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Information on EC 3.4.11.3 - cystinyl aminopeptidase
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3.4.11.3 cystinyl aminopeptidaseSpecify your search results
Word Map
- 3.4.11.3
- envelope
- pregnancy
- viruses
- vaccinia
- angiotensin
- t-cells
-
humoral
-
hiv-1-infected
-
aminopeptidases
-
virion
- macaque
-
simian
-
hiv-specific
-
syncytium
- insipidus
-
immunodominant
-
anti-hiv-1
-
vaccinees
- chymosin
- desmopressin
-
pepsinogen
-
1-infected
-
hiv-seropositive
-
seronegative
-
glut4-containing
-
cross-neutralizing
-
milk-clotting
-
intrarectal
-
sivmac239
-
non-neutralizing
- shiv
-
seroconverted
-
seropositive
-
oligosaccharyltransferase
-
radioimmunoprecipitation
-
ddavp
- furin
-
alum
- medicine
-
hiv-1iiib
-
virus-neutralizing
- gag-pol
-
prime-boost
-
vaccine-induced
- angiotensinase
-
virus-like
- chimpanzee
- seroconversion
-
hiv-seronegative
-
anti-cd4
-
hiv-induced
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Release of an N-terminal amino acid, Cys-/-Xaa-, in which the half-cystine residue is involved in a disulfide loop, notably in oxytocin or vasopressin. Hydrolysis rates on a range of aminoacyl arylamides exceed that for the cystinyl derivative, however
Synonyms
gp160, p-lap, oxytocinase, insulin-regulated aminopeptidase, vasopressinase, at4 receptor, cystine aminopeptidase, placental leucine aminopeptidase, otase, insulin-responsive aminopeptidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-Aminoacyl-peptide hydrolase
-
-
-
-
aminopeptidase, cystyl
-
-
-
-
AT4 receptor
CAP-I
-
-
-
-
CAP-II
-
-
-
-
cysteine aminopeptidase
-
-
-
-
cystine aminopeptidase
Cystinyl aminopeptidase
cystyl aminopeptidase
-
-
-
-
GP160
insulin-regulated aminopeptidase
Insulin-regulated membrane aminopeptidase
Insulin-responsive aminopeptidase
IRAP
L-cystine aminopeptidase
-
-
-
-
OTase
-
-
-
-
oxytocin peptidase
-
-
-
-
oxytocinase
P-LAP
P-LAP/IRAP
Placental leucine aminopeptidase
placental leucine aminopeptidase/oxytocinase
placental leucine aminopeptidase/oxytocinase/insulin-regulated membrane aminopeptidase
-
-
vasopresssinase
-
-
-
-
Vesicle protein of 165 kDa
-
-
-
-
Vp165
yscXVI
-
-
-
-
cystine aminopeptidase
-
-
-
-
Cystinyl aminopeptidase
-
-
-
-
GP160
-
-
-
-
Insulin-regulated membrane aminopeptidase
-
-
-
-
Insulin-responsive aminopeptidase
-
-
-
-
IRAP
-
-
-
-
oxytocinase
-
-
-
-
P-LAP
-
-
-
-
Placental leucine aminopeptidase
-
-
-
-
Placental leucine aminopeptidase
-
-
Vp165
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Release of an N-terminal amino acid, Cys-/-Xaa-, in which the half-cystine residue is involved in a disulfide loop, notably in oxytocin or vasopressin. Hydrolysis rates on a range of aminoacyl arylamides exceed that for the cystinyl derivative, however
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
exopeptidase, N-terminus amino acid
-
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CAS REGISTRY NUMBER
COMMENTARY
9031-41-8
-
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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
alpha-L-Asp1-Val5-angiotensin II + H2O
beta-Asp1-Val5-angiotensin II
-
transformation to beta form
-
ir
Arg-4-methylcoumaryl-7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
-
-
?
L-benzyl-L-cysteine-p-nitroanilide + H2O
L-benzyl-L-cysteine + p-nitroaniline
-
-
-
-
?
L-leucine-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
-
L-leucine-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
-
-
-
?
Lys-4-methylcoumaryl-7-amide + H2O
Lys + 7-amino-4-methylcoumarin
-
-
-
?
Met-4-methylcoumaryl-7-amide + H2O
Met + 7-amino-4-methylcoumarin
-
-
-
?
Peptides + H2O
?
-
enzyme plays a role in general metabolism of peptides during pregnancy
-
-
-
S-benzyl-Cys-4-methylcoumaryl-7-amide + H2O
S-benzyl-Cys + 7-amino-4-methylcoumarin
-
-
-
?
S-benzyl-cysteine-4-methylcoumarin 7-amide + H2O
S-benzyl-cysteine + 7-amino-4-methylcoumarin
-
-
-
-
?
angiotensin III + H2O
?
-
P-LAP/OTase may be involved in maintaining pregnancy homeostasis via metabolizing peptides such as oxytocin and vasopressin
-
-
?
angiotensin III + H2O
?
-
the enzyme plays a role in blood pressure regulation via hydrolyzing vasopressin and angiotensin III
-
-
?
L-cystine-di-p-nitroanilide + H2O
L-cystine + p-nitroaniline
-
-
-
-
?
Leu-4-methylcoumaryl-7-amide + H2O
Leu + 7-amino-4-methylcoumarin
-
-
-
?
oxytocin + H2O
?
-
in the placenta the enzyme is thought to play a role in the prevention of premature labour and maintenance of an adequate blood flow to the uterus
-
-
?
oxytocin + H2O
?
-
P-LAP in HUVEC cells regulates effects of oxytocin with resolution
-
-
?
oxytocin + H2O
?
-
cleavage sites: Cys-/-Tyr-/-Ile-/-Gln-/-Asn-/-Cys-Pro-Leu-Gly-NH2
-
-
?
oxytocin + H2O
?
-
cleavage sites: Cys-/-Tyr-/-Phe-/-Gln-Asn-Cys-Pro-Arg-Gly-NH2
-
-
?
oxytocin + H2O
acyclic peptide + H2O
-
-
tyrosyl-isoleucyl-glutaminyl-asparaginyl-S-(S-cysteine)cysteinyl-prolyl-leucyl-glycinamide, first product
?
oxytocin + H2O
acyclic peptide + H2O
-
cleavage of bond between N-terminal cysteine and adjacent tyrosine
-
-
?
