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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
-
-
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
-
-
-
?
arginine vasopressin + H2O
?
-
-
-
-
?
Cys-4-nitroanilide + H2O
Cys + 4-nitroaniline
L-Ala-2-naphthylamide + H2O
L-Ala + 2-naphthylamine
-
-
-
-
?
L-alanine-p-nitroanilide + H2O
L-alanine + p-nitroaniline
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
-
-
-
?
L-Arg-vasopressin + H2O
L-Arg + vasopressin
-
-
-
-
?
L-arginine-7-amido-4-methylcoumarin + H2O
L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
L-benzyl-L-Cys-2-naphthylamide + H2O
L-benzyl-L-Cys + 2-naphthylamine
-
-
-
-
?
L-benzyl-L-cysteine-p-nitroanilide + H2O
L-benzyl-L-cysteine + p-nitroaniline
-
-
-
-
?
L-Cys-beta-naphthylamide + H2O
L-Cys + beta-naphthylamine
L-cystine di-beta-naphthylamide + H2O
?
L-cystine-di-beta-naphthylamide + 2 H2O
L-cystine + 2 beta-naphthylamine
L-cystine-di-p-nitroanilide + H2O
L-cystine + p-nitroaniline
L-Leu-2-naphthylamide + H2O
2-naphthylamine + L-Leu
-
-
-
-
?
L-Leu-2-naphthylamide + H2O
L-Leu + 2-naphthylamine
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
L-Leu-enkephalin + H2O
L-Leu + enkephalin
-
-
-
-
?
L-Leu-p-nitroanilide + H2O
L-Leu + p-nitroaniline
-
-
-
-
?
L-leucine-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
?
L-leucine-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
-
-
-
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
-
-
-
-
?
L-lysine-p-nitroanilide + H2O
L-lysine + p-nitroaniline
L-methionine-p-nitroanilide + H2O
L-methionine + p-nitroaniline
-
-
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Trp-2-naphthylamide + H2O
L-Trp + 2-naphthylamine
-
-
-
-
?
Leu-4-methylcoumaryl-7-amide + H2O
Leu + 7-amino-4-methylcoumarin
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
leucyl-beta-naphthylamide + H2O
leucine + beta-naphthylamine
-
-
-
?
LGGGGGL + H2O
L-Leu + GGGGGL
hydrolysis of poly-glycine peptides, overview
-
-
?
Lys-4-methylcoumaryl-7-amide + H2O
Lys + 7-amino-4-methylcoumarin
-
-
-
?
lysine-vasopressin + H2O
?
-
-
-
-
?
Met-4-methylcoumaryl-7-amide + H2O
Met + 7-amino-4-methylcoumarin
-
-
-
?
oxytocin + H2O
acyclic peptide + H2O
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
-
-
-
-
?
S-benzyl-L-cysteine-p-nitroanilide + H2O
S-benzyl-L-cysteine + p-nitroaniline
somatostatin + H2O
?
-
-
-
-
?
vasopressin + H2O
hydrolyzed vasopressin
additional information
?
-
angiotensin III + H2O
?
-
-
-
-
?
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
-
-
?
Cys-4-nitroanilide + H2O
Cys + 4-nitroaniline
-
-
-
?
Cys-4-nitroanilide + H2O
Cys + 4-nitroaniline
-
-
-
-
?
L-alanine-p-nitroanilide + H2O
L-alanine + p-nitroaniline
-
-
-
-
?
L-alanine-p-nitroanilide + H2O
L-alanine + p-nitroaniline
-
-
-
-
?
L-Cys-beta-naphthylamide + H2O
L-Cys + beta-naphthylamine
-
-
-
?
L-Cys-beta-naphthylamide + H2O
L-Cys + beta-naphthylamine
-
-
-
?
L-cystine di-beta-naphthylamide + H2O
?
-
-
-
-
?
L-cystine di-beta-naphthylamide + H2O
?
-
-
-
-
?
L-cystine-di-beta-naphthylamide + 2 H2O
L-cystine + 2 beta-naphthylamine
-
-
-
?
L-cystine-di-beta-naphthylamide + 2 H2O
L-cystine + 2 beta-naphthylamine
in the presence of thiol, the substrate is converted to L-cystine beta-naphthylamide
-
-
?
L-cystine-di-beta-naphthylamide + 2 H2O
L-cystine + 2 beta-naphthylamine
in the presence of thiol, the substrate is converted to L-cystine beta-naphthylamide
-
-
?
L-cystine-di-beta-naphthylamide + 2 H2O
L-cystine + 2 beta-naphthylamine
-
-
-
?
L-cystine-di-p-nitroanilide + H2O
L-cystine + p-nitroaniline
-
-
-
-
?
L-cystine-di-p-nitroanilide + H2O
L-cystine + p-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-lysine-p-nitroanilide + H2O
L-lysine + p-nitroaniline
-
-
-
-
?
L-lysine-p-nitroanilide + H2O
L-lysine + p-nitroaniline
-
-
-
-
?
L-lysine-p-nitroanilide + H2O
L-lysine + p-nitroaniline
-
-
-
-
?
L-lysine-p-nitroanilide + H2O
L-lysine + p-nitroaniline
-
-
-
-
?
Leu-4-methylcoumaryl-7-amide + H2O
Leu + 7-amino-4-methylcoumarin
-
-
-
?
Leu-4-methylcoumaryl-7-amide + H2O
Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
oxytocin + H2O
?
-
-
-
-
?
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
?
-
enzyme opens the N-terminal cystine loop of oxytocin
-
-
?
oxytocin + H2O
?
a macrocyclic IRAP substrate
-
-
?
oxytocin + H2O
?
-
-
N-terminal processing
-
?
oxytocin + H2O
acyclic peptide + H2O
-
-
-
-
?
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
-
-
?
oxytocin + H2O
acyclic peptide + H2O
-
-
-
-
?
oxytocin + H2O
acyclic peptide + H2O
-
-
-
-
?
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
?
-
-
-
-
?
Vasopressin + H2O
?
-
-
-
?
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
?
a macrocyclic IRAP substrate
-
-
?
Vasopressin + H2O
?
-
-
-
?
Vasopressin + H2O
?
inactivation of vasopressin
-
-
?
Vasopressin + H2O
?
-
-
-
?
Vasopressin + H2O
?
inactivation of vasopressin
-
-
?
Vasopressin + H2O
?
-
-
-
?
Vasopressin + H2O
?
-
-
-
?
vasopressin + H2O
hydrolyzed vasopressin
-
-
-
-
?
vasopressin + H2O
hydrolyzed vasopressin
-
vasopressin is a physiological substrate
N-terminal processing
-
?
vasopressin + H2O
hydrolyzed vasopressin
-
-
-
-
?
additional information
?
-
-
broad specificity
-
-
?
additional information
?
-
-
broad specificity
-
-
?
additional information
?
-
-
broad specificity
-
-
?
additional information
?
-
-
S-benzyl-Cys-Pro-Leu-Gly(NH2)
-
-
?
