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Information on EC 3.4.24.71 - endothelin-converting enzyme 1 and Organism(s) Homo sapiens
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3.4.24.71 endothelin-converting enzyme 1Specify your search results
Word Map
- 3.4.24.71
- endothelins
- phosphoramidon
- artery
-
vasoconstrictor
- endopeptidase
- cardiovascular
- hypertension
- cardiac
- pulmonary
- angiotensin
- neprilysin
-
tone
-
vasoactive
- metalloprotease
- vessel
- coronary
-
phosphoramidon-sensitive
- metallopeptidases
-
contractile
-
preproet-1
- vasospasm
- thiorphan
-
atrial
-
natriuretic
-
pressor
- ventricular
- aortic
-
angiotensin-converting
- preproendothelin-1
-
endothelium-derived
-
et-1-induced
-
insulin-degrading
- drug development
-
baecs
-
hemodynamic
- medicine
-
vasopeptidase
-
etb-receptors
-
3.4.24.11
- metalloendopeptidase
-
subarachnoid
- chymase
-
conscious
-
ednra
- sarafotoxin
-
basilar
-
ppet-1
-
21-amino
-
prepro
- enzyme-2
- bosentan
-
et-1-mediated
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
ece-1, endothelin-converting enzyme, endothelin converting enzyme, endothelin-converting enzyme-1, ece-1b, endothelin converting enzyme-1, hece-1, et converting enzyme, endothelin-converting enzyme 1, endothelin-converting enzyme 1 (ece-1), 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ECE-1
endothelin converting enzyme-1
Endothelin-converting enzyme
endothelin-converting enzyme 1
endothelin-converting enzyme-1
additional information
ECE-1
-
-
-
-
ECE-1
-
-
649414, 649885, 651235, 652710, 653706, 667961, 668981, 669533, 669569, 669782, 669970, 670866, 683321, 683416, 683434, 683435, 683437, 683438, 683439, 683440, 683474, 683513, 683696, 683702, 683720, 683965, 684002, 697033, 697100, 697686, 699415, 701191, 709039, 709470, 709856, 710094, 719207, 720290, 720472
ECE-1
-
Endothelin-converting enzyme
-
-
-
-
endothelin-converting enzyme-1
-
-
additional information
-
ECE-1 is a type II membrane protease belonging to the neprilysin family of zinc metallopeptidases
additional information
-
endothelin-converting enzymes are a class of type II integral membrane-bound proteases, belonging to the M13 family of zinc metallopeptidases
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of the -Trp21-/-Val- bond in big endothelin to form endothelin 1
ECE-1 promotes the recycling and re-sensitization of NK1 receptors, by degrading endocytosed substance P in endothelial cell endosomes. ECE-1 promotes CGRP and somatostatin receptor recycling
-
Hydrolysis of the -Trp21-/-Val- bond in big endothelin to form endothelin 1
ECE-1 regulates re-sensitization of substance P signalling in HMEC-1-NK1 receptor cells
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
138238-81-0
-
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
(7-methoxy-coumarin-4-yl)acetyl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys(2,4-dinitrophenyl) + H2O
?
-
fluorogenic substrate
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys(2,4-dinitrophenyl)-OH + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-2,4-dinitrophenyl-OH + H2O
?
-
-
-
-
?
corticotropin-releasing factor + H2O
?
-
ECE-1 cleaves urocortin-1 (Ucn1) at three different sites but cleaves corticotropin-releasing factor (CRF) at only one site. ECE-1 degrades Ucn1 at both extracellular (pH 7.4) and endosomal (pH 5.5), whereas CRF is degraded at acidic pH alone. At a low or basal level, ECE-1 can disrupt association of Ucn1 or CRF with CRF1 in endosomes and free the receptor to promote recycling and resensitization
-
-
?
M7-methoxycoumarin-4-ylacetyl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys(2,4-dinitrophenyl)-OH + H2O
?
-
-
-
-
?
Somatostatin-14 + H2O
?
-
i.e. SST-14, degradation of rat substrate internalized via recombinantly expressed somatostatin receptor subtype sst2A into HEK-293 cells
-
-
?
urocortin-1 + H2O
?
-
ECE-1 cleaves urocortin-1 (Ucn1) at three different sites but cleaves corticotropin-releasing factor (CRF) at only one site. ECE-1 cleaves Ucn1 at Arg-34, which allows this ligands to bind and activate CRF1. ECE-1 degrades Ucn1 at both extracellular (pH 7.4) and endosomal (pH 5.5), whereas CRF is degraded at acidic pH alone. At a low or basal level, ECE-1 can disrupt association of Ucn1 or CRF with CRF1 in endosomes and free the receptor to promote recycling and resensitization
-
-
?
big endothelin + H2O
endothelin + ?
-
ECE-1 is a membrane-bound metalloprotease responsible for production of vasoactive endothelin-1 from inactive big ET-1
-
-
?
big endothelin + H2O
endothelin 1 + ?
-
ECE-1a, 1b, 1c and 1d are all equally active on endothelin
-
-
?
big endothelin-1 + H2O
endothelin + ?
-
key enzyme in the biosynthesis of the endothelins
-
?
big endothelin-1 + H2O
endothelin + ?
-
ECE-1 is a critical enzyme in the production of the potent vasoconstrictor peptide endothelin, ET-1
-
-
?
big endothelin-1 + H2O
endothelin-1 + ?
-
final step of posttranslational processing of this peptide
-
?
big endothelin-1 + H2O
endothelin-1 + ?
-
most potent naturally occurring vasoconstrictor
-
?
big endothelin-1 + H2O
endothelin-1 + ?
-
activation
-
-
?
big endothelin-1 + H2O
endothelin-1 + ?
-
ECE-1 inhibition in MCF-7 breast cancer cells leads to a significantly decreased ET-1 expression and reduced cell invasiveness, overview
-
-
?
big endothelin-1 + H2O
endothelin-1 + ?
-
short-term endothelin-1 release is not involved in the isometric tension in response to different agonists, e.g. 15-E2t-IsoP, of human umbilical vein ring with or without endothelium, overview
-
-
?
big endothelin-1 + H2O
endothelin-1 + ?
big endothelin-1 is hydrolyzed at Asp18-Ile19
-
-
?
big endothelin-I + H2O
endothelin + ?
-
key enzyme in the biosynthesis of the endothelins
-
?
calcitonin gene-related peptide + H2O
?
-
degradation, co-internalization with ECE-1 into early endosomes, calcitonin gene-related peptide degradation promotes CLR/RAMP1 recycling and beta-arrestin2 redistribution into the cytosol, ECE-1 inhibition or knockdown traps CLR/RAMP1 and beta-arrestin2 in endosomes and inhibits CLR/RAMP1 recycling and resensitization, whereas ECE-1 overexpression has the opposite effect, mechanism, overview
-
-
?
additional information
?
-
-
isoforms of endothelin-converting enzyme-1, ECE-1a-d, are present in early endosomes, where they degrade neuropeptides and regulate post-endocytic sorting of receptors, ECE-1 does not regulate either the resensitization of receptors for peptides that are not ECE-1 substrates, e.g. angiotensin II, or the recycling of the bradykinin B2 receptor, which transiently interacts with beta-arrestins
-
-
?
additional information
?