S-benzyl-L-cysteine-p-nitroanilide + H2O
S-benzyl-L-cysteine + p-nitroaniline
-
-
-
-
-
S-benzyl-L-cysteine-p-nitroanilide + H2O
S-benzyl-L-cysteine + p-nitroaniline
-
-
-
-
?
S-benzyl-L-cysteine-p-nitroanilide + H2O
S-benzyl-L-cysteine + p-nitroaniline
-
-
-
-
?
S-benzyl-L-cysteine-p-nitroanilide + H2O
S-benzyl-L-cysteine + p-nitroaniline
-
-
-
-
?
Vasopressin + H2O
?
-
P-LAP/OTase may be involved in maintaining pregnancy homeostasis via metabolizing peptides such as oxytocin and vasopressin
-
-
?
Vasopressin + H2O
?
-
the enzyme plays a role in blood pressure regulation via hydrolyzing vasopressin and angiotensin III
-
-
?
vasopressin + H2O
hydrolyzed vasopressin
-
vasopressin is a physiological substrate
N-terminal processing
-
?
additional information
?
-
-
peptides having proline as the second amino acid residue
-
-
-
additional information
?
-
-
peptides having proline as the second amino acid residue
-
-
-
additional information
?
-
-
peptides having proline as the second amino acid residue
-
-
-
additional information
?
-
-
not: L-Asp-beta-naphthylamide, L-Glu-beta-naphthylamide
-
-
-
additional information
?
-
-
hydrolyses neutral, aromatic, basic and acidic N-terminal amino acids from peptides
-
-
-
additional information
?
-
-
N-terminal aspartic acid bound via its beta-carboxyl group in a peptide bond
-
-
-
additional information
?
-
-
N-terminal aspartic acid bound via its beta-carboxyl group in a peptide bond
-
-
-
additional information
?
-
-
in individuals with type 2 diabetes the insulin-stimulated translocation of IRAP to the cell-surface of muscle and fat cells is impaired. This defect may lead to decreased cleavage and consequently increased action of peptide hormones that are substrates for IRAP. Impaiered IRAP action may thus play a role in the development of complications in type 2 diabetes
-
-
-
additional information
?
-
-
involvement of the enzyme in memory processing. AT4 ligands, upon binding to the catalytic site of insulin-regulated aminopeptidase, enhance spatial learning, facilitate memory retention and retrieval and reverse amnesia
-
-
-
additional information
?
-
-
vasopressinase cannot degrade 1-deamino-8D-arginine vasopressin
-
-
-
additional information
?
-
-
IRAP is required for maintenance of key constituents of endosome-derived vesicles in cardiac muscle cells
-
-
-
additional information
?
-
-
IRAP is involved in glucose transporter GLUT4 storage vesicle trafficking
-
-
-
additional information
?
-
-
the enzyme plays an imprtant role for IRAP in reproductive physiology in regulating the action of peptide hormones
-
-
-
additional information
?
-
-
activity is greatly increased in rats with mammary tumors. The activity may be involved in the promotion and progression of breast cancer through oxytocin, vasopressin and/or renin-angiotensin system misregulation
-
-
-
additional information
?
-
-
the enzyme is involved in the metabolism of angiotensin
-
-
-
additional information
?
-
-
the enzyme plays a role as a mediator for the effects of angiotensin IV and related peptides on extracellular dopamine levels in striatum
-
-
-
additional information
?
-
-
the enzyme plays diverse physiological roles in the rat central nervous system
-
-
-
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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
Peptides + H2O
?
-
enzyme plays a role in general metabolism of peptides during pregnancy
-
-
-
vasopressin + H2O
hydrolyzed vasopressin
-
vasopressin is a physiological substrate
N-terminal processing
-
?
angiotensin III + H2O
?
-
P-LAP/OTase may be involved in maintaining pregnancy homeostasis via metabolizing peptides such as oxytocin and vasopressin
-
-
?
angiotensin III + H2O
?
-
the enzyme plays a role in blood pressure regulation via hydrolyzing vasopressin and angiotensin III
-
-
?
oxytocin + H2O
?
-
in the placenta the enzyme is thought to play a role in the prevention of premature labour and maintenance of an adequate blood flow to the uterus
-
-
?
oxytocin + H2O
?
-
P-LAP in HUVEC cells regulates effects of oxytocin with resolution
-
-
?
Vasopressin + H2O
?
-
P-LAP/OTase may be involved in maintaining pregnancy homeostasis via metabolizing peptides such as oxytocin and vasopressin
-
-
?
Vasopressin + H2O
?
-
the enzyme plays a role in blood pressure regulation via hydrolyzing vasopressin and angiotensin III
-
-
?
additional information
?
-
-
in individuals with type 2 diabetes the insulin-stimulated translocation of IRAP to the cell-surface of muscle and fat cells is impaired. This defect may lead to decreased cleavage and consequently increased action of peptide hormones that are substrates for IRAP. Impaiered IRAP action may thus play a role in the development of complications in type 2 diabetes
-
-
-
additional information
?
-
-
IRAP is required for maintenance of key constituents of endosome-derived vesicles in cardiac muscle cells
-
-
-
additional information
?
-
-
IRAP is involved in glucose transporter GLUT4 storage vesicle trafficking
-
-
-
additional information
?
-
-
the enzyme plays an imprtant role for IRAP in reproductive physiology in regulating the action of peptide hormones
-
-
-
additional information
?
-
-
activity is greatly increased in rats with mammary tumors. The activity may be involved in the promotion and progression of breast cancer through oxytocin, vasopressin and/or renin-angiotensin system misregulation
-
-
-
additional information
?
-
-
the enzyme is involved in the metabolism of angiotensin
-
-
-
additional information
?
-
-
the enzyme plays a role as a mediator for the effects of angiotensin IV and related peptides on extracellular dopamine levels in striatum
-
-
-
additional information
?