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
?
-
-
glycyl-p-nitroanilide
-
-
?
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
?
-
no activity with 1-deamino-8-D-arginine vasopressin
-
-
?
additional information
?
-
-
no activity with 1-deamino-8-D-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
?
-
recombinant IRAP bound to TUG, and this interaction is mapped to a short peptide in IRAP which is critical for GLUT4 intracellular retention. TUG controls vesicle translocation by interacting with IRAP as well as GLUT4
-
-
?
additional information
?
-
-
recombinant IRAP bound to TUG, and this interaction is mapped to a short peptide in IRAP which is critical for GLUT4 intracellular retention. TUG controls vesicle translocation by interacting with IRAP as well as GLUT4
-
-
?
additional information
?
-
recombinant IRAP bound to TUG, and this interaction is mapped to a short peptide in IRAP which is critical for GLUT4 intracellular retention. TUG controls vesicle translocation by interacting with IRAP as well as GLUT4
-
-
?
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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(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
-
-
1,16-bis(4-methyl-2,5-dioxo-3-furyl)hexadecane
-
tyromycin A
1,2-Acyclic oxytocin
-
slight inhibition of oxytocin degradation, marked inhibition of cystine di-beta-naphthylamide degradation
1-methyl-N-[3-(1H-tetrazol-5-yl)phenyl]-1H-indole-6-sulfonamide
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
2,4,5-trichloro-N-[3-(1H-tetrazol-5-yl)phenyl]benzene-1-sulfonamide
-
2,4,5-trichloro-N-[3-(1H-tetrazol-5-yl)phenyl]benzenesulfonamide
-
-
2-amino-4-(3,4-dimethoxyphenyl)-7-hydroxy-4H-chromene-3-carbonitrile
-
-
2-amino-4-(3,5-dimethoxyphenyl)-7-hydroxy-4H-chromene-3-carbonitrile
-
-
2-amino-4-[4-(dimethylamino)phenyl]-7-hydroxy-4H-chromene-3-carbonitrile
-
-
2-amino-7-hydroxy-4-(3,4,5-trimethoxyphenyl)-4H-chromene-3-carbonitrile
-
-
2-amino-7-hydroxy-4-(3-methoxyphenyl)-4H-chromene-3-carbonitrile
-
-
2-amino-7-hydroxy-4-(4-methoxyphenyl)-4H-chromene-3-carbonitrile
-
-
2-amino-7-hydroxy-4-(pyridin-4-yl)-4H-chromene-3-carbonitrile
-
-
2-methoxyethyl 2-amino-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
-
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
-
-
3,4-dichloro-N-[3-(1H-tetrazol-5-yl)phenyl]benzene-1-sulfonamide
-
3,4-dichloro-N-[3-(1H-tetrazol-5-yl)phenyl]benzenesulfonamide
-
-
3,4-dimethyl-N-[3-(1H-tetrazol-5-yl)phenyl]benzene-1-sulfonamide
-
3,4-dimethyl-N-[3-(1H-tetrazol-5-yl)phenyl]benzenesulfonamide
-
-
3-([(4-bromo-5-chlorothiophen-2-yl)sulfonyl]amino)-N-methylbenzamide
-
-
3-[(4-bromo-5-chlorothiophene-2-sulfonyl)amino]-N-methylbenzamide
-
4,5-dichloro-N-[3-(1H-tetrazol-5-yl)phenyl]thiophene-2-sulfinamide
-
4,5-dichloro-N-[3-(1H-tetrazol-5-yl)phenyl]thiophene-2-sulfonamide
4-amino-3-(L-arginylamino)benzoic acid
-
4-amino-3-(L-tyrosylamino)benzoic acid
-
4-amino-3-[(O-benzyl-L-tyrosyl)amino]benzoic acid
-
4-bromo-2,6-difluoro-N-[3-(1H-tetrazol-5-yl)phenyl]benzene-1-sulfonamide
-
4-bromo-2,6-difluoro-N-[3-(1H-tetrazol-5-yl)phenyl]benzenesulfonamide
-
-
4-bromo-2-fluoro-N-[3-(1H-tetrazol-5-yl)phenyl]benzene-1-sulfonamide
-
4-bromo-2-fluoro-N-[3-(1H-tetrazol-5-yl)phenyl]benzenesulfonamide
-
-
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
-
-
7-chloro-N-[3-(1H-tetrazol-5-yl)phenyl]-2,1,3-benzoxadiazole-4-sulfonamide
-
amino(phenyl)methyl phosphonic acid
-
benzyl 2-amino-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
-
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-(L-leucylamino)benzoyl]-L-tryptophanate
-
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophanate
-
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-valinate
-
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-(D-norleucylamino)benzoyl]-L-valinate
-
benzyl N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophanate
-
benzyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophanate
-
benzyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-valinate
-
benzyl N-[4-amino-3-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tryptophanate
-
butyl 2-amino-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
-
CuCl2
-
0.1 mM, 91% inhibition. 0.01 mM, 87% inhibition
cyclohexylmethyl 2-amino-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
50% inhibition at 100 microM
diethylenetriamine-N,N,N',N'',N''-pentaacetic acid
-
weak
divalinal-angiotensin IV
-
-
ethyl 2,7-diamino-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
50% inhibition at 100 microM
ethyl 2-(acetylamino)-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
-
ethyl 2-(acetylamino)-7-hydroxy-4-(quinolin-3-yl)-4H-chromene-3-carboxylate
-
-
ethyl 2-acetamido-7-hydroxy-4-(3-quinolinyl)-4H-chromene-3-carboxylate
HFI-437
ethyl 2-amino-4-(2,4-dichloropyridin-3-yl)-7-hydroxy-4H-chromene-3-carboxylate
-
-
ethyl 2-amino-4-(2-cyanophenyl)-7-hydroxy-4H-chromene-3-carboxylate
-
-
ethyl 2-amino-4-(3,4-dimethoxyphenyl)-7-hydroxy-4H-chromene-3-carboxylate
-
-
ethyl 2-amino-4-(3-chlorophenyl)-7-hydroxy-4H-chromene-3-carboxylate
-
-
ethyl 2-amino-4-(3-cyanophenyl)-7-hydroxy-4H-chromene-3-carboxylate
-
-
ethyl 2-amino-4-(4-bromophenyl)-7-hydroxy-4H-chromene-3-carboxylate
-
-
ethyl 2-amino-4-(4-chlorophenyl)-7-hydroxy-4H-chromene-3-carboxylate
-
-
ethyl 2-amino-4-(4-cyanophenyl)-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-(pyridin-3-yl)-4H-benzo[g]chromene-3-carboxylate
-
-
ethyl 2-amino-4-(pyridin-3-yl)-4H-benzo[h]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-6-chloro-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
-
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-(2-nitrophenyl)-4H-chromene-3-carboxylate
-
-
ethyl 2-amino-7-hydroxy-4-(4-methylphenyl)-4H-chromene-3-carboxylate
-
-
ethyl 2-amino-7-hydroxy-4-(4-nitrophenyl)-4H-chromene-3-carboxylate
-
-
ethyl 2-amino-7-hydroxy-4-(pyridin-2-yl)-4H-chromene-3-carboxylate
-
-
ethyl 2-amino-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
-
ethyl 2-amino-7-hydroxy-4-(pyridin-4-yl)-4H-chromene-3-carboxylate
-
-
ethyl 2-amino-7-hydroxy-4-(quinolin-3-yl)-4H-chromene-3-carboxylate
-
-
ethyl 2-amino-7-hydroxy-4-(quinolin-4-yl)-4H-chromene-3-carboxylate
-
-
ethyl 2-amino-7-hydroxy-4-(thiophen-2-yl)-4H-chromene-3-carboxylate
-
50% inhibition at 100 microM
ethyl 2-amino-7-hydroxy-4-phenyl-4H-chromene-3-carboxylate
-
-
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
ethyl 2-amino-8-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
-
HA-08
a macrocyclic IRAP inhibitor
L-Arg-vasopressin
-
Ki-value for wild-type, mutants G428E, G428D, G428Q above 0.03 mM
L-methionine
-
form I inhibited, form II slightly activated
L-trans-epoxysuccinyl-leucinamido(4-guanidino)-butane
-
E64
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