-
-
the enzyme catalyzes the final step in endothelin processing
-
-
?
additional information
?
-
-
the enzyme is involved in chalizia, a granulomatous lesions of the eyelid
-
-
?
additional information
?
-
-
the enzyme plays a crucial role in the regulation of vascular tone and endothelial function
-
-
?
additional information
?
-
-
ECE-1 and endosomal acidification regulate the duration of substance P-induced ERK2 activation
-
-
?
additional information
?
-
-
ECEs can hydrolyze several other biologically active peptides in vitro by cleavage on the amino side of hydrophobic residues
-
-
?
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
big endothelin-I + H2O
endothelin + ?
-
key enzyme in the biosynthesis of the endothelins
-
?
calcitonin gene-related peptide + H2O
?
-
degradation, co-internalization with ECE-1 into early endosomes, calcitonin gene-related peptide degradation promotes CLR/RAMP1 recycling and beta-arrestin2 redistribution into the cytosol, ECE-1 inhibition or knockdown traps CLR/RAMP1 and beta-arrestin2 in endosomes and inhibits CLR/RAMP1 recycling and resensitization, whereas ECE-1 overexpression has the opposite effect, mechanism, overview
-
-
?
big endothelin + H2O
endothelin + ?
-
ECE-1 is a membrane-bound metalloprotease responsible for production of vasoactive endothelin-1 from inactive big ET-1
-
-
?
big endothelin-1 + H2O
endothelin + ?
-
key enzyme in the biosynthesis of the endothelins
-
?
big endothelin-1 + H2O
endothelin + ?
-
ECE-1 is a critical enzyme in the production of the potent vasoconstrictor peptide endothelin, ET-1
-
-
?
big endothelin-1 + H2O
endothelin-1 + ?
-
final step of posttranslational processing of this peptide
-
?
big endothelin-1 + H2O
endothelin-1 + ?
-
most potent naturally occurring vasoconstrictor
-
?
big endothelin-1 + H2O
endothelin-1 + ?
-
ECE-1 inhibition in MCF-7 breast cancer cells leads to a significantly decreased ET-1 expression and reduced cell invasiveness, overview
-
-
?
big endothelin-1 + H2O
endothelin-1 + ?
-
short-term endothelin-1 release is not involved in the isometric tension in response to different agonists, e.g. 15-E2t-IsoP, of human umbilical vein ring with or without endothelium, overview
-
-
?
big endothelin-1 + H2O
endothelin-1 + ?
big endothelin-1 is hydrolyzed at Asp18-Ile19
-
-
?
additional information
?
-
-
isoforms of endothelin-converting enzyme-1, ECE-1a-d, are present in early endosomes, where they degrade neuropeptides and regulate post-endocytic sorting of receptors, ECE-1 does not regulate either the resensitization of receptors for peptides that are not ECE-1 substrates, e.g. angiotensin II, or the recycling of the bradykinin B2 receptor, which transiently interacts with beta-arrestins
-
-
?
additional information
?
-
-
the enzyme catalyzes the final step in endothelin processing
-
-
?
additional information
?
-
-
the enzyme is involved in chalizia, a granulomatous lesions of the eyelid
-
-
?
additional information
?
-
-
the enzyme plays a crucial role in the regulation of vascular tone and endothelial function
-
-
?
additional information
?
-
-
ECE-1 and endosomal acidification regulate the duration of substance P-induced ERK2 activation
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
additional information
Zn2+
binding site is located in the C-terminal domain and is close to the inner surface of the protein, coordinated in an approximately tetrahedral geometry, involving the side chains of the residues His607, His611, and Glu667
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,3R,4R,5R)-(2S)-(4-[2-(1,3-dioxo-1H,3H-benzo[de]isoquinolin-2-yl)ethyl]-3-isobutyl-5-phosphonopyrrolidine-2-carbonyl-amino)-3-(1H-indol-3-yl)propionic acid
-
0.01 mM, 91% inhibition of enzyme activity
(2R,4S,5R,6R)-(2S)-(5-[2-(1,3-dioxo-1H,3H-benzo[de]isoquinolin-2-yl)ethyl]-4-isobutyl-6-phosphonopiperidine-2-carbonyl-amino)-3-(1H-indol-3-yl)propionic acid
-
0.01 mM, 98% inhibition of enzyme activity
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2R)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino) 1H-Indole-3-propanoic acid
-
-
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2R)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
-
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2S)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino) 1H-indole-3-propanoic acid
-
-
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2S)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
-
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]amino)ethyl)phosphinyl]-(2R)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-phenyl propanoic acid
-
-
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]amino)ethyl)phosphinyl]-(2S)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-phenyl propanoic acid
-
-
(2S)-2-([3-(1,1'-biphenyl)-2-([hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]amino)ethyl)phosphinyl]methyl)-1-oxopropyl]-amino) 1H-indole-3-propanoic acid
-
-
(2S)-2-([3-(3'-[1,1'-biphenyl]-4''-yl-4',5'-dihydro-5'-isoxazolyl)-2-([hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]amino)ethyl)-phosphinyl]methyl)-1-oxopropyl]amino) 1H-indole-3-propanoic acid
-
-
(2S,4R)-2-[(2,5-difluorobenzylamino)methyl]-4-mercaptopyrrolidine-1-carboxylic acid isopropyl ester
-
IC50: 0.00109 mM
(2S,4R)-2-[2-[[4-mercapto-1-(naphthalene-2-sulfonyl)-pyrrolidine-2-carbonyl]methylamino]acetylamino]-benzoic acid methyl ester
-
IC50: 0.01089 mM
(2S,4R)-4-acetylsulfanyl-2-(2,4,5-trifluorobenzyloxymethyl)pyrrolidine-1-carboxylic acid 2,3-dihydrobenzo-[1,4]dioxin-5-yl ester
-
IC50: 0.0000765 mM
(2S,4R)-4-acetylsulfanyl-2-(2,4,5-trifluorobenzyloxymethyl)pyrrolidine-1-carboxylic acid 2-methoxycarbonylphenylester
-
IC50: 0.0000215 mM
(2S,4R)-4-mercapto-1-(naphthalene-2-sulfonyl)pyrrolidine-2-carboxylic acid N-methyl-N-(4-methylphenylsulfonyl)hydrazide
-
IC50: 0.00253 mM