-
-
the enzyme plays diverse physiological roles in the rat central nervous system
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
-
inhibitory effect of EDTA plus 1,10-phenanthroline can be completely reversed by Zn2+. Ca2+ and Mg2+ increase the potency of Zn2+ for this process
Mn2+
Zinc
Zn2+
Ca2+
-
inhibitory effect of EDTA plus 1,10-phenanthroline can be completely reversed by Zn2+. Ca2+ and Mg2+ increase the potency of Zn2+ for this process
Zinc
-
enzyme contains 1 mol of zinc per mol of enzyme, contains the consensus HEXXH(X)18E motif of zinc-metallopeptidase proteins
Zinc
-
contains the characteristic Zn2+-coordination sequence element, HEXXH-(18-64X)-E
Zn2+
-
inhibitory effect of EDTA plus 1,10-phenanthroline can be completely reversed by Zn2+. Ca2+ and Mg2+ increase the potency of Zn2+ for this process
Zn2+
-
complete inhibition of the enzyme activity by 0.1 mM EDTA and 0.1 mM 1,10-phenanthroline can be prevented in the presence of 0.04-0.1 mM ZnCl2
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2-[[(1-[[3-(4-hydroxybenzyl)-5-(L-norleucylamino)phenyl]carbonyl]-L-prolyl)amino]methyl]phenyl)acetic acid
-
-
(2-[[(1-[[3-(4-hydroxybenzyl)-5-(L-valylamino)phenyl]carbonyl]-L-prolyl)amino]methyl]phenyl)acetic acid
-
-
(2-[[(N-[[3-(4-hydroxybenzyl)-5-(L-norleucylamino)phenyl]carbonyl]-L-isoleucyl)amino]methyl]phenyl)acetic acid
-
-
(2-[[(N-[[3-(4-hydroxybenzyl)-5-(L-norleucylamino)phenyl]carbonyl]-L-leucyl)amino]methyl]phenyl)acetic acid
-
-
(2-[[(N-[[3-(4-hydroxybenzyl)-5-(L-valylamino)phenyl]carbonyl]-L-isoleucyl)amino]methyl]phenyl)acetic acid
-
-
(2-[[(N-[[3-amino-5-(4-hydroxybenzyl)phenyl]carbonyl]-L-isoleucyl)amino]methyl]phenyl)acetic acid
-
-
1,2-Acyclic oxytocin
-
slight inhibition of oxytocin degradation, marked inhibition of cystine di-beta-naphthylamide degradation
2,2'-bipyridine
-
acetic acid-containing chelators potentiate the inhibitory effect of 2,2'-bipyridine. Efficiacy decreases in the order: diethylenetriamine-N,N,N',N'',N''-pentaacetic acid, EDTA, EGTA
2-[[(1-[[3-(4-hydroxybenzyl)-5-(L-norleucylamino)phenyl]carbonyl]-L-prolyl)amino]methyl]benzoic acid
-
-
2-[[(1-[[3-(4-hydroxybenzyl)-5-(L-valylamino)phenyl]carbonyl]-L-prolyl)amino]methyl]benzoic acid
-
-
2-[[(N-[[3-(4-hydroxybenzyl)-5-(L-norleucylamino)phenyl]carbonyl]-L-isoleucyl)amino]methyl]benzoic acid
-
-
2-[[(N-[[3-(4-hydroxybenzyl)-5-(L-norleucylamino)phenyl]carbonyl]-L-leucyl)amino]methyl]benzoic acid
-
-
2-[[(N-[[3-(4-hydroxybenzyl)-5-(L-valylamino)phenyl]carbonyl]-L-isoleucyl)amino]methyl]benzoic acid
-
-
4-bromo-5-chloro-N-methyl-N-[3-(1H-tetrazol-5-yl)phenyl]thiophene-2-sulfonamide
-
-
4-bromo-5-chloro-N-[3-(1-methyl-1H-tetrazol-5-yl)phenyl]thiophene-2-sulfonamide
-
-
4-bromo-5-chloro-N-[3-(1H-tetrazol-5-yl)phenyl]thiophene-2-carboxamide
-
-
4-bromo-5-chloro-N-[3-(1H-tetrazol-5-yl)phenyl]thiophene-2-sulfonamide
-
-
7-chloro-N-[3-(1H-tetrazol-5-yl)phenyl]-1,3-dihydro-2,1,3-benzoxadiazole-4-sulfonamide
-
-
benzyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tryptophanate
-
benzyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-valinate
-
benzyl N-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tryptophanate
-
benzyl N-[3-amino-4-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoyl]-L-tryptophanate
-
benzyl N-[3-amino-4-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tryptophanate
-
benzyl N-[4-amino-3-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tryptophanate
-
cyclohexylmethyl 2-amino-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
50% inhibition at 100 microM
ethyl 2,7-diamino-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
50% inhibition at 100 microM
ethyl 2-amino-4-(2,4-dichloropyridin-3-yl)-7-hydroxy-4H-chromene-3-carboxylate
-
-
ethyl 2-amino-4-(5,8-dihydroquinolin-2-yl)-7-hydroxy-4H-chromene-3-carboxylate
-
-
ethyl 2-amino-4-[4-(dimethylamino)phenyl]-7-hydroxy-4H-chromene-3-carboxylate
-
-
ethyl 2-amino-6-bromo-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
50% inhibition at 100 microM
ethyl 2-amino-7-(dimethylamino)-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
50% inhibition at 100 microM
ethyl 2-amino-7-(formyloxy)-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
50% inhibition at 100 microM
ethyl 2-amino-7-hydroxy-4-(1,3-thiazol-2-yl)-4H-chromene-3-carboxylate
-
50% inhibition at 100 microM
ethyl 2-amino-7-hydroxy-4-(thiophen-2-yl)-4H-chromene-3-carboxylate
-
50% inhibition at 100 microM
ethyl 2-amino-7-hydroxy-4-[4-(pyridin-2-yl)phenyl]-4H-chromene-3-carboxylate
-
-
ethyl 2-amino-7-methoxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
50% inhibition at 100 microM
L-Arg-vasopressin
-
Ki-value for wild-type, mutants G428E, G428D, G428Q above 0.03 mM
L-Val-L-Tyr-L-Ile-2-aminomethylphenylacetic acid
-
inhibits both IRAP and aminopeptidase N and induces proliferation of stem cells at low concentrations
L-Val-L-Tyr-L-Ile-L-Cys-L-Pro-L-Cys
-
cyclic disulfide, angiotensin IV analog, considerably more stable than angiotensin IV toward enzymatic degradation
methyl 4-amino-3-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoate
-
methyl 4-amino-3-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoate
-
methyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
-
methyl N-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
-
methyl N2-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-argininate
-
methyl N2-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-lysinate
-
methyl N2-(4-amino-3-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-lysinate
-
methyl N2-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-lysinate
-
methyl N2-[4-amino-3-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoyl]-L-lysinate
-
N-(3-amino-4-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
-
N-(4-amino-3-[[(2R)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
-
N-[[3-(4-hydroxybenzyl)-5-(L-valylamino)phenyl]carbonyl]-L-isoleucyl-L-histidyl-L-prolyl-L-phenylalanine
-
-
N2-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-ornithine
-
[2-amino-7-hydroxy-4-(pyridin-3-yl)-4H-chromen-3-yl](phenyl)methanone
-
50% inhibition at 100 microM
[2-[([[3-(4-hydroxybenzyl)-5-(L-valylamino)phenyl]carbonyl]amino)methyl]phenyl]acetic acid
-
-