L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-cyclohexylalanine
-
-
L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe
Leu-Val-Val-haemorphin 7
-
-
leupeptin
-
0.1 mM, 53% inhibition
LVV hemorphin 7
LVV-H7, IRAP ligands are on the one hand competitive inhibitors of the enzymatic activity of IRAP and on the other hand regulators of its trafficking
methyl 2-amino-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
-
methyl 3-amino-4-(L-arginylamino)benzoate
-
methyl 3-amino-4-(L-norleucylamino)benzoate
-
methyl 3-amino-4-(L-tyrosylamino)benzoate
-
methyl 3-amino-4-[(O-benzyl-L-tyrosyl)amino]benzoate
-
methyl 3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoate
-
methyl 4-amino-3-(L-arginylamino)benzoate
-
methyl 4-amino-3-(L-norleucylamino)benzoate
-
methyl 4-amino-3-(L-tyrosylamino)benzoate
-
methyl 4-amino-3-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoate
-
methyl 4-amino-3-[(O-benzyl-L-tyrosyl)amino]benzoate
-
methyl 4-amino-3-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoate
-
methyl N-(3,4-diaminobenzoyl)-L-tyrosinate
-
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 N-[3-amino-4-(L-arginylamino)benzoyl]-L-tyrosinate
-
methyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tyrosinate
-
methyl N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tyrosinate
-
methyl N-[3-amino-4-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tyrosinate
-
methyl N-[4-amino-3-(D-norleucylamino)benzoyl]-D-tyrosinate
-
methyl N-[4-amino-3-(L-arginylamino)benzoyl]-D-tyrosinate
-
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-threoninate
-
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tyrosinate
-
methyl N2-(3,4-diaminobenzoyl)-L-argininate
-
methyl N2-(3,4-diaminobenzoyl)-L-lysinate
-
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-[3-amino-4-(L-arginylamino)benzoyl]-L-lysinate
-
methyl N2-[3-amino-4-(L-leucylamino)benzoyl]-L-lysinate
-
methyl N2-[3-amino-4-(L-norleucylamino)benzoyl]-L-lysinate
-
methyl N2-[3-amino-4-(L-tyrosylamino)benzoyl]-L-lysinate
-
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-D-argininate
-
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-L-lysinate
-
methyl N2-[4-amino-3-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoyl]-L-lysinate
-
N-(3,4-diaminobenzoyl)-L-tryptophan
-
N-(3-(1H-tetrazol-5-yl)phenyl)-2,3,4-trichlorobenzenesulfonamide
-
N-(3-(1H-tetrazol-5-yl)phenyl)-2,5-bis(trifluoromethyl)-benzenesulfonamide
-
N-(3-(1H-tetrazol-5-yl)phenyl)-2-fluoro-5-(trifluoromethyl)benzenesulfonamide
-
N-(3-(1H-tetrazol-5-yl)phenyl)-3,4-difluorobenzenesulfonamide
-
N-(3-(1H-tetrazol-5-yl)phenyl)-3,5-bis(trifluoromethyl)-benzenesulfonamide
-
N-(3-(1H-tetrazol-5-yl)phenyl)-3-fluoro-4-(trifluoromethyl)benzenesulfonamide
-
N-(3-(1H-tetrazol-5-yl)phenyl)-3-methyl-4-(trifluoromethyl)benzenesulfonamide
-
N-(3-(1H-tetrazol-5-yl)phenyl)-4-methyl-3-(trifluoromethyl)benzenesulfonamide
-
N-(3-amino-4-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
-
N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-valine
-
N-(4-amino-3-[[(2R)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
-
N-alpha-tosyl-L-lysylchloromethane
-
-
N-hexanoyl-L-Tyr-L-Ile
a dipeptide derivative from Ang IV, a strong cognitive enhancer and enzyme inhibitor
N-[3-(1H-tetrazol-5-yl)phenyl]-1-benzothiophene-2-sulfonamide
N-[3-(1H-tetrazol-5-yl)phenyl]-2-benzothiophene-1-sulfonamide
-
N-[3-(1H-tetrazol-5-yl)phenyl]-2-benzothiophene-4-sulfonamide
-
-
N-[3-(1H-tetrazol-5-yl)phenyl]benzenesulfonamide
N-[3-(1H-tetrazol-5-yl)phenyl]biphenyl-4-sulfonamide
-
-
N-[3-(1H-tetrazol-5-yl)phenyl]pyridine-3-sulfonamide
N-[3-(1H-tetrazol-5-yl)phenyl]thiophene-2-sulfonamide
N-[3-(1H-tetrazol-5-yl)phenyl][1,1'-biphenyl]-4-sulfonamide
-
N-[3-amino-4-(L-arginylamino)benzoyl]-L-tryptophan
-
N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophan
-
N-[3-amino-4-(L-norleucylamino)benzoyl]-L-valine
-
N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tryptophan
-
N-[4-amino-3-(D-norleucylamino)benzoyl]-L-valine
-
N-[4-amino-3-(L-arginylamino)benzoyl]-L-tryptophan
-
N-[4-amino-3-(L-arginylamino)benzoyl]-L-valine
-
N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophan
-
N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophan
-
N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-valine
-
N-[[3-(4-hydroxybenzyl)-5-(L-valylamino)phenyl]carbonyl]-L-isoleucine
-
-
N-[[3-(4-hydroxybenzyl)-5-(L-valylamino)phenyl]carbonyl]-L-isoleucyl-L-histidyl-L-prolyl-L-phenylalanine
-
-
N2-(2- 8[(1-amino-3-phenylpropyl)(hydroxy)phosphoryl]methyl]-4-methylpentanoyl)-L-lysyl-L-histidyl-L-histidyl-L-alanyl-L-phenylalanyl-L-seryl-L-phenylalanyl-L-lysine
i.e. DG025, an antigenic peptide precursor analogue, enzyme binding structure determination and analysis. The canonical orientation of the two N-terminal residues of DG025 is defined by the transition state nature of the ligand and the hydrophobic and aromatic interactions of the hPhe residue in the S1 specificity pocket of the enzyme (and in particular with Phe544). The remaining of the peptide extends toward the base of the cavity, where it is sandwiched between domains II and IV
N2-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-ornithine
-
N2-[4-amino-3-(L-leucylamino)benzoyl]-L-lysine
-
N2-[4-amino-3-(L-phenylalanylamino)benzoyl]-L-lysine
-
N2-[4-amino-3-(L-tyrosylamino)benzoyl]-L-lysine
-
p-hydroxymercuribenzoate
-
-
pepstatin A
-
0.1 mM, 70% inhibition
Polyphloretin phosphate
-
-
propyl 2-amino-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
-
puromycin
-
0.1 mM, 36% inhibition. 0.01 mM, 5% inhibition
S-Benzyl-L-cysteinyl-L-prolyl-L-leucyl-glycinamide
-
-
S-benzylcysteine
-
and S-benzylcysteine containing peptides
tert-butyl 2-amino-7-hydroxy-4-(pyridin-3-yl)-4H-chromene-3-carboxylate
-
-
tosylphenylalanine-chloromethane
-
-
ZnCl2
-
0.1 mM, 98% inhibition. 0.01 mM, 77% inhibition
[(5R)-6-amino-5-benzyl-2-(2,2-diphenylethyl)-3,6-dioxohexyl][(1R)-1-amino-3-phenylpropyl]phosphinic acid
i.e. DG026, a phosphinic pseudotripeptide that acts as very potent inhibitor of IRAP. DG026 is able to selectively downregulate IRAP-dependent cross-presentation by dendritic cells but leave ERAP1-dependent cross-presentation unaffected. Enzyme binding structure determination and analysis, overview
[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
1,10-phenanthroline
-
0.1 mM, 83% inhibition. 0.01 mM, 10% inhibition
1-methyl-N-[3-(1H-tetrazol-5-yl)phenyl]-1H-indole-6-sulfonamide
-
-
1-methyl-N-[3-(1H-tetrazol-5-yl)phenyl]-1H-indole-6-sulfonamide
-
2-mercaptoethanol
-
slight
2-mercaptoethanol
-
inhibition above 1 mM
4,5-dichloro-N-[3-(1H-tetrazol-5-yl)phenyl]thiophene-2-sulfonamide
-
-
4,5-dichloro-N-[3-(1H-tetrazol-5-yl)phenyl]thiophene-2-sulfonamide
-
4-bromo-5-chloro-N-methyl-N-[3-(1H-tetrazol-5-yl)phenyl]thiophene-2-sulfonamide
-
-