(2S,4R)-4-mercapto-2-(2,4,5-trifluorobenzyloxymethyl)-pyrrolidine-1-carboxylic acid 2,3-dihydrobenzo[1,4]-dioxin-5-yl ester
-
IC50: 0.000137 mM
(2S,4R)-4-mercapto-2-(2,4,5-trifluorobenzyloxymethyl)-pyrrolidine-1-carboxylic acid 2-ethoxycarbonylphenylester
-
IC50: 0.000067 mM
(2S,4R)-5-[(2,5-difluorobenzylamino)methyl]-1-(5-propylpyrimidin-2-yl)pyrrolidine-3-thiol
-
IC50: 0.0000729 mM
(3R,5S)-1-(5-propylpyrimidin-2-yl)-5-(2,4,5-trifluorobenzyloxymethyl)pyrrolidine-3-thiol trifluoroacetate
-
IC50: 0.0000198 mM
(R,R)-5-[(2,4-difluorophenyl)-2-(3,3,3-trifluoro-2-methoxy-2-phenylpropionyl)amino]pent-4-ynoic acid methyl ester
-
-
(R,S)-5-[(2,4-difluorophenyl)-2-(3,3,3-trifluoro-2-methoxy-2-phenylpropionyl)amino]pent-4-ynoic acid methyl ester
-
-
(S)-2-[(tert-butoxycarbonyl)amino]-5-(2,4-difluorophenyl)pent-4-ynoic acid methyl ester
-
-
(S)-5-(2,4-difluorophenyl)-2-[[(dimethoxyphosphoryl)methyl]amino]pent-4-ynoic acid
-
-
(S)-5-(2,4-difluorophenyl)-2-[[(dimethoxyphosphoryl)methyl]amino]pent-4-ynoic acid methyl ester
-
-
(S)-[1-[(2-cyanoethyl)-1-H-tetrazol-5-yl]-4-(2-methoxyphenyl)but-3-ynyl]carbamic acid tert-butyl ester
-
-
(S)-[1-[(2-cyanoethyl)carbamoyl]-4-(2-methoxyphenyl)but-3-ynyl]carbamic acid tert-butyl ester
-
-
(S)-[[1-[[(2-biphenyl-4-ylethyl)-carbamoyl]-4-(2-fluorophenyl)but-3-ynyl]amino]methyl]phosphonic acid
-
-
(S)-[[[1-[1-(2-cyanoethyl)-1-H-tetrazol-5-yl]-4-(2-methoxyphenyl)but-3-ynyl]amino]methyl] phosphonic acid diphenyl ester
-
-
(S)-[[[[4-(2-methoxyphenyl)-1-H-tetrazol-5-yl]but-3-ynyl]amino]methyl] phosphonic acid
-
-
(S)-[[[[4-(2-methoxyphenyl)-1-H-tetrazol-5-yl]but-3-ynyl]amino]methyl] phosphonic acid diphenyl ester
-
-
(S,S)-2-[5-(2,4-difluorophenyl)-2-[[(dimethoxyphosphoryl)methyl]amino]pent-4-ynoyl]-4-methylpentanoic acid methyl ester
-
-
(S,S)-2-[[2-amino-5-(2-chlorophenyl)pent-4-ynoyl]amino]-4-methylpentanoic acid methyl ester
-
-
(S,S)-2-[[2-[(tert-butoxycarbonyl)amino]-5-(2-chlorophenyl)pent-4-ynoyl]-amino]-4-methylpentanoic acid methyl ester
-
-
(S,S)-2-[[2-[(tert-butoxycarbonyl)amino]pent-4-ynoyl]-amino]-4-methylpentanoic acid methyl ester
-
-
(S,S)-2-[[5-(2,4-difluorophenyl)-2-[(phosphonomethyl)amino]pent-4-ynoyl]amino]-4-methylpentanoic acid
-
-
(S,S)-2-[[5-(2-chlorophenyl)-2-[(phosphonomethyl)amino]pent-4-ynoyl]amino]-4-methylpentanoic acid
-
-
(S,S)-2-[[5-(2-chlorophenyl)-2-[[(dimethoxyphosphoryl)-methyl]amino]pent-4-ynoyl]amino]-4-methylpentanoic acid methyl ester
-
-
(S,S)-2-[[5-(2-fluorophenyl)-2-[(phosphonomethyl)-amino]pent-4-ynoyl]amino]-4-methyl pentanoic acid
-
-
(S,S)-2-[[5-(3-fluorophenyl)-2-[(phosphonomethyl)-amino]pent-4-ynoyl]amino]-4-methyl pentanoic acid
-
-
(S,S)-5-phenyl-2-[(3,3,3-trifluoro-2-methoxy-2-phenylpropionyl)amino]pent-4-ynoic acid (2-cyanoethyl)amide
-
-
1-(2,6-difluorobenzyl)-5-[(3,3-dimethylbutanoyl)amino]-N-phenyl-1H-indole-2-carboxamide
-
IC50: 0.00065 mM
1-(2-fluorobenzyl)-5-[[(1-methylcyclopentyl)acetyl]amino]-N-phenyl-1H-indole-2-carboxamide
-
IC50: 0.00012 mM
1-(cyclohexylmethyl)-5-[(3,3-dimethylbutanoyl)amino]-N-phenyl-1H-indole-2-carboxamide
-
IC50: 0.00086 mM
2-[(tert-butoxycarbonyl)amino]-5-(2,4-difluorophenyl)pent-4-ynoic acid methyl ester
-
-
2-{[(1-{[(2S)-3-methyl-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]amino}-3-(naphthalen-1-yl)propanoic acid
-
2-{[(1-{[(2S)-3-methyl-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]amino}-3-(naphthalen-2-yl)propanoic acid
-
2-{[(1-{[(2S)-3-methyl-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]amino}-3-[3'-(trifluoromethyl)biphenyl-4-yl]propanoic acid
-
3-(2'-methoxybiphenyl-4-yl)-2-{[(1-{[(2S)-3-methyl-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]amino}propanoic acid
-
3-(2,3'-bipyridin-5'-yl)-N-[(1-{[(2S)-3-methyl-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]alanine
-
3-(3'-chloro-4'-fluorobiphenyl-4-yl)-2-{[(1-{[(2S)-3-methyl-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]amino}propanoic acid
-
3-(4'-chlorobiphenyl-4-yl)-2-{[(1-{[(2S)-3-methyl-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]amino}propanoic acid
-
3-(4'-fluorobiphenyl-4-yl)-2-{[(1-{[(2S)-3-methyl-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]amino}propanoic acid
-
3-(biphenyl-4-yl)-2-[({1-[(2-methyl-2-sulfanylpropanoyl)amino]cyclopentyl}carbonyl)amino]propanoic acid
-
3-(biphenyl-4-yl)-2-{[(1-{[(2R)-2-sulfanylhexanoyl]amino}cyclopentyl)carbonyl]amino}propanoic acid
-
3-(biphenyl-4-yl)-2-{[(1-{[(2R)-3-hydroxy-2-sulfanylpropanoyl]amino}cyclopentyl)carbonyl]amino}propanoic acid
-
3-(biphenyl-4-yl)-2-{[(1-{[(2R)-3-methoxy-2-sulfanylpropanoyl]amino}cyclopentyl)carbonyl]amino}propanoic acid
-
3-(biphenyl-4-yl)-2-{[(1-{[(2R)-3-phenyl-2-sulfanylpropanoyl]amino}cyclopentyl)carbonyl]amino}propanoic acid
-
3-(biphenyl-4-yl)-2-{[(1-{[(2R)-4-(methylsulfanyl)-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]amino}propanoic acid
-
3-(biphenyl-4-yl)-2-{[(1-{[(2R)-4-methyl-2-sulfanylpentanoyl]amino}cyclopentyl)carbonyl]amino}propanoic acid
-
3-(biphenyl-4-yl)-2-{[(1-{[(2S)-2-sulfanylhexanoyl]amino}cyclopentyl)carbonyl]amino}propanoic acid
-
3-(biphenyl-4-yl)-2-{[(1-{[(2S)-3-methyl-2-sulfanylpentanoyl]amino}cyclopentyl)carbonyl]amino}propanoic acid
-
3-(biphenyl-4-yl)-2-{[(1-{[(2S)-4-methyl-2-sulfanylpentanoyl]amino}cyclopentyl)carbonyl]amino}propanoic acid
-
3-(biphenyl-4-yl)-2-{[(1-{[(3S)-3-methoxy-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]amino}propanoic acid
-
3-(biphenyl-4-yl)-2-{[(1-{[(3S)-3-methyl-2-sulfanylpentanoyl]amino}cyclopentyl)carbonyl]amino}propanoic acid
-
3-[4-(furan-2-yl)pyrimidin-5-yl]-N-[(1-{[(2S)-3-methyl-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]alanine
-
3-[4-(furan-3-yl)pyrimidin-5-yl]-N-[(1-{[(2S)-3-methyl-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]alanine
-
3-[5-(2-methoxyphenyl)pyridin-3-yl]-N-[(1-{[(2S)-3-methyl-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]alanine
-
3-[6-(3-aminophenyl)pyridin-3-yl]-N-[(1-{[(2S)-3-methyl-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]alanine