[2-[([[3-amino-5-(4-hydroxybenzyl)phenyl]carbonyl]amino)methyl]phenyl]acetic acid
-
-
1,10-phenanthroline
-
competition between 1,10-phenanthroline and the substrate only in presence of EDTA. Inhibitory effect of EDTA plus 1,10-phenanthroline can be completely reversed by Zn2+. Ca2+ and Mg2+ increase the potency of Zn2+ for this process
1,10-phenanthroline
-
IC50: 0.2 mM. Inhibitory effect is substantially potentiated by both EDTA and EGTA. A combined and complete inhibition of the enzyme activity by 0.1 mM EDTA and 0.1 mM 1,10-phenanthroline can be prevented in the presence of 0.04-0.1 mM ZnCl2
L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe
-
i.e. angiotensin IV, adopts a gamma-turn in the C-terminal of its bioactive conformation
additional information
-
inhibitory potency in decreasing order: angiotensin III, angiotensin IV, LVV-hemorphin 7, divalinal/angiotensin IV, angiotensin II, angiotensin 4-8
-
additional information
-
inhibitory potency in decreasing order: angiotensin IV, angiotensin III, LVV-hemorphin 7, divalinal/angiotensin IV, angiotensin 4-8, angiotensin III
-
additional information
-
inhibitory potency in decreasing order: angiotensin IV, angiotensin III, divalinal/angiotensin IV, LVV-hemorphin 7, angiotensin 4-8, angiotensin III
-
additional information
-
inhibitory potency in decreasing order: angiotensin IV, angiotensin III, divalinal/angiotensin IV, LVV-hemorphin 7, angiotensin 4-8, angiotensin III
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0033
(2-[[(1-[[3-(4-hydroxybenzyl)-5-(L-norleucylamino)phenyl]carbonyl]-L-prolyl)amino]methyl]phenyl)acetic acid
-
-
0.0074
(2-[[(1-[[3-(4-hydroxybenzyl)-5-(L-valylamino)phenyl]carbonyl]-L-prolyl)amino]methyl]phenyl)acetic acid
-
-
0.0014
(2-[[(N-[[3-(4-hydroxybenzyl)-5-(L-norleucylamino)phenyl]carbonyl]-L-isoleucyl)amino]methyl]phenyl)acetic acid
-
-
0.0039
(2-[[(N-[[3-(4-hydroxybenzyl)-5-(L-norleucylamino)phenyl]carbonyl]-L-leucyl)amino]methyl]phenyl)acetic acid
-
-
0.0013
(2-[[(N-[[3-(4-hydroxybenzyl)-5-(L-valylamino)phenyl]carbonyl]-L-isoleucyl)amino]methyl]phenyl)acetic acid
-
-
97
(2-[[(N-[[3-amino-5-(4-hydroxybenzyl)phenyl]carbonyl]-L-isoleucyl)amino]methyl]phenyl)acetic acid
-
-
0.05
2-amino-4-(3,4-dimethoxyphenyl)-7-hydroxy-4H-chromene-3-carbonitrile
-
pH 7.4, 37°C
0.1
2-amino-4-(3,5-dimethoxyphenyl)-7-hydroxy-4H-chromene-3-carbonitrile
-
value above, pH 7.4, 37°C
0.1
2-amino-4-[4-(dimethylamino)phenyl]-7-hydroxy-4H-chromene-3-carbonitrile
-
value above, pH 7.4, 37°C
0.1
2-amino-7-hydroxy-4-(3,4,5-trimethoxyphenyl)-4H-chromene-3-carbonitrile
-
value above, pH 7.4, 37°C
0.1
2-amino-7-hydroxy-4-(3-methoxyphenyl)-4H-chromene-3-carbonitrile
-
value above, pH 7.4, 37°C
0.1
2-amino-7-hydroxy-4-(4-methoxyphenyl)-4H-chromene-3-carbonitrile
-
value above, pH 7.4, 37°C
0.1
2-amino-7-hydroxy-4-(pyridin-4-yl)-4H-chromene-3-carbonitrile
-
value above, pH 7.4, 37°C
0.004
2-methoxyethyl 2-amino-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.0063
2-[[(1-[[3-(4-hydroxybenzyl)-5-(L-norleucylamino)phenyl]carbonyl]-L-prolyl)amino]methyl]benzoic acid
-
-
0.012
2-[[(1-[[3-(4-hydroxybenzyl)-5-(L-valylamino)phenyl]carbonyl]-L-prolyl)amino]methyl]benzoic acid
-
-
0.0018
2-[[(N-[[3-(4-hydroxybenzyl)-5-(L-norleucylamino)phenyl]carbonyl]-L-isoleucyl)amino]methyl]benzoic acid
-
-
0.0037
2-[[(N-[[3-(4-hydroxybenzyl)-5-(L-norleucylamino)phenyl]carbonyl]-L-leucyl)amino]methyl]benzoic acid
-
-
0.0013
2-[[(N-[[3-(4-hydroxybenzyl)-5-(L-valylamino)phenyl]carbonyl]-L-isoleucyl)amino]methyl]benzoic acid
-
-
0.00006
angiotensin IV
-
in 50 mM Tris-HCl (pH 7.4), 140 mM NaCl, 0.1% (w/v) bovine serum albumin, and 0.1 mM phenylmethylsulfonyl fluoride, at 37°C
0.0017
benzyl 2-amino-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.0026
butyl 2-amino-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.00048
ethyl 2-(acetylamino)-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.00003
ethyl 2-(acetylamino)-7-hydroxy-4-(quinolin-3-yl)-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.014
ethyl 2-amino-4-(2,4-dichloropyridin-3-yl)-7-hydroxy-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.1
ethyl 2-amino-4-(2-cyanophenyl)-7-hydroxy-4H-chromene-3-carboxylate
-
value above, pH 7.4, 37°C
0.0062
ethyl 2-amino-4-(3,4-dimethoxyphenyl)-7-hydroxy-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.035
ethyl 2-amino-4-(3-chlorophenyl)-7-hydroxy-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.0032
ethyl 2-amino-4-(3-cyanophenyl)-7-hydroxy-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.1
ethyl 2-amino-4-(4-bromophenyl)-7-hydroxy-4H-chromene-3-carboxylate
-
value above, pH 7.4, 37°C
0.1
ethyl 2-amino-4-(4-chlorophenyl)-7-hydroxy-4H-chromene-3-carboxylate
-
value above, pH 7.4, 37°C
0.011
ethyl 2-amino-4-(4-cyanophenyl)-7-hydroxy-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.003
ethyl 2-amino-4-(5,8-dihydroquinolin-2-yl)-7-hydroxy-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.1
ethyl 2-amino-4-(pyridin-3-yl)-4H-benzo[g]chromene-3-carboxylate
-
value above, pH 7.4, 37°C
0.1
ethyl 2-amino-4-(pyridin-3-yl)-4H-benzo[h]chromene-3-carboxylate
-
value above, pH 7.4, 37°C
0.0053
ethyl 2-amino-4-[4-(dimethylamino)phenyl]-7-hydroxy-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.0056
ethyl 2-amino-6-chloro-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.042
ethyl 2-amino-7-hydroxy-4-(2-nitrophenyl)-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.1
ethyl 2-amino-7-hydroxy-4-(4-methylphenyl)-4H-chromene-3-carboxylate
-
value above, pH 7.4, 37°C
0.0077
ethyl 2-amino-7-hydroxy-4-(4-nitrophenyl)-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.0029
ethyl 2-amino-7-hydroxy-4-(pyridin-2-yl)-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.0018
ethyl 2-amino-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.0037
ethyl 2-amino-7-hydroxy-4-(pyridin-4-yl)-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.00036
ethyl 2-amino-7-hydroxy-4-(quinolin-3-yl)-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.0009
ethyl 2-amino-7-hydroxy-4-(quinolin-4-yl)-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.1
ethyl 2-amino-7-hydroxy-4-phenyl-4H-chromene-3-carboxylate
-
value above, pH 7.4, 37°C
0.1
ethyl 2-amino-7-hydroxy-4-[4-(pyridin-2-yl)phenyl]-4H-chromene-3-carboxylate