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-(1-methyl-1H-tetrazol-5-yl)phenyl]thiophene-2-sulfonamide
-
4-bromo-5-chloro-N-[3-(1H-tetrazol-5-yl)phenyl]thiophene-2-sulfonamide
-
-
4-bromo-5-chloro-N-[3-(1H-tetrazol-5-yl)phenyl]thiophene-2-sulfonamide
-
amastatin
-
CAP II
amastatin
-
0.1 mM, 96% inhibition. 0.01 mM, 79% inhibition
angiotensin 4-8
-
-
angiotensin II
-
-
angiotensin III
-
-
angiotensin IV
-
-
angiotensin IV
-
IC50: 0.00072 mM
angiotensin IV
-
competitive
angiotensin IV
-
angiotensin is the hexapeptide Val-Tyr-Ile-His-Pro-Phe
angiotensin IV
Ang IV, a hexapeptide IRAP inhibitor
angiotensin IV
AngIV, induces an increase in the intracellular calcium concentration in pinealocytes by 72% at 10 nM, but AngIV does not alter cAMP levels
angiotensin IV
IRAP ligands are on the one hand competitive inhibitors of the enzymatic activity of IRAP and on the other hand regulators of its trafficking
bestatin
-
-
bestatin
-
0.1 mM, 43% inhibition. 0.01 mM, 12% inhibition
Cd2+
-
-
Co2+
-
reverses EDTA inhibition
Co2+
-
at high concentration inhibition
Co2+
-
reverses EDTA inhibition
Co2+
-
at high concentration inhibition
Co2+
-
at high concentration inhibition
cysteine
-
-
divalinal
-
-
EDTA
-
weak
EDTA
-
form I inhibited, form II uninfluenced or slightly activated
EGTA
-
weak
Hg2+
-
-
iodoacetic acid
-
slightly
L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe
-
i.e.angiotensin IV
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
LVV-H7
-
-
LVV-hemorphin 7
-
-
Mn2+
-
at high concentration inhibition
Mn2+
-
at high concentration inhibition; reverses EDTA inhibition
N-[3-(1H-tetrazol-5-yl)phenyl]-1-benzothiophene-2-sulfonamide
-
-
N-[3-(1H-tetrazol-5-yl)phenyl]-1-benzothiophene-2-sulfonamide
-
N-[3-(1H-tetrazol-5-yl)phenyl]benzenesulfonamide
-
-
N-[3-(1H-tetrazol-5-yl)phenyl]benzenesulfonamide
-
N-[3-(1H-tetrazol-5-yl)phenyl]pyridine-3-sulfonamide
-
-
N-[3-(1H-tetrazol-5-yl)phenyl]pyridine-3-sulfonamide
-
N-[3-(1H-tetrazol-5-yl)phenyl]thiophene-2-sulfonamide
-
-
N-[3-(1H-tetrazol-5-yl)phenyl]thiophene-2-sulfonamide
-
Ni2+
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
Pb2+
-
inhibits at pH 6.0, not at pH 7.4
prostaglandin E-1
-
at pH 6.2, not at pH 6.8 and 7. 4
prostaglandin E-1
-
pH-dependent inhibition
prostaglandin E2
-
at pH 6.2, not at pH 6.8 and 7. 4
prostaglandin E2
-
pH-dependent inhibition
prostaglandin F-2alpha
-
at pH 6.2, not at pH 6.8 and 7. 4
prostaglandin F-2alpha
-
pH-dependent inhibition
prostaglandin F-2alpha
-
-
Zn2+
-
-
Zn2+
-
inhibition at pH 6.0 not at pH 7.5
Zn2+
-
at high concentration
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
-
EDTA has no effect
-
additional information
-
inhibitory potency in decreasing order: angiotensin IV, angiotensin III, divalinal/angiotensin IV, LVV-hemorphin 7, angiotensin 4-8, angiotensin III
-
additional information
inhibition of insulin-regulated aminopeptidase (IRAP) by aryl sulfonamides, structural basis, docking and moelling, molecular dynamics simulations, overview. The fluorinated series exhibit high metabolic stability in microsomes and encompasses compounds with submicromolar affinity. The binding modes are thoroughly examined by molecular dynamics (MD)-related methods for binding affinity estimation for the whole series of aryl sulfonamides
-
additional information
-
inhibition of insulin-regulated aminopeptidase (IRAP) by aryl sulfonamides, structural basis, docking and moelling, molecular dynamics simulations, overview. The fluorinated series exhibit high metabolic stability in microsomes and encompasses compounds with submicromolar affinity. The binding modes are thoroughly examined by molecular dynamics (MD)-related methods for binding affinity estimation for the whole series of aryl sulfonamides
-
additional information
virtual screening from three-dimensional structure models for transition state analogue inhibitors of IRAP based on quantum mechanically derived reaction coordinates, overview. Transition state and high energy intermediate mimetics have the potential to be very potent enzyme inhibitors. Method development and evaluation
-
additional information
enzyme IRAP undergoes a conformational change upon inhibitor binding, docking study. Analysis of structural determinants for inhibitor selectivity, overview. Significant affinity is generated by structural elements common to all homologous enzymes: the active-site Zn(II) atom, the catalytic Tyr549 and Glu465, N-terminus recognition by Glu295, Glu431, and Glu487, and the S1 specificity residue Phe544
-
additional information
-
inhibitory potency in decreasing order: angiotensin IV, angiotensin III, divalinal/angiotensin IV, LVV-hemorphin 7, angiotensin 4-8, angiotensin III
-
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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
pH and temperature not specified in the publication
0.01
4-amino-3-(L-tyrosylamino)benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.01
4-amino-3-[(O-benzyl-L-tyrosyl)amino]benzoic acid
Homo sapiens
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
0.00072
angiotensin IV
Cricetulus griseus
-
IC50: 0.00072 mM
0.0024
benzyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tryptophanate
Homo sapiens
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
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
pH and temperature not specified in the publication
0.0037
benzyl N-[3-amino-4-(L-leucylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.000438
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.0039
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-valinate
Homo sapiens
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
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
pH and temperature not specified in the publication
0.001
benzyl N-[4-amino-3-(D-norleucylamino)benzoyl]-L-valinate
Homo sapiens
pH and temperature not specified in the publication
0.000105
benzyl N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.0071
benzyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.012
benzyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-valinate
Homo sapiens
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
pH and temperature not specified in the publication
0.000218
DG002A
Homo sapiens
pH and temperature not specified in the publication
0.000344
DG002B
Homo sapiens
pH and temperature not specified in the publication
0.00003
DG013A
Homo sapiens
pH and temperature not specified in the publication
0.0022
DG013B
Homo sapiens
pH and temperature not specified in the publication
0.000002
DG023
Homo sapiens
pH and temperature not specified in the publication
0.000032
DG026
Homo sapiens
pH and temperature not specified in the publication
0.0396
methyl 3-amino-4-(L-arginylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.0033