-
3-{6-[3-(acetylamino)phenyl]pyridin-3-yl}-N-[(1-{[(2S)-3-methyl-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]alanine
-
4-chloro-N-(((4-cyano-3-methyl-1-phenyl-1H-pyrazol-5-yl)amino)carbonyl)benzenesulfonamide
-
-
4-chloro-N-[(4-cyano-3-methyl-1-phenyl-1H-pyrazol-5-yl)amino]carbonyl benzenesulfonamide
-
-
4-cyclohexyl-N-[(1-{[(2S)-3-methyl-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]phenylalanine
-
4-furan-2-yl-N-[(1-{[(2S)-3-methyl-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]phenylalanine
-
4-[([5-[(2,2-dimethylpropyl)carbamoyl]-1-(2-fluorobenzyl)-1H-indol-2-yl]carbonyl)amino]benzoic acid
-
IC50: 0.00039 mM
5-[(3,3-dimethylbutanethioyl)amino]-1-(2-fluorobenzyl)-N-phenyl-1H-indole-2-carboxamide
-
IC50: 0.00066 mM
5-[(3,3-dimethylbutanoyl)amino]-1-(2-fluorobenzyl)-N-phenyl-1H-indole-2-carboxamide
-
IC50: 0.00022 mM
5-[(3,3-dimethylbutanoyl)amino]-1-(2-methylbenzyl)-N-phenyl-1H-indole-2-carboxamide
-
IC50: 0.003 mM
5-[(3,3-dimethylbutanoyl)amino]-1-[(2-methyl-1,3-thiazol-4-yl)methyl]-N-phenyl-1H-indole-2-carboxamide
-
IC50: 0.0022 mM
5-[(3,3-dimethylbutanoyl)amino]-N,1-diphenyl-1H-indole-2-carboxamide
-
IC50: 0.0059 mM
5-[(3,3-dimethylbutanoyl)amino]-N-phenyl-1-(2-phenylethyl)-1H-indole-2-carboxamide
-
IC50: 0.0051 mM
5-[(3,3-dimethylbutanoyl)amino]-N-phenyl-1-[2-(trifluoromethyl)benzyl]-1H-indole-2-carboxamide
-
IC50: 0.00017 mM
5-[(4,4-dimethylpentanoyl)amino]-1-(2-fluorobenzyl)-N-phenyl-1H-indole-2-carboxamide
-
IC50: 0.00074 mM
5-[(bicyclo[2.2.1]hept-2-ylacetyl)amino]-1-(2-fluorobenzyl)-N-phenyl-1H-indole-2-carboxamide
-
IC50: 0.0003 mM
5-[(cyclopentylacetyl)amino]-1-(2-fluorobenzyl)-N-phenyl-1H-indole-2-carboxamide
-
IC50: 0.0064 mM
5-[([5-[(2,2-dimethylpropyl)carbamoyl]-1-(2-fluorobenzyl)-1H-indol-2-yl]carbonyl)amino]pyridine-3-carboxylic acid
-
IC50: 0.074 mM
5-[[(2,2-dimethylpropyl)sulfonyl]amino]-1-(2-fluorobenzyl)-N-phenyl-1H-indole-2-carboxamide
-
IC50: 0.0067 mM
benzoylsulfanyl-2-(2,4,5-trifluorobenzyloxymethyl)-pyrrolidine-1-carboxylic acid 2,3-dihydrobenzo[1,4]-dioxin-5-yl ester
-
IC50: 0.0004805 mM
cyclohexyl-2-[[5-(2,4-difluorophenyl)-2-[(phosphonomethyl)-amino]pent-4-ynoyl]amino]propionic acid
-
-
ECEi
-
addition of an ECE-1 specific inhibitor (ECEi) to PC-3 cells reduces phosphorylation of focal adhesion kinase
-
L-tryptophan, N-[[1-[[(2S)-2-(acetylthio)-4-methyl-1 oxopentyl]amino]cyclopentyl]-carbonyl]-methyl ester
-
CGS 37808, at an oral dose of 10 mgEq per kg, CGS 37808 produced 71% and 67% inhibition of the big ET-1 pressor response at 30 and 120 min, respectively
L-tryptophan, N-[[1-[[(2S)-2-mercapto-4-methyl-1-oxopentyl]amino]-cyclopentyl]carbonyl]
-
CGS 35601, IC50: 55 nM
N-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-2-(3-phenyl-1,2,4-oxadiazol-5-yl)-1H-indole-5-carboxamide
-
IC50: 0.01 mM
N-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-2-[(phenylamino)methyl]-1H-indole-5-carboxamide
-
IC50: 0.01 mM
N-(2-benzyl-3-[[(1R)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]propanoyl)-L-tryptophan
-
-
N-(3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-{[3-(biphenyl-4-yl)-4,5-dihydro-1,2-oxazol-5-yl]methyl}propanoyl)-L-tryptophan
-
-
N-(alpha-L-rhamnopyranosyl-oxyhydroxy-phosphinyl)-L-Leu-L-Trp
mechanism of inhibitor binding analysed (cocrystallization)
N-[(1-{[(2R)-2-sulfanylhexanoyl]amino}cyclopentyl)carbonyl]-3-[4-(thiophen-3-yl)pyrimidin-5-yl]alanine
-
N-[(1-{[(2R)-2-sulfanylpentanoyl]amino}cyclopentyl)carbonyl]-3-[4-(thiophen-3-yl)pyrimidin-5-yl]alanine
-
N-[(1-{[(2S)-2-sulfanylhexanoyl]amino}cyclopentyl)carbonyl]-3-[4-(thiophen-3-yl)pyrimidin-5-yl]alanine
-
N-[(1-{[(2S)-2-sulfanylpentanoyl]amino}cyclopentyl)carbonyl]-3-[4-(thiophen-3-yl)pyrimidin-5-yl]alanine
-
N-[(1-{[(2S)-3-cyclohexyl-2-sulfanylpropanoyl]amino}cyclopentyl)carbonyl]-3-[4-(thiophen-3-yl)pyrimidin-5-yl]alanine
-
N-[(1-{[(2S)-3-methyl-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]-3-(4-phenylpyrimidin-5-yl)alanine
-
N-[(1-{[(2S)-3-methyl-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]-3-[4-(thiophen-3-yl)pyrimidin-5-yl]alanine
-
N-[(1-{[(2S)-3-methyl-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]-3-[6-(3-nitrophenyl)pyridin-3-yl]alanine
-
N-[(1-{[(2S)-3-methyl-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]-4-thiophen-3-ylphenylalanine
-
N-[(1-{[(2S)-4-(methylsulfanyl)-2-sulfanylbutanoyl]amino}cyclopentyl)carbonyl]-3-[4-(thiophen-3-yl)pyrimidin-5-yl]alanine
-
N-[(1-{[(2S)-4-methyl-2-sulfanylpentanoyl]amino}cyclopentyl)carbonyl]-3-[4-(thiophen-3-yl)pyrimidin-5-yl]alanine
-
N-[3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-(biphenyl-4-ylmethyl)propanoyl]-L-tryptophan
-
-
N-{(2S)-3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-[(3-phenyl-1,2-oxazol-5-yl)methyl]propanoyl}-L-tryptophan
-
-
N2-(4-carbamoylphenyl)-N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-1H-indole-2,5-dicarboxamide
-
IC50: 0.00022 mM
N2-(5-aminopyridin-2-yl)-N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-1H-indole-2,5-dicarboxamide
-
IC50: 0.0012 mM
N2-(6-aminopyridin-3-yl)-N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-1H-indole-2,5-dicarboxamide
-
IC50: 0.00017 mM
N2-(6-chloropyridin-3-yl)-N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-1H-indole-2,5-dicarboxamide
-
IC50: 0.00044 mM
N2-[4-(dimethylcarbamoyl)phenyl]-N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-1H-indole-2,5-dicarboxamide
-
IC50: 0.00021 mM
N2-[4-[(butylsulfonyl)amino]phenyl]-N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-1H-indole-2,5-dicarboxamide
-
IC50: 0.0002 mM
N2-[6-(acetylamino)pyridin-3-yl]-N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-1H-indole-2,5-dicarboxamide
-
IC50: 0.00013 mM
N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-N2-(3-[[4-(methylsulfamoyl)phenyl]carbamoyl]phenyl)-1H-indole-2,5-dicarboxamide
-
IC50: 0.00015 mM
N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-N2-1,3,4-thiadiazol-2-yl-1H-indole-2,5-dicarboxamide