-
value above, pH 7.4, 37°C
0.0098
ethyl 2-amino-8-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.0049
methyl 2-amino-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.0012
N-[[3-(4-hydroxybenzyl)-5-(L-valylamino)phenyl]carbonyl]-L-isoleucyl-L-histidyl-L-prolyl-L-phenylalanine
-
-
0.0016
propyl 2-amino-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
0.0119
tert-butyl 2-amino-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
pH 7.4, 37°C
16
[2-[([[3-(4-hydroxybenzyl)-5-(L-valylamino)phenyl]carbonyl]amino)methyl]phenyl]acetic acid
-
-
35
[2-[([[3-amino-5-(4-hydroxybenzyl)phenyl]carbonyl]amino)methyl]phenyl]acetic acid
-
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
1,10-phenanthroline
Cricetulus griseus
-
IC50: 0.2 mM. Inhibitory effect is substantially potentiated by both EDTA and EGTA. A combined and complete inhibition of the enzyme activity by 0.1 mM EDTA and 0.1 mM 1,10-phenanthroline can be prevented in the presence of 0.04-0.1 mM ZnCl2
0.022
1-methyl-N-[3-(1H-tetrazol-5-yl)phenyl]-1H-indole-6-sulfonamide
Cricetulus griseus
-
pH 7.4, temperature not specified in the publication
0.0029
2,4,5-trichloro-N-[3-(1H-tetrazol-5-yl)phenyl]benzenesulfonamide
Cricetulus griseus
-
pH 7.4, temperature not specified in the publication
0.0011
3,4-dichloro-N-[3-(1H-tetrazol-5-yl)phenyl]benzenesulfonamide
Cricetulus griseus
-
pH 7.4, temperature not specified in the publication
0.0031
3,4-dimethyl-N-[3-(1H-tetrazol-5-yl)phenyl]benzenesulfonamide
Cricetulus griseus
-
pH 7.4, temperature not specified in the publication
0.125
3-([(4-bromo-5-chlorothiophen-2-yl)sulfonyl]amino)-N-methylbenzamide
Cricetulus griseus
-
pH 7.4, temperature not specified in the publication
0.0018
4,5-dichloro-N-[3-(1H-tetrazol-5-yl)phenyl]thiophene-2-sulfonamide
Cricetulus griseus
-
pH 7.4, temperature not specified in the publication
0.034
4-amino-3-(L-arginylamino)benzoic acid
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.01
4-amino-3-(L-tyrosylamino)benzoic acid
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.01
4-amino-3-[(O-benzyl-L-tyrosyl)amino]benzoic acid
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0079
4-bromo-2,6-difluoro-N-[3-(1H-tetrazol-5-yl)phenyl]benzenesulfonamide
Cricetulus griseus
-
pH 7.4, temperature not specified in the publication
0.0016
4-bromo-2-fluoro-N-[3-(1H-tetrazol-5-yl)phenyl]benzenesulfonamide
Cricetulus griseus
-
pH 7.4, temperature not specified in the publication
0.058
4-bromo-5-chloro-N-methyl-N-[3-(1H-tetrazol-5-yl)phenyl]thiophene-2-sulfonamide
Cricetulus griseus
-
pH 7.4, temperature not specified in the publication
0.125
4-bromo-5-chloro-N-[3-(1-methyl-1H-tetrazol-5-yl)phenyl]thiophene-2-sulfonamide
Cricetulus griseus
-
pH 7.4, temperature not specified in the publication
0.067
4-bromo-5-chloro-N-[3-(1H-tetrazol-5-yl)phenyl]thiophene-2-carboxamide
Cricetulus griseus
-
pH 7.4, temperature not specified in the publication
0.0021
4-bromo-5-chloro-N-[3-(1H-tetrazol-5-yl)phenyl]thiophene-2-sulfonamide
Cricetulus griseus
-
pH 7.4, temperature not specified in the publication
0.0013
7-chloro-N-[3-(1H-tetrazol-5-yl)phenyl]-1,3-dihydro-2,1,3-benzoxadiazole-4-sulfonamide
Cricetulus griseus
-
pH 7.4, temperature not specified in the publication
0.0024
benzyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tryptophanate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.014
benzyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-valinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0013
benzyl N-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tryptophanate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0037
benzyl N-[3-amino-4-(L-leucylamino)benzoyl]-L-tryptophanate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.000438
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophanate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0039
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-valinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0034
benzyl N-[3-amino-4-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoyl]-L-tryptophanate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0038
benzyl N-[3-amino-4-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tryptophanate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.001
benzyl N-[4-amino-3-(D-norleucylamino)benzoyl]-L-valinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.000105
benzyl N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophanate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0071
benzyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophanate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.012
benzyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-valinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.000933
benzyl N-[4-amino-3-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tryptophanate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0396
methyl 3-amino-4-(L-arginylamino)benzoate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0033
methyl 3-amino-4-(L-norleucylamino)benzoate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0083
methyl 3-amino-4-(L-tyrosylamino)benzoate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0017
methyl 3-amino-4-[(O-benzyl-L-tyrosyl)amino]benzoate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.031
methyl 3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.014
methyl 4-amino-3-(L-arginylamino)benzoate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0072
methyl 4-amino-3-(L-norleucylamino)benzoate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.057
methyl 4-amino-3-(L-tyrosylamino)benzoate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0021
methyl 4-amino-3-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.01
methyl 4-amino-3-[(O-benzyl-L-tyrosyl)amino]benzoate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.012
methyl 4-amino-3-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0013
methyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0036
methyl N-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0022
methyl N-[3-amino-4-(L-arginylamino)benzoyl]-L-tyrosinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0036
methyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tyrosinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0037
methyl N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tyrosinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0029
methyl N-[3-amino-4-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tyrosinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0012
methyl N-[4-amino-3-(D-norleucylamino)benzoyl]-D-tyrosinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.000966
methyl N-[4-amino-3-(L-arginylamino)benzoyl]-D-tyrosinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.1
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-threoninate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.022
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tyrosinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0025
methyl N2-(3,4-diaminobenzoyl)-L-argininate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.1
methyl N2-(3,4-diaminobenzoyl)-L-lysinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0047
methyl N2-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-argininate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.02
methyl N2-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-lysinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0107
methyl N2-(4-amino-3-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-lysinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.01
methyl N2-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-lysinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0049
methyl N2-[3-amino-4-(L-arginylamino)benzoyl]-L-lysinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.1
methyl N2-[3-amino-4-(L-leucylamino)benzoyl]-L-lysinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0357
methyl N2-[3-amino-4-(L-norleucylamino)benzoyl]-L-lysinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.07
methyl N2-[3-amino-4-(L-tyrosylamino)benzoyl]-L-lysinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.031
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-D-argininate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.1
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-L-lysinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0057
methyl N2-[4-amino-3-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoyl]-L-lysinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.1
N-(3,4-diaminobenzoyl)-L-tryptophan
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0052
N-(3-amino-4-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.02
N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-valine
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0044
N-(4-amino-3-[[(2R)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.016
N-[3-(1H-tetrazol-5-yl)phenyl]-1-benzothiophene-2-sulfonamide
Cricetulus griseus
-
pH 7.4, temperature not specified in the publication
0.039
N-[3-(1H-tetrazol-5-yl)phenyl]-2-benzothiophene-4-sulfonamide
Cricetulus griseus
-
pH 7.4, temperature not specified in the publication
0.125
N-[3-(1H-tetrazol-5-yl)phenyl]benzenesulfonamide
Cricetulus griseus
-
pH 7.4, temperature not specified in the publication
0.044
N-[3-(1H-tetrazol-5-yl)phenyl]biphenyl-4-sulfonamide
Cricetulus griseus
-
pH 7.4, temperature not specified in the publication
0.125
N-[3-(1H-tetrazol-5-yl)phenyl]pyridine-3-sulfonamide
Cricetulus griseus
-
pH 7.4, temperature not specified in the publication
0.125
N-[3-(1H-tetrazol-5-yl)phenyl]thiophene-2-sulfonamide
Cricetulus griseus
-
pH 7.4, temperature not specified in the publication
0.0076
N-[3-amino-4-(L-arginylamino)benzoyl]-L-tryptophan
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0017
N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophan
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.1
N-[3-amino-4-(L-norleucylamino)benzoyl]-L-valine
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0013
N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tryptophan
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.1
N-[4-amino-3-(D-norleucylamino)benzoyl]-L-valine
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.000655
N-[4-amino-3-(L-arginylamino)benzoyl]-L-tryptophan
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0033
N-[4-amino-3-(L-arginylamino)benzoyl]-L-valine
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.000296
N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophan
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.1
N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophan
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.1
N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-valine
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.1
N2-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-ornithine
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0041
N2-[4-amino-3-(L-leucylamino)benzoyl]-L-lysine
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0038
N2-[4-amino-3-(L-phenylalanylamino)benzoyl]-L-lysine
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0048
N2-[4-amino-3-(L-tyrosylamino)benzoyl]-L-lysine
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.0099
methyl N-(3,4-diaminobenzoyl)-L-tyrosinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
0.022
methyl N-(3,4-diaminobenzoyl)-L-tyrosinate
Homo sapiens
Q9UIQ6
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8
-
pH 7.0: about 15% of activity maximum, pH 8.0: about 10% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
35899, 35900, 35903, 35904, 35905, 35906, 35907, 35908, 35911, 35919, 651074, 651116, 664275, 667810, 667811, 667887, 667888, 668752, 668753, 668760, 670127, 670450, 670742, 670859, 683204, 683302, 683431, 683795, 683806, 684051, 696727, 699736, 732310
-
-
brenda
-
-
-
brenda
Otsuka Long Evans Tokushima Fatty rats, model of type II Diabetes mellitus
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
trophoblastic cell. Insulin induces enzyme expression in trophoblasts
brenda
-
P-LAP is detected in all clear-cell adenocarcinomas
brenda
-
P-LAP is detected in 15 of 17 endometrioid adenocarcinomas
brenda
-
high activity in the inner mucosal lining of the ampulla segment of the Fallopian tube, lower level in the interstitial and isthmus