methyl 3-amino-4-(L-norleucylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.0083
methyl 3-amino-4-(L-tyrosylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.0017
methyl 3-amino-4-[(O-benzyl-L-tyrosyl)amino]benzoate
Homo sapiens
pH and temperature not specified in the publication
0.031
methyl 3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoate
Homo sapiens
pH and temperature not specified in the publication
0.014
methyl 4-amino-3-(L-arginylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.0072
methyl 4-amino-3-(L-norleucylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.057
methyl 4-amino-3-(L-tyrosylamino)benzoate
Homo sapiens
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
pH and temperature not specified in the publication
0.01
methyl 4-amino-3-[(O-benzyl-L-tyrosyl)amino]benzoate
Homo sapiens
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
pH and temperature not specified in the publication
0.0099 - 0.022
methyl N-(3,4-diaminobenzoyl)-L-tyrosinate
0.0013
methyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
Homo sapiens
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
pH and temperature not specified in the publication
0.0022
methyl N-[3-amino-4-(L-arginylamino)benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.0036
methyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.0037
methyl N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tyrosinate
Homo sapiens
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
pH and temperature not specified in the publication
0.0012
methyl N-[4-amino-3-(D-norleucylamino)benzoyl]-D-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.000966
methyl N-[4-amino-3-(L-arginylamino)benzoyl]-D-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-threoninate
Homo sapiens
pH and temperature not specified in the publication
0.022
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.0025
methyl N2-(3,4-diaminobenzoyl)-L-argininate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N2-(3,4-diaminobenzoyl)-L-lysinate
Homo sapiens
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
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
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
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
pH and temperature not specified in the publication
0.0049
methyl N2-[3-amino-4-(L-arginylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N2-[3-amino-4-(L-leucylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.0357
methyl N2-[3-amino-4-(L-norleucylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.07
methyl N2-[3-amino-4-(L-tyrosylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.031
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-D-argininate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-L-lysinate
Homo sapiens
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
pH and temperature not specified in the publication
0.1
N-(3,4-diaminobenzoyl)-L-tryptophan
Homo sapiens
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
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
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
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
pH and temperature not specified in the publication
0.0017
N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.1
N-[3-amino-4-(L-norleucylamino)benzoyl]-L-valine
Homo sapiens
pH and temperature not specified in the publication
0.0013
N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.1
N-[4-amino-3-(D-norleucylamino)benzoyl]-L-valine
Homo sapiens
pH and temperature not specified in the publication
0.000655
N-[4-amino-3-(L-arginylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.0033
N-[4-amino-3-(L-arginylamino)benzoyl]-L-valine
Homo sapiens
pH and temperature not specified in the publication
0.000296
N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.1
N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.1
N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-valine
Homo sapiens
pH and temperature not specified in the publication
0.0000077
N2-(2- 8[(1-amino-3-phenylpropyl)(hydroxy)phosphoryl]methyl]-4-methylpentanoyl)-L-lysyl-L-histidyl-L-histidyl-L-alanyl-L-phenylalanyl-L-seryl-L-phenylalanyl-L-lysine
Homo sapiens
pH 7.0, 37°C, recombinant wild-type enzyme
0.1
N2-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-ornithine
Homo sapiens
pH and temperature not specified in the publication
0.0041
N2-[4-amino-3-(L-leucylamino)benzoyl]-L-lysine
Homo sapiens
pH and temperature not specified in the publication
0.0038
N2-[4-amino-3-(L-phenylalanylamino)benzoyl]-L-lysine
Homo sapiens
pH and temperature not specified in the publication
0.0048
N2-[4-amino-3-(L-tyrosylamino)benzoyl]-L-lysine
Homo sapiens
pH and temperature not specified in the publication
0.0099
methyl N-(3,4-diaminobenzoyl)-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.022
methyl N-(3,4-diaminobenzoyl)-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
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evolution
IRAP is a member of the M1 family of zinc-dependent metalloproteinases
evolution
IRAP is a member of the oxytocinase subfamily of M1 aminopeptidases characterised by the presence of two key sequence motifs, the HEXXH zinc-binding and GXMEN substrate recognition sequences
evolution
IRAP is a type-2 membrane glycoprotein from the M1 family of zinc-dependent aminopeptidases
evolution
ovarian tissue LNPEP of Amargosa pupfish, Cyprinodon nevadensis, exhibits high amino acid identity to human LNPEP both in the protein's active domain that includes the peptide binding site and zinc cofactor binding motif (53.1% identity), and in an intracellular region that distinguishes LNPEP from other aminopeptidases (70.3% identity). The pupfish LNPEP-like enzyme also shares a conserved di-leucine amino acid sequence in the N-terminus intracellular region with placental LNPEP
evolution
-
IRAP is a member of the M1 family of zinc-dependent metalloproteinases
-
malfunction
inhibition of central enzyme activity by injection of amastatin in anaesthetised suckling mothers increases the frequency of reflex milk ejections
malfunction
catalytic preference and insulin-regulated traffic of IRAP in adipocytes are disturbed by obesity and are interrelated with comprehensive roles of endogenous substrates with N-terminal cysteine pair in energy metabolism homeostasis
malfunction
diabetes insipidus (DI) is a rare complication of pregnancy occurring in pregnancy, it is associated with excessive vasopressinase activity, secreted by placental trophoblasts, which increases the rate of degradation of anti-diuretic hormone. It is responsive to synthetic desmopressin 1-deamino-8-D-arginine vasopressin as this form is not degraded by placental vasopressinase. Vasopressinase-induced diabetes insipidus is associated with pre-eclampsia