-
IC50: 0.0023 mM
N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-N2-1H-pyrazol-3-yl-1H-indole-2,5-dicarboxamide
-
IC50: 0.01 mM
N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-N2-phenyl-1H-indole-2,5-dicarboxamide
-
IC50: 0.007 mM; IC50: 0.01 mM
N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-N2-pyridin-3-yl-1H-indole-2,5-dicarboxamide
-
IC50: 0.00085 mM
N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-N2-[3-[(4-sulfamoylphenyl)carbamoyl]phenyl]-1H-indole-2,5-dicarboxamide
-
IC50: 0.000039 mM
N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-N2-[5-[(4-methylpiperazin-1-yl)carbonyl]pyridin-3-yl]-1H-indole-2,5-dicarboxamide
-
IC50: 0.09 mM
RO 67-7447
-
i.e. (2S,4R)-4-mercapto-2-(2,4,5-trifluoro-benzyloxymethyl)-pyrrolidine-1-carboxylic acid 2-methoxycarbonyl-phenyl ester, a selective ECE-1 inhibitor
SLV-306
-
KC-12792, synthetic inhibitor, ECE-1/NEP inhibitor, clinical trial for treatment of arterial hypertension and heart failure in human
specific ECE-1 inhibitor
-
in the presence of 0.001 M ECE-1 inhibitor, cell number was effectively reduced to ~70% of control
-
[Lys-Gly-His-Lys-Cu]+
-
metallopeptide, IC50: 0.0049 mM under hydrolytic condtions
SM-19712
-
a specific ECE-1 inhibitor. SM-191712 causes sustained ERK2 activation in cytosolic and nuclear fractions after substance P removal
additional information
-
acidification to pH 6.4 inhibits plasma membrane ECE activity
-
additional information
-
prevention of acidification of endosomes using bafilomycin A1 inhibits the degradation of internalized somatostatin-14
-
additional information
-
carbachol and phorbol 12-myristate 13-acetate reduce enzyme expression in neuroblastoma NB7 cells, only isozyme ECE-1c remains detectable, overview
-
additional information
-
RNAi-induced knockdown of ECE-1 reduces ECE-1 mRNA and protein levels leading to 80% to 90% inhibition of endothelin-1 secretion by the ovarian carcinoma cells, analysation of cell's behaviour and effect on the cancer
-
additional information
-
ECE-1 inhibition causes endosomal retention of the substance P neurokinin 1 receptor, beta-arrestins, and Src, resulting in markedly sustained ERK2 activation in the cytosol and nucleus. ECE-1 inhibition also enhances substance P-induced expression and phosphorylation of the nuclear death receptor Nur77, resulting in cell death
-
additional information
-
phosphinic tripeptides as dual angiotensin-converting enzyme C-domain and endothelin-converting enzyme-1, while sparing neprilysin, inhibitors, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
K49-P1-20
i.e. N-terminal domain of Bothrops asper myotoxin II, 2fold enhancement of enzyme activity (maximal stimulation with 0.0001 mg/ml), activation concentration 50 (AC50) is 0.00192 mM
additional information
-
protein kinase C epsilon, PKCepsilon, stimulates ECE-1 activity, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0046
(7-methoxycoumarin-4-yl)acetyl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-2,4-dinitrophenyl-OH
-
pH not specified in the publication, temperature not specified in the publication
0.0164
amyloid beta 40
in the presence of K49-P1-20, at pH 6.3 and 37°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000008
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2R)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino) 1H-Indole-3-propanoic acid
-
pH not specified in the publication, temperature not specified in the publication
0.000014
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2R)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
pH not specified in the publication, temperature not specified in the publication
0.000026
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2S)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino) 1H-indole-3-propanoic acid
-
pH not specified in the publication, temperature not specified in the publication
0.000275
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2S)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0000077
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]amino)ethyl)phosphinyl]-(2R)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-phenyl propanoic acid
-
pH not specified in the publication, temperature not specified in the publication
0.00024
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]amino)ethyl)phosphinyl]-(2S)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-phenyl propanoic acid
-
pH not specified in the publication, temperature not specified in the publication
0.01
(2S)-2-([3-(1,1'-biphenyl)-2-([hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]amino)ethyl)phosphinyl]methyl)-1-oxopropyl]-amino) 1H-indole-3-propanoic acid
-
pH not specified in the publication, temperature not specified in the publication
0.01
(2S)-2-([3-(3'-[1,1'-biphenyl]-4''-yl-4',5'-dihydro-5'-isoxazolyl)-2-([hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]amino)ethyl)-phosphinyl]methyl)-1-oxopropyl]amino) 1H-indole-3-propanoic acid
-
pH not specified in the publication, temperature not specified in the publication
0.000022
CGS 35066
-
pH not specified in the publication, temperature not specified in the publication
0.0012
N-(2-benzyl-3-[[(1R)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]propanoyl)-L-tryptophan
-
pH not specified in the publication, temperature not specified in the publication
0.00091
N-(3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-{[3-(biphenyl-4-yl)-4,5-dihydro-1,2-oxazol-5-yl]methyl}propanoyl)-L-tryptophan
-
pH not specified in the publication, temperature not specified in the publication
0.0021
N-[3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-(biphenyl-4-ylmethyl)propanoyl]-L-tryptophan
-
pH not specified in the publication, temperature not specified in the publication
0.005
N-{(2S)-3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-[(3-phenyl-1,2-oxazol-5-yl)methyl]propanoyl}-L-tryptophan