brenda
-
highest concentration in the outer myometrial layer of the uterus, lower levels in the inner myometrial layer and in the luminal epithelium
brenda
-
enzyme in soluble fraction, no activity detected in particulate fraction
brenda
-
P-LAP is located in the periphery in early gestation, located in both the periphery and inner cells during mid-gestation, located only in inner cells in late gestation
brenda
-
P-LAP is detected in 13 of 14 mucinous adenocarcinomas
brenda
-
P-LAP is detected in 7 of 14 borderline tumors
brenda
-
expression of the enzyme is increased during the differentiation of the cells into neuronal cells
brenda
-
cystinyl aminopeptidase is 100% higher in the left than in the right prefrontal cortex
brenda
-
tendency towards increased P-LAP expression with advancing grade is observed in serous adenocarcinomas
brenda
additional information
-
no activity in soluble and particulate fraction of midbrain and hypophysis
brenda
-
low activity, enzyme in soluble fraction, no activity detected in particulate fraction
brenda
-
during normal pregnancy, enzyme activity in maternal serum gradually increases to the maximum at near term
brenda
-
type III integral membrane protein, converted to a soluble form existing in maternal serum by metalloproteases
brenda
-
activity is greatly increased in rats with mammary tumors. The activity may be involved in the promotion and progression of breast cancer through oxytocin, vasopressin and/or renin-angiotensin system misregulation
brenda
-
highly expressed in selected olfactory regions, in septal and hypothalamic nuclei, throughout the hippocampal formation and cerebral cortex, and in motor and motor associated nuclei. IRAP is expressed exclusively in neurons in these regions
brenda
-
the enzyme is suggested to be involved in reducing chemosensitivity and may be a therapeutic target in endometrial carcinoma
brenda
-
P-LAP is an independent prognosticator of clinical outcome in patients with endometrial carcinoma. Assessment of the P-LAP status provides clinically useful prognostic information in patients with endometrial carcinoma
brenda
-
immunodetection of enzyme with large 100-200 nm vesicles in hippocampal neurons
brenda
-
cystinyl aminopeptidase is 300% higher in the left than in the right hippocampus
brenda
-
colocalization with the potential in vivo substrates, oxytocin and vasopression
brenda
-
located in distal and collecting tubules but not in proximal tubules
brenda
-
treatment with cyclosporin increases the activity of cystyl aminopeptidase as well as neutral, basic, prolyl imino and pyroglutamyl soluble aminopeptidase in the renal cortex
brenda
-
low activity, enzyme in soluble fraction, no activity detected in particulate fraction
brenda
-
among hematopoietic cells in fetal liver only megakaryocytes show strong expression of P-LAP
brenda
-
enzyme in soluble fraction, no activity detected in particulate fraction
brenda
expressed in magnocellular neurones of the supraoptic (SON) and paraventricular (PVN) nuclei
brenda
-
high activity level in corpus albicans, lower activity throughout the ovarian cortex and the surrounding connective tissue
brenda
-
enzyme in soluble fraction, no activity detected in particulate fraction
brenda
-
the enzyme is predominantly expressed in differentiated trophoblasts
brenda
-
predominantly expressed in differentiated trophoblasts, syncytiotrophoblasts
brenda
-
expressed in differentiated trophoblasts; in the placenta the enzyme is thought to play a role in the prevention of premature labour and maintenance of an adequate blood flow to the uterus
brenda
-
blocking of alpha-1adrenoceptor by doxazosin increases enzyme activity in male, but not in female
brenda
-
highest concentration in the outer myometrial layer of the uterus, lower levels in the inner myometrial layer and in the luminal epithelium
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme translocates to the cell surface within GLUT4 vesicles in response to insulin
brenda
-
P-LAP is translocated from the cytosol to the plasma membrane by oxytocin stimulation in vascular endothelial cells and by vasopressin in renal cells
brenda
-
insulin-stimulated translocation of IRAP remains intact despite substantial knock-down of glucose transporter GLUT4. By contrast, insulin-stimulated GLUT4 translocation is impaired upon IRAP knock-down. Tankyrase knock-down alters the basal partitioning of GLUT4 and IRAP within endosomal compartments
brenda
-
defects in the intracellular trafficking of P-LAP/IRAP-containing GLUT4 vesicle are associated with type 2 diabetes
-
brenda
-
the enzyme colocalizes with GLUT4 in specific intracellular vesicles
-
brenda
-
insulin-regulated aminopeptidase is a marker protein for specialized vesicles containing the insulin-responsive glucose transporter, GLUT4. The enzyme is thought to be involved in the tethering of GLUT4 vesicles to intracellular compartments
-
brenda
-
comparison of enzyme activity in membranes of COS-7 cells, HEK-293 cells, SK-N-MC cells, CHO-K1 cells and MDBK cells. Comparatively, CHO-K1 cells display the highest level of enzyme. In all cell types, the enzyme predominates over aminopeptidase N
brenda
-
comparison of enzyme activity in membranes of COS-7 cells, HEK-293 cells, SK-N-MC cells, CHO-K1 cells and MDBK cells. Comparatively, CHO-K1 cells display the highest level of enzyme. In all cell types, the enzyme predominates over aminopeptidase N
brenda
-
membrane-bound placental enzyme is released into maternal blood flow via proteolytic cleavage by metalloproteases and metalloproteinases
brenda
-
type III integral membrane protein, converted to a soluble form existing in maternal serum by metalloproteases
brenda
-
the soluble form present in maternal serum is converted from the membrane-bound form in placenta by an enzyme with metalloprotease activity by posttranslational proteolytic cleavage between Phe154 and Ala155. P-LAP is translocated from the cytosol to the plasma membrane by oxytocin stimulation in vascular endothelial cells and by vasopressin in renal cells
brenda
-
comparison of enzyme activity in membranes of COS-7 cells, HEK-293 cells, SK-N-MC cells, CHO-K1 cells and MDBK cells. Comparatively, CHO-K1 cells display the highest level of enzyme. In all cell types, the enzyme predominates over aminopeptidase N