malfunction
in IRAP knockout mice, the half-life of circulating vasopressin is increased 3fold, and plasma concentrations are increased 2fold. Transgenic mice with constitutive TUG proteolysis in muscle consume much more water than wild-type control mice. The transgenic mice lose more body weight during water restriction, and the abundance of renal AQP2 water channels is reduced, implying that vasopressin activity is decreased. To compensate for accelerated vasopressin degradation, vasopressin secretion is increased, as assessed by the cosecreted protein copeptin. IRAP abundance is increased in T-tubule fractions of fasting transgenic mice, when compared with controls
malfunction
peptide inhibitor DG026 is able to selectively downregulate IRAP-dependent cross-presentation by dendritic cells but leave ERAP1-dependent cross-presentation unaffected
malfunction
protein S-acylation (also referred to as palmitoylation) is a post-translational modification (PTM) involving the attachment of palmitate and other fatty acids to cysteine residues of proteins via thioester linkage, no effects of mutating the modified cysteines on the plasma membrane localisation of IRAP in transfected HEK-293T cells are detected
malfunction
-
catalytic preference and insulin-regulated traffic of IRAP in adipocytes are disturbed by obesity and are interrelated with comprehensive roles of endogenous substrates with N-terminal cysteine pair in energy metabolism homeostasis
-
malfunction
-
in IRAP knockout mice, the half-life of circulating vasopressin is increased 3fold, and plasma concentrations are increased 2fold. Transgenic mice with constitutive TUG proteolysis in muscle consume much more water than wild-type control mice. The transgenic mice lose more body weight during water restriction, and the abundance of renal AQP2 water channels is reduced, implying that vasopressin activity is decreased. To compensate for accelerated vasopressin degradation, vasopressin secretion is increased, as assessed by the cosecreted protein copeptin. IRAP abundance is increased in T-tubule fractions of fasting transgenic mice, when compared with controls
-
metabolism
diabetes insipidus can manifest during pregnancy, induced by increased vasopressinase activity secreted by placental trophoblasts and usually manifests in the third trimester
metabolism
insulin stimulates the exocytic translocation of vesicles containing GLUT4 glucose transporters and insulin-regulated aminopeptidase (IRAP). Insulin acts through TUG proteins to control IRAP targeting, similar to GLUT4, the activity of vasopressin, an IRAP substrate, is reduced in mice with disrupted TUG action in muscle. TUG regulates vasopressin action. Exocytic translocation of vesicles in muscle coordinates vasopressin inactivation by IRAP with glucose uptake
metabolism
insulin-regulated aminopeptidase (IRAP) has many important regulatory functions
metabolism
the type of dietary fat does not influence latency period, incidence of animals with tumors, incidence of mortality, or tumor yield per rat. However, changes are observed in tumor volume and the histopathology. The type of dietary fat also differently modifies the enzymes involved in RAS regulation. Both insulin-regulated aminopeptidase (IRAP) and angiotensin IV forming activities are involved in this animal model of breast pathogenesis. The increase in serum IRAP activity can be an indicator of a misregulation of vasopressin (AVP) function
metabolism
-
insulin stimulates the exocytic translocation of vesicles containing GLUT4 glucose transporters and insulin-regulated aminopeptidase (IRAP). Insulin acts through TUG proteins to control IRAP targeting, similar to GLUT4, the activity of vasopressin, an IRAP substrate, is reduced in mice with disrupted TUG action in muscle. TUG regulates vasopressin action. Exocytic translocation of vesicles in muscle coordinates vasopressin inactivation by IRAP with glucose uptake
-
physiological function
-
part of the AT4 receptor
physiological function
aminopeptidases generate antigenic peptides influence immunodominance and adaptive cytotoxic immune responses. These enzymes efficiently process a vast number of different long peptide substrates. Insulin-regulated aminopeptidase prepares antigenic epitopes for crosspresentation in dendritic cells
physiological function
analysis of enzyme activity in high (HDM) and low (LDM) density microsomal fractions, and plasma membrane fraction (MF) from isolated adipocytes of healthy (C), food deprived (FD) and monosodium glutamate (MSG) obese rats on aminoacyl substrates with N-terminal Cys or Leu, in absence or presence of insulin, overview. The hydrolytic activity trafficking from LDM to MF under influence of insulin in C, MSG and FD acts only on N-terminal Cys. The pathophysiological significance of IRAP in adipocytes seems to be linked to comprehensive energy metabolism related roles of endogenous substrates with N-terminal cysteine pair such as vasopressin and oxytocin. Insulin-dependent traffic of CysAP activity has important pathophysiological implications
physiological function
association between behavioral social status and hypothalamic lnpep transcript abundance of LNPEP, variation in the rate of VT/IT peptide inactivation by LNPEP may be a contributing component in the mechanism whereby nonapeptides regulate social behavior, overview
physiological function
functional roles of soluble (Sol) and membrane-bound (MB) cystinylaminopeptidase (CysAP) activities, overview. Soluble and membrane-bound CysAP activities, acting separately or in concert and mainly in renal medulla, regulate the function of their susceptible endogenous substrates, and may participate meaningfully in the control of blood pressure and fluid balance
physiological function
placental vasopressinase, expressed in placental trophoblasts, degrades endogenous anti-diuretic hormone (ADH) but not 1-deamino-8-D-arginine vasopressin (dDAVP), the synthetic form with a modified N-terminal, thereby allowing the resolution of symptoms with dDAVP administration
physiological function
the AT4 receptor identified as the IRAP is found in neurons in the cortex, hippocampus and basal ganglia. The presence of aminopeptidases A and N in the pineal gland suggests local production of Ang IV that could act through its specific receptor (IRAP)/AT4 to modulate melatonin synthesis, analysis of the role of enzyme inhibitor Ang IV on melatonin synthesis using isolated pinealocyte cultures, overview. IRAP is an enzyme that is mostly associated with cellular membranes, and its translocation appears to be regulated by insulin, which activates its migration from the intracellular vesicles to the cellular membrane together with the glucose transporter, Glut4. IRAP plays either the role of a true receptor, the (IRAP)/AT4 receptor, inducing intracellular signaling pathways, or the role of an enzyme that metabolizes several peptides, such as oxytocin and arginine vasopressin