-
pH not specified in the publication, temperature not specified in the publication
0.0012
phosphoramidon
-
pH not specified in the publication, temperature not specified in the publication
0.05
RXPA380
-
pH not specified in the publication, temperature not specified in the publication
0.00008
SCH-54,470
-
pH not specified in the publication, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00109
(2S,4R)-2-[(2,5-difluorobenzylamino)methyl]-4-mercaptopyrrolidine-1-carboxylic acid isopropyl ester
Homo sapiens
-
IC50: 0.00109 mM
0.01089
(2S,4R)-2-[2-[[4-mercapto-1-(naphthalene-2-sulfonyl)-pyrrolidine-2-carbonyl]methylamino]acetylamino]-benzoic acid methyl ester
Homo sapiens
-
IC50: 0.01089 mM
0.0000765
(2S,4R)-4-acetylsulfanyl-2-(2,4,5-trifluorobenzyloxymethyl)pyrrolidine-1-carboxylic acid 2,3-dihydrobenzo-[1,4]dioxin-5-yl ester
Homo sapiens
-
IC50: 0.0000765 mM
0.0000215
(2S,4R)-4-acetylsulfanyl-2-(2,4,5-trifluorobenzyloxymethyl)pyrrolidine-1-carboxylic acid 2-methoxycarbonylphenylester
Homo sapiens
-
IC50: 0.0000215 mM
0.00253
(2S,4R)-4-mercapto-1-(naphthalene-2-sulfonyl)pyrrolidine-2-carboxylic acid N-methyl-N-(4-methylphenylsulfonyl)hydrazide
Homo sapiens
-
IC50: 0.00253 mM
0.000137
(2S,4R)-4-mercapto-2-(2,4,5-trifluorobenzyloxymethyl)-pyrrolidine-1-carboxylic acid 2,3-dihydrobenzo[1,4]-dioxin-5-yl ester
Homo sapiens
-
IC50: 0.000137 mM
0.000067
(2S,4R)-4-mercapto-2-(2,4,5-trifluorobenzyloxymethyl)-pyrrolidine-1-carboxylic acid 2-ethoxycarbonylphenylester
Homo sapiens
-
IC50: 0.000067 mM
0.0000729
(2S,4R)-5-[(2,5-difluorobenzylamino)methyl]-1-(5-propylpyrimidin-2-yl)pyrrolidine-3-thiol
Homo sapiens
-
IC50: 0.0000729 mM
0.0000198
(3R,5S)-1-(5-propylpyrimidin-2-yl)-5-(2,4,5-trifluorobenzyloxymethyl)pyrrolidine-3-thiol trifluoroacetate
Homo sapiens
-
IC50: 0.0000198 mM
0.00065
1-(2,6-difluorobenzyl)-5-[(3,3-dimethylbutanoyl)amino]-N-phenyl-1H-indole-2-carboxamide
Homo sapiens
-
IC50: 0.00065 mM
0.00012
1-(2-fluorobenzyl)-5-[[(1-methylcyclopentyl)acetyl]amino]-N-phenyl-1H-indole-2-carboxamide
Homo sapiens
-
IC50: 0.00012 mM
0.00086
1-(cyclohexylmethyl)-5-[(3,3-dimethylbutanoyl)amino]-N-phenyl-1H-indole-2-carboxamide
Homo sapiens
-
IC50: 0.00086 mM
0.00039
4-[([5-[(2,2-dimethylpropyl)carbamoyl]-1-(2-fluorobenzyl)-1H-indol-2-yl]carbonyl)amino]benzoic acid
Homo sapiens
-
IC50: 0.00039 mM
0.00066
5-[(3,3-dimethylbutanethioyl)amino]-1-(2-fluorobenzyl)-N-phenyl-1H-indole-2-carboxamide
Homo sapiens
-
IC50: 0.00066 mM
0.00022
5-[(3,3-dimethylbutanoyl)amino]-1-(2-fluorobenzyl)-N-phenyl-1H-indole-2-carboxamide
Homo sapiens
-
IC50: 0.00022 mM
0.003
5-[(3,3-dimethylbutanoyl)amino]-1-(2-methylbenzyl)-N-phenyl-1H-indole-2-carboxamide
Homo sapiens
-
IC50: 0.003 mM
0.0022
5-[(3,3-dimethylbutanoyl)amino]-1-[(2-methyl-1,3-thiazol-4-yl)methyl]-N-phenyl-1H-indole-2-carboxamide
Homo sapiens
-
IC50: 0.0022 mM
0.0059
5-[(3,3-dimethylbutanoyl)amino]-N,1-diphenyl-1H-indole-2-carboxamide
Homo sapiens
-
IC50: 0.0059 mM
0.0051
5-[(3,3-dimethylbutanoyl)amino]-N-phenyl-1-(2-phenylethyl)-1H-indole-2-carboxamide
Homo sapiens
-
IC50: 0.0051 mM
0.00017
5-[(3,3-dimethylbutanoyl)amino]-N-phenyl-1-[2-(trifluoromethyl)benzyl]-1H-indole-2-carboxamide
Homo sapiens
-
IC50: 0.00017 mM
0.00074
5-[(4,4-dimethylpentanoyl)amino]-1-(2-fluorobenzyl)-N-phenyl-1H-indole-2-carboxamide
Homo sapiens
-
IC50: 0.00074 mM
0.0003
5-[(bicyclo[2.2.1]hept-2-ylacetyl)amino]-1-(2-fluorobenzyl)-N-phenyl-1H-indole-2-carboxamide
Homo sapiens
-
IC50: 0.0003 mM
0.0064
5-[(cyclopentylacetyl)amino]-1-(2-fluorobenzyl)-N-phenyl-1H-indole-2-carboxamide
Homo sapiens
-
IC50: 0.0064 mM
0.074
5-[([5-[(2,2-dimethylpropyl)carbamoyl]-1-(2-fluorobenzyl)-1H-indol-2-yl]carbonyl)amino]pyridine-3-carboxylic acid
Homo sapiens
-
IC50: 0.074 mM
0.0067
5-[[(2,2-dimethylpropyl)sulfonyl]amino]-1-(2-fluorobenzyl)-N-phenyl-1H-indole-2-carboxamide
Homo sapiens
-
IC50: 0.0067 mM
0.0004805
benzoylsulfanyl-2-(2,4,5-trifluorobenzyloxymethyl)-pyrrolidine-1-carboxylic acid 2,3-dihydrobenzo[1,4]-dioxin-5-yl ester
Homo sapiens
-
IC50: 0.0004805 mM
0.000017
CGS 26303
Homo sapiens
-
optimized form of inhibitor, human recombinant ECE-1 overexpressed in CHO cells
0.000055
L-tryptophan, N-[[1-[[(2S)-2-mercapto-4-methyl-1-oxopentyl]amino]-cyclopentyl]carbonyl]
Homo sapiens
-
CGS 35601, IC50: 55 nM
0.01
N-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-2-(3-phenyl-1,2,4-oxadiazol-5-yl)-1H-indole-5-carboxamide
Homo sapiens
-
IC50: 0.01 mM
0.01
N-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-2-[(phenylamino)methyl]-1H-indole-5-carboxamide
Homo sapiens
-
IC50: 0.01 mM
0.00022
N2-(4-carbamoylphenyl)-N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-1H-indole-2,5-dicarboxamide
Homo sapiens
-
IC50: 0.00022 mM
0.0012
N2-(5-aminopyridin-2-yl)-N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-1H-indole-2,5-dicarboxamide
Homo sapiens
-
IC50: 0.0012 mM
0.00017
N2-(6-aminopyridin-3-yl)-N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-1H-indole-2,5-dicarboxamide
Homo sapiens
-
IC50: 0.00017 mM
0.00044
N2-(6-chloropyridin-3-yl)-N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-1H-indole-2,5-dicarboxamide
Homo sapiens
-
IC50: 0.00044 mM
0.00021
N2-[4-(dimethylcarbamoyl)phenyl]-N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-1H-indole-2,5-dicarboxamide
Homo sapiens
-
IC50: 0.00021 mM
0.0002
N2-[4-[(butylsulfonyl)amino]phenyl]-N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-1H-indole-2,5-dicarboxamide
Homo sapiens
-
IC50: 0.0002 mM
0.00013
N2-[6-(acetylamino)pyridin-3-yl]-N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-1H-indole-2,5-dicarboxamide
Homo sapiens
-
IC50: 0.00013 mM
0.00015
N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-N2-(3-[[4-(methylsulfamoyl)phenyl]carbamoyl]phenyl)-1H-indole-2,5-dicarboxamide
Homo sapiens
-
IC50: 0.00015 mM
0.0023
N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-N2-1,3,4-thiadiazol-2-yl-1H-indole-2,5-dicarboxamide
