.; Segarra, A.B.; Montoro-Molina, S.; de Gracia, M.D.; Osuna, A.; O'Valle, F.; Gomez-Guzman, M.; Vargas, F.; Wangensteen, R.
Glutamyl aminopeptidase in microvesicular and exosomal fractions of urine is related with renal dysfunction in cisplatin-treated rats
PLoS ONE
12
e0175462
2017
Rattus norvegicus (P15684), Rattus norvegicus Wistar (P15684)
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