brenda
-
after exposure of 3T3-L1 adipocytes to insulin, IRAP translocates to the plasma membrane
brenda
-
comparison of enzyme activity in membranes of COS-7 cells, HEK-293 cells, SK-N-MC cells, CHO-K1 cells and MDBK cells. Comparatively, CHO-K1 cells display the highest level of enzyme. In all cell types, the enzyme predominates over aminopeptidase N
brenda
-
enzyme is enriched in low density microsome, and exhibits lower levels in high density microsomes. Co-localization with the vesicular marker VAMP2
-
brenda
-
enzyme is enriched in low density microsome, and exhibits lower levels in high density microsomes. Co-localization with the vesicular marker VAMP2
-
brenda
-
insulin induces a translocation of the enzyme from GLUT4 vesicles to plasma membrane by increasing the recycling rate
brenda
-
translocated with GLUT4 to the plasma membrane unedr insulin stimulation
brenda
-
the soluble form present in maternal serum is converted from the membrane-bound form in placenta by an enzyme with metalloprotease activity
-
brenda
-
IRAP vesicles represent a IgE-sensitive exocytotic compartment in mast cells, which is regulated differently from secretory granules
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
inhibition of central enzyme activity by injection of amastatin in anaesthetised suckling mothers increases the frequency of reflex milk ejections
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000
280000
300000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
-
the soluble form present in maternal serum is converted from the membrane-bound form in placenta by an enzyme with metalloprotease activity by posttranslational proteolytic cleavage between Phe154 and Ala155
side-chain modification
side-chain modification
-
44% carbohydrate; enzyme molecule contains about 40 sialic acid residues
side-chain modification
-
sialic acid not necessary for enzymatic activity, essential to conformation
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A429G
G428A
-
the ratio of maximal velocity to Km-value is 90% of the value for the wild-type enzyme
G428D
-
80% of wild-type activity with L-Arg-vasopressin, no activity with L-Leu-enkephalin
G428E
-
50% of wild-type activity with L-Arg-vasopressin, no activity with L-Leu-enkephalin
G428Q
-
more than wild-type activity with L-Arg-vasopressin, less than 10% of wild-type activity with L-Leu-enkephalin
M430I
-
the ratio of maximal velocity to Km-value is 6.2% of the value for the wild-type enzyme
M430K
-
the ratio of maximal velocity to Km-value is 3.3% of the value for the wild-type enzyme
L76A/L77A
-
mutation results in rapid default of the enzyme to the cell surface. In presence of a dominant interfering mutant of clathrin adaptor GGA1, insulin-stimulated translocation of wild-type enzyme, but not of mutant L76A/L77A is inhibited
additional information
A429G
-
the ratio of maximal velocity to Km-value is 75% of the value for the wild-type enzyme
additional information
-
endometrial adenocarcinoma A-MEC cells expressing the enzyme exhibit a significant growth-stimulatory effect compared with control. They have a remarkably high level of p85PI3K protein and show a higher degree of AKT phosphorylation by insulin stimulation
additional information
-
adipocytes and skeletal muscle cells of IRAP-/- mice do not process vasopressin and oxytocin from their N-terminus. In IRAP-/- mice, plasma vasopressin level is elevated twofold and vasopressin levels in mutant mice brains show a compensatory decrease
additional information
-
alanine-substitution of 9 residues amino- or carboxy-terminal to the dileucine motif at positions 76, 77 does not perturb basal intracellular sequestration of the enzyme
additional information
-
IRAP knockout mice with an accelerated, age-realted decline in spatial memory
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, 0.01 M potassium phosphate, pH 7.4, protein concentration 0.5 mg/ml, 6 months
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression in HEK-293 cell
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
development of stable second generation inhibitors of IRAP based on the AT4 ligands angiotensin IV or LVV-H7 may provide the opportunity for the development of therapeutics for memory loss in patients Altheimer's disease
medicine
-
the enzyme is suggested to be involved in reducing chemosensitivity and may be a therapeutic target in endometrial carcinoma
medicine
-
P-LAP is available for evaluation of avarian epithelial malignancy and also as target for molecular therapy
medicine
-
P-LAP is an independent prognosticator of clinical outcome in patients with endometrial carcinoma. Assessment of the P-LAP status provides clinically useful prognostic information in patients with endometrial carcinoma
medicine
-
plasma activities of cystinyl-, aspartyl-, and glutamyl-aminopeptidase are decreased by 39.4%, 24.9%, and 33.3%, respectively, in patients with Parkinson's disease
medicine
-
activities of soluble cystyl aminopeptidase do not differ between diabetic and control rats in both hippocampus and hypothalamus. Membrane-bound cystyl aminopeptidase is about 2.5foldincreased in the hypothalamus and 5fold increased in the hippocampus
medicine
-
enzyme isoform IRAP is involved in increasing malignant potential of endometrial cancer mediated by insulin. Endometrial adenocarcinoma A-MEC cells expressing the enzyme exhibit a significant growth-stimulatory effect compared with control. They have a remarkably high level of p85PI3K protein and show a higher degree of AKT phosphorylation by insulin stimulation
medicine
-
blocking of alpha-1adrenoceptor by doxazosin increases enzyme activity in male, but not in female thalamus. Increased capacity of males to degrade vasopressin and to regulate cardiovascular homeostasis
medicine
-
Otsuka Long Evans Tokushima Fatty rats, model of type II Diabetes mellitus, show significantly lower cell surface IRAP equilibrium activity than control. Time to reach equilibrium is significantly longer and adipocytes isolated from the model rats demonstrate both a delay and a reduction in 3-O-methyl-D-glucose uptake
medicin