Homo sapiens
-
IC50: 0.0023 mM
0.01
N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-N2-1H-pyrazol-3-yl-1H-indole-2,5-dicarboxamide
Homo sapiens
-
IC50: 0.01 mM
0.007 - 0.01
N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-N2-phenyl-1H-indole-2,5-dicarboxamide
0.00085
N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-N2-pyridin-3-yl-1H-indole-2,5-dicarboxamide
Homo sapiens
-
IC50: 0.00085 mM
0.000039
N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-N2-[3-[(4-sulfamoylphenyl)carbamoyl]phenyl]-1H-indole-2,5-dicarboxamide
Homo sapiens
-
IC50: 0.000039 mM
0.09
N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-N2-[5-[(4-methylpiperazin-1-yl)carbonyl]pyridin-3-yl]-1H-indole-2,5-dicarboxamide
Homo sapiens
-
IC50: 0.09 mM
0.0049
[Lys-Gly-His-Lys-Cu]+
Homo sapiens
-
metallopeptide, IC50: 0.0049 mM under hydrolytic condtions
0.007
N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-N2-phenyl-1H-indole-2,5-dicarboxamide
Homo sapiens
-
IC50: 0.007 mM
0.01
N5-(2,2-dimethylpropyl)-1-(2-fluorobenzyl)-N2-phenyl-1H-indole-2,5-dicarboxamide
Homo sapiens
-
IC50: 0.01 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
667961, 668981, 669533, 669569, 669782, 669970, 669974, 670866, 683321, 683416, 683439, 683474, 683513, 683702, 683720, 683725, 683918, 683965, 684002, 697033, 697034, 697100, 697686, 699415
-
-
-
UniProt
Chinese population, ECE1 shows four isoforms, ECE-1a, ECE-1b, ECE-1c and ECE-1d, gene ECE-1b
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
determination of enzyme expression by immunohistochemical analysis on atherosclerotic and nonatherosclerotic vascular tissue using a combination of ECE-1 isoform-specific antibodies, distinct expression patterns for ECE-1a and ECE-1c, overview
-
ECE-1 overexpression, immunohistochemic ECE-1 expression analysis of 600 different samples, the expression of ECE-1 is correlated to VEGF expression, overview
-
ECE-1 expression in Alzheimer's disease brain shows no significant difference compared with age-matched controls
-
from healthy persons and from patients with Crohn's disease, enzyme expression anaylsis in different samples, healthy tissue shows enzyme expression mainly in the muscular layer and the vasculature, while in Crohn'sdisease colonic tissue, the enzyme is found at inflammatory sites and fibrotic tissue, overview
-
enzyme distribution in the endometrium during different developmental phases, the enzyme expression varies during the menstrual cycle, epithelial cell, overview
-
enzyme expression in chalizia in meibomian adenomers, conjunctival epithelium, tarsal mucous glands, and in inflammatory cells, immunohistochemic analysis, overview
-
from blood, determination of enzyme expression by immunohistochemical analysis using a combination of ECE-1 isoform-specific antibodies, expression of isozymes ECE-1a and ECE-1c
-
increased ECE-1 content in hypercholesterolemic patients
-
primary cells derived from malignant tissue from radical prostatectomies, expression and localization of the ECE-1 isozymes, overview, upregulation of the isozyme ECE-1c
-
primary cells derived from benign tissue from radical prostatectomies, expression and localization of the ECE-1 isozymes, overview
-
aortic, determination of enzyme expression by immunohistochemical analysis using a combination of ECE-1 isoform-specific antibodies, expression of isozyme ECE-1a
additional information
-
analysis of the levels of ECE-1 expression and distribution under normal and pathologic conditions of Alzheimer disease, overview
-
expression analysis of ECE-1 in the temporal cortex of patients with Alzheimer's disease, vascular dementia, and controls, overview. ECE-1 occurs in vascular endothelial cells. ECE-1 mRNA or protein levels, of either full-length ECE-1 or soluble spliced variant, ECE-1sv, in Alzheimer's disease or vascular dementia show no differences compared to controls
-
quantitative immunohistochemic analysis of enzyme distribution in autopsy specimen of post-percutaneous coronary intervention, PCI, sites and restenotic sites, the enzyme is detectable in the first 3 months after PCI, overview
-
ECE-1 occurs in neurons in the cerebral cortex, hippocampus, amygdala, basal forebrain nuclei, diencephalon, brain stem and cerebellar hemisphere
-
ECE-1 is secreted to the medium, ECE-1 shedding from the surface of endothelial cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
ECE-1a but not ECE-1b co-localizes with nuclear membrane markers
additional information
-
early endosomes from sequestration of recombinant somatostatin receptor subtype 2A, sst2A, in HEK-293 cells after induction by somatostatin-14 or octreotide, co-localization od ECE-1 and sst2A, overview
additional information
-
expression and localization of ECE-1 isozymes in symptomatic atherosclerotic disease and saphenous vein, overview
-
additional information
-
maintenance of cells in high glucose at 25 mM promotes relocalization of ECE-1a from the membrane to the intracellular compartment, mechanism, overview, phosphorylation might play an important role in the regulation of intracellular trafficking of ECE-1 subisoforms
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
ECE-1 inhibition causes endosomal retention of the substance P neurokinin 1 receptor, beta-arrestins, and Src, resulting in markedly sustained ERK2 activation in the cytosol and nucleus, whereas ECE-1 overexpression attenuates ERK2 activation. ECE-1 inhibition also enhances substance P-induced expression and phosphorylation of the nuclear death receptor Nur77, resulting in cell death
malfunction
-
siRNA-mediated knockdown of ECE-1 results in a significant reduction in FAK phosphorylation. Transient ECE-1 overexpression in PNT1-a cells increases FAK phosphorylation
malfunction
enzyme inhibition increases glucagon-like peptide 1-induced activation of extracellular signal-regulated kinase and generation of cAMP. Enzyme inhibition blocks resensitisation of glucagon-like peptide 1 7-36 amide-mediated Ca2+ signalling