physiological function
the enzyme inactivates vasopressin in the muscle and adipose tissue regulated by TUG. Vasopressin regulates water permeability in the renal collecting system by both minute-to-minute effects on AQP2 targeting and hour-to-daylong effects on AQP2 abundance. Recombinant IRAP binds to TUG, and this interaction is mapped to a short peptide in IRAP that is critical for GLUT4 intracellular retention
physiological function
the insulin-regulated aminopeptidase (IRAP) is involved in vesicular trafficking and shares common regional distribution with the major somatostatin (SRIF) receptor subtype, the sst2A receptor, which is localized at postsynaptic sites of the principal neurons where it modulates neuronal activity. IRAP regulates the trafficking of the sst2A receptor, it is a negative regulator of sst2A receptor recycling. Following agonist exposure, this receptor rapidly internalizes and recycles slowly through the trans-Golgi network. IRAP ligands display anticonvulsive properties involving the sst2A receptor. IRAP ligands accelerate the recycling of the sst2A receptor that has internalized in neurons in vitro or in vivo. Most importantly, because IRAP ligands increase the density of this inhibitory receptor at the plasma membrane, they also potentiate the neuropeptide SRIF inhibitory effects on seizure activity. In addition to its aminopeptidase activity involved in peptide hormone processing, IRAP also acts as a receptor for the endogenous ligands angiotensin IV (Ang IV) and LVV hemorphin 7 (LVV-H7). IRAP ligands are on the one hand competitive inhibitors of the enzymatic activity of IRAP and on the other hand regulators of its trafficking with memory- and cognitive-enhancing effects of IRAP ligands. The extracellular part of IRAP contains the aminopeptidase activity, whereas its intracellular domain interacts with cytosolic proteins that contribute to GLUT4 vesicle retention and translocation to the plasma membrane
physiological function
-
the insulin-regulated aminopeptidase (IRAP) is involved in vesicular trafficking and shares common regional distribution with the major somatostatin (SRIF) receptor subtype, the sst2A receptor, which is localized at postsynaptic sites of the principal neurons where it modulates neuronal activity. IRAP regulates the trafficking of the sst2A receptor, it is a negative regulator of sst2A receptor recycling. Following agonist exposure, this receptor rapidly internalizes and recycles slowly through the trans-Golgi network. IRAP ligands display anticonvulsive properties involving the sst2A receptor. IRAP ligands accelerate the recycling of the sst2A receptor that has internalized in neurons in vitro or in vivo. Most importantly, because IRAP ligands increase the density of this inhibitory receptor at the plasma membrane, they also potentiate the neuropeptide SRIF inhibitory effects on seizure activity. In addition to its aminopeptidase activity involved in peptide hormone processing, IRAP also acts as a receptor for the endogenous ligands angiotensin IV (Ang IV) and LVV hemorphin 7 (LVV-H7). IRAP ligands are on the one hand competitive inhibitors of the enzymatic activity of IRAP and on the other hand regulators of its trafficking with memory- and cognitive-enhancing effects of IRAP ligands. The extracellular part of IRAP contains the aminopeptidase activity, whereas its intracellular domain interacts with cytosolic proteins that contribute to GLUT4 vesicle retention and translocation to the plasma membrane
-
physiological function
-
analysis of enzyme activity in high (HDM) and low (LDM) density microsomal fractions, and plasma membrane fraction (MF) from isolated adipocytes of healthy (C), food deprived (FD) and monosodium glutamate (MSG) obese rats on aminoacyl substrates with N-terminal Cys or Leu, in absence or presence of insulin, overview. The hydrolytic activity trafficking from LDM to MF under influence of insulin in C, MSG and FD acts only on N-terminal Cys. The pathophysiological significance of IRAP in adipocytes seems to be linked to comprehensive energy metabolism related roles of endogenous substrates with N-terminal cysteine pair such as vasopressin and oxytocin. Insulin-dependent traffic of CysAP activity has important pathophysiological implications
-
physiological function
-
the enzyme inactivates vasopressin in the muscle and adipose tissue regulated by TUG. Vasopressin regulates water permeability in the renal collecting system by both minute-to-minute effects on AQP2 targeting and hour-to-daylong effects on AQP2 abundance. Recombinant IRAP binds to TUG, and this interaction is mapped to a short peptide in IRAP that is critical for GLUT4 intracellular retention
-
physiological function
-
functional roles of soluble (Sol) and membrane-bound (MB) cystinylaminopeptidase (CysAP) activities, overview. Soluble and membrane-bound CysAP activities, acting separately or in concert and mainly in renal medulla, regulate the function of their susceptible endogenous substrates, and may participate meaningfully in the control of blood pressure and fluid balance
-
additional information
analysis of the structure of IRAP in an intermediate semi-close conformation, overview. Significant rearrangements of the GAMEN motif in IRAP are observed upon ligand binding, which couples to the transition between the original partially open and a new, fully closed conformation of the protein. Molecular dynamics simulations of IRAP focusing on local adaptation to the binding of a pseudopeptidic ligand
additional information
enzyme IRAP undergoes a conformational change upon inhibitor binding
additional information
insulin-responsive aminopeptidase (IRAP) is identified as an S-acylated protein in adipocytes and other tissues, semi-quantitative acyl-RAC technique shows that approximately 60% of IRAP is S-acylated in 3T3-L1 adipocytes
additional information
modeling of peptide hydrolysis in the active site of insulin-regulated aminopeptidase (IRAP) developed using density functional theory calculations and the cluster approach
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Tisljar, U.; Wolf, D.H.
Purification and characterization of the cystinyl bond cleaving yeast aminopeptidase yscXVI
FEBS Lett.
322
191-196
1993
Saccharomyces cerevisiae
brenda
Hanson, H.; Mannsfeldt, H.G.
Biochemische Beitraege zur Kenntnis der Serum-Oxytocinase
Nova Acta Leopold.
36
7-45
1971
Homo sapiens
-
brenda
Roy, A.C.; Sen, D.K.; Ratnam, S.S.
Fractionation and characterization of oxytocinases in human semen
J. Reprod. Fertil.
87
163-168
1989
Homo sapiens
brenda
Van Oudheusden, A.P.M.
Oxytocinase
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
5
15-20
1984
Homo sapiens
-
brenda
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Homo sapiens
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Homo sapiens
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Homo sapiens
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Homo sapiens
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Homo sapiens
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Ovis aries
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Insulin-regulated aminopeptidase marks an antigen-stimulated recycling compartment in mast cells
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Rattus norvegicus
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Homo sapiens
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Rattus norvegicus
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Mus musculus
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Homo sapiens
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P-LAP/IRAP-induced cell proliferation and glucose uptake in endometrial carcinoma cells via insulin receptor signaling
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Homo sapiens
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Rattus norvegicus
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Homo sapiens, Mus musculus
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Homo sapiens
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Homo sapiens
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Takeuchi, M.; Itakura, A.; Okada, M.; Mizutani, S.; Kikkawa, F.
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Rattus norvegicus
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Larrinaga, G.; Lopez, J.I.; Casis, L.; Blanco, L.; Gil, J.; Agirregoitia, E.; Varona, A.
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Homo sapiens
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Homo sapiens
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Homo sapiens
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Involvement of the AT1 receptor subtype in the effects of angiotensin IV and LVV-haemorphin 7 on hippocampal neurotransmitter levels and spatial working memory
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Mus musculus
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Gene knockout of insulin-regulated aminopeptidase: loss of the specific binding site for angiotensin IV and age-related deficit in spatial memory
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Mus musculus
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Inhibition of insulin-regulated aminopeptidase (IRAP) by arylsulfonamides
ChemistryOpen
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2014
Cricetulus griseus
brenda
Mountford, S.J.; Albiston, A.L.; Charman, W.N.; Ng, L.; Holien, J.K.; Parker, M.W.; Nicolazzo, J.A.; Thompson, P.E.; Chai, S.Y.
Synthesis, structure-activity relationships and brain uptake of a novel series of benzopyran inhibitors of insulin-regulated aminopeptidase
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Homo sapiens
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Papakyriakou, A.; Zervoudi, E.; Tsoukalidou, S.; Mauvais, F.X.; Sfyroera, G.; Mastellos, D.C.; van Endert, P.; Theodorakis, E.A.; Vourloumis, D.; Stratikos, E.
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Homo sapiens (Q9UIQ6), Homo sapiens
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Tobin, V.A.; Arechaga, G.; Brunton, P.J.; Russell, J.A.; Leng, G.; Ludwig, M.; Douglas, A.J.
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Rattus norvegicus (P97629)
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Vanga, S.R.; Saevmarker, J.; Ng, L.; Larhed, M.; Hallberg, M.; Aqvist, J.; Hallberg, A.; Chai, S.Y.; Gutierrez-de-Teran, H.
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ACS omega
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Homo sapiens (Q9UIQ6), Homo sapiens
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Abrahao, M.V.; Dos Santos, N.F.T.; Kuwabara, W.M.T.; do Amaral, F.G.; do Carmo Buonfiglio, D.; Peres, R.; Vendrame, R.F.A.; Flavio da Silveira, P.; Cipolla-Neto, J.; Baltatu, O.C.; Afeche, S.C.
Identification of insulin-regulated aminopeptidase (IRAP) in the rat pineal gland and the modulation of melatonin synthesis by angiotensin IV
Brain Res.
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Rattus norvegicus (P97629)
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Rodrigo, N.; Hocking, S.
Transient diabetes insipidus in a post-partum woman with pre-eclampsia associated with residual placental vasopressinase activity
Endocrinol. Diabetes Metab. Case Rep.
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2018
Homo sapiens (Q9UIQ6), Homo sapiens
brenda
Elkins, E.A.; Walti, K.A.; Newberry, K.E.; Lema, S.C.
Identification of an oxytocinase/vasopressinase-like leucyl-cystinyl aminopeptidase (LNPEP) in teleost fish and evidence for hypothalamic mRNA expression linked to behavioral social status
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Cyprinodon nevadensis amargosae (A0A1Z2WUC0)
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Hanson, A.L.; Morton, C.J.; Parker, M.W.; Bessette, D.; Kenna, T.J.
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Homo sapiens (Q9UIQ6)
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Ruixadz-Sanjuan, M.; Martinez-Martos, J.; Carrera-Gonzalez, M.; Mayas, M.; Garcia, M.; Arrazola, M.; Ramirez-Exposito, M.
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Rattus norvegicus (P97629)
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Habtemichael, E.N.; Alcazar-Roman, A.; Rubin, B.R.; Grossi, L.R.; Belman, J.P.; Julca, O.; Loeffler, M.G.; Li, H.; Chi, N.W.; Samuel, V.T.; Bogan, J.S.
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Mus musculus (Q8C129), Mus musculus, Mus musculus C57BL/6J (Q8C129)
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Svensson, F.; Engen, K.; Lundbaeck, T.; Larhed, M.; Skoeld, C.
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Homo sapiens (Q9UIQ6)
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Mpakali, A.; Saridakis, E.; Harlos, K.; Zhao, Y.; Papakyriakou, A.; Kokkala, P.; Georgiadis, D.; Stratikos, E.
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Homo sapiens (Q9UIQ6)
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Mpakali, A.; Saridakis, E.; Harlos, K.; Zhao, Y.; Kokkala, P.; Georgiadis, D.; Giastas, P.; Papakyriakou, A.; Stratikos, E.
ligand-induced conformational change of insulin-regulated aminopeptidase insights on catalytic mechanism and active site plasticity
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Homo sapiens (Q9UIQ6)
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Alponti, R.F.; Viana, L.G.; Yamanouye, N.; Silveira, P.F.
Insulin-regulated aminopeptidase in adipocyte is Cys-specific and affected by obesity
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Rattus norvegicus (P97629), Rattus norvegicus Wistar (P97629)
brenda
De Bundel, D.; Fafouri, A.; Csaba, Z.; Loyens, E.; Lebon, S.; El Ghouzzi, V.; Peineau, S.; Vodjdani, G.; Kiagiadaki, F.; Aourz, N.; Coppens, J.; Walrave, L.; Portelli, J.; Vanderheyden, P.; Chai, S.Y.; Thermos, K.; Bernard, V.; Collingridge, G.; Auvin, S.; Gressens, P.; Smolders, I.; Dournaud, P.
Trans-modulation of the somatostatin type 2A receptor trafficking by insulin-regulated aminopeptidase decreases limbic seizures
J. Neurosci.
35
11960-11975
2015
Rattus norvegicus (P97629), Rattus norvegicus Wistar (P97629)
brenda
Prieto, I.; Villarejo, A.B.; Segarra, A.B.; Wangensteen, R.; Banegas, I.; de Gasparo, M.; Vanderheyden, P.; Zorad, S.; Vives, F.; Ramirez-Sanchez, M.
Tissue distribution of CysAP activity and its relationship to blood pressure and water balance
Life Sci.
134
73-78
2015
Rattus norvegicus (P97629), Rattus norvegicus Wistar-Kyoto (P97629)
brenda
Werno, M.; Chamberlain, L.
S-acylation of the insulin-responsive aminopeptidase (IRAP) quantitative analysis and identification of modified cysteines
Sci. Rep.
5
12413-12420
2015
Mus musculus (Q8C129)
brenda