metabolism
-
regulation of neuropeptide signaling at the cell surface involving ECE-1, detailed overview
metabolism
the enzyme regulates glucagon-like peptide-1 receptor signalling and resensitisation
physiological function
-
ECE-1 regulates the duration and subcellular location of substance P-induced, beta-arrestin-dependent ERK activation, overview
physiological function
-
involvement of ECE-1 in the development of atherosclerosis disease, overview
physiological function
-
differential degradation by ECE-1 is a novel mechanism by which corticotropin-releasing factor receptor 1 is protected from overactivation by physiologically relevant high concentrations of higher affinity ligand to mediate distinct resensitization and downstream signaling
physiological function
-
ECE-1 influences PC cell invasion via both ET-1-mediated FAK phosphorylation and ET-1 independent mechanisms
physiological function
the enzyme is a key regulator of endothelin 1-induced pruritus and neural signaling of itch
physiological function
the enzyme is involved in substance P-induced pigmentation. The enzyme is essential for endothelin 1 secretion in melanocytes
physiological function
the primary function of ECE-1 in substance P-dependent inflammatory signaling is to promote resensitization, which allows the sustained neurokinin 1 receptor signaling from the plasma membrane that drives inflammation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). EFCE2_HUMAN
883
1
99773
Swiss-Prot
other Location (Reliability: 2)
ECE1_HUMAN
770
1
87164
Swiss-Prot
Secretory Pathway (Reliability: 4)
ECE2_HUMAN
811
1
91211
Swiss-Prot
other Location (Reliability: 1)
E9PHZ1_HUMAN
134
1
14538
TrEMBL
other Location (Reliability: 3)
B4DKB2_HUMAN
738
1
83574
TrEMBL
Secretory Pathway (Reliability: 4)
A0A3B3ISF9_HUMAN
842
1
94479
TrEMBL
other Location (Reliability: 2)
A1PUP8_HUMAN
770
1
87164
TrEMBL
Secretory Pathway (Reliability: 4)
A0A024RAB2_HUMAN
767
1
87022
TrEMBL
other Location (Reliability: 3)
E9PJG1_HUMAN
77
0
8800
TrEMBL
other Location (Reliability: 1)
A0A024RAB0_HUMAN
758
1
85808
TrEMBL
Mitochondrion (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
115000
-
2 * 110000-140000, gel filtration, 2 * 115000, isoenzyme sECE, gel filtration
78000
crystallization, 680 residues of monomeric enzyme (extracellular domain, residues 90-770)
80000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
dimer
-
2 * 110000-140000, gel filtration, 2 * 115000, isoenzyme sECE, gel filtration
homodimer
forms in vivo, intra-molecular disulfide bond formed by C428, here crystallisation of monomeric mutant (extracellular domain, residues 90-770)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
isozyme ECE-1d and ECE-1e are deglycosylated by PNGase F, the truncated variant ECE-1sv, lacking the signal peptide, is not glycosylated
phosphoprotein
additional information
phosphoprotein
-
the isozymes contain a different number of putative phosphorylation sites for protein kinase C and protein kinase A in the amino-terminal region, stimulation of phosphorylation by phorbol myristate acetate, inhibition by calphostin C, phosphorylation might play an important role in the regulation of intracellular trafficking of ECE-1 subisoforms
phosphoprotein
the enzyme is phosphorylated by protein kinase C and dephosphorylated by TIMAP-protein phosphatase 1-complex
additional information
intra-molecular disulfide bond formed by C428 (homodimer)
additional information
-
intra-molecular disulfide bond formed by C428 (homodimer)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cocrystallization of C428S mutant of monomeric form (extracellular domain, residues 90-770) with inhibitor N-(alpha-L-rhamnopyranosyl-oxyhydroxy-phosphinyl)-L-Leu-L-Trp
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C338A
the mutation in isoform ECE-1b creates a new E2F-2 transcription factor binding site and enhances expression of this intracellular isoform
additional information
additional information
-
ECE-1 inhibition or knockdown traps CLR/RAMP1 and beta-arrestin2 in endosomes and inhibits CLR/RAMP1 recycling and resensitization, whereas ECE-1 overexpression has the opposite effect, overview
additional information
-
increased ECE activity in PKCepsilon-transfected EA.hy926 cells
additional information
-
the ECE encoding gene shows polymorphisms, genotyping, overview
additional information
-
overexpression of ECE-1a or 1b in CHO cells results in a 75-90% reduction in Abeta1-40 and a 45-60% reduction in Abeta1-42, completely abolished by treatment with phosphoramidon
additional information
-
the C338A polymorphism, that is located in the ECE-1 gene promoter, occurs in gene ECE-1b in carotid atherosclerosis, genotyping of a Chinese population, carotid atherosclerosis patients and healthy subjects, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cell rupture by lysozyme and continuous cell disrupter, washing of insoluble pellet
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and anaylsis, genotyping, the ECE encoding gene shows several single nucleotide polymorphisms, overview
-
expression of ECE-1 is significantly higher in the solid tumors compared with effusions
-
extracellular domain of monomeric human ECE-1 (C428S) mutant (Q90-W770) is amplified by PCR and produced recombinantly in Escherichia coli (inclusion bodies)
isozyme genetic structure, overview, expression of wild-type isozyme ECE-1d and of truncated variant ECE-1sv lacking the signal peptide, expression analysis of isozymes and splicing variants, overview
-
overexpression of GFP-tagged isozymes in HEK cell endosomes, subcellular localization, overview
-
sECE, constructed by fusing the cleavable signal peptide of pro-opiomelanocortin in frame to complete extracellular domain of ECE-1, expressed in CHO cells
-
solECE-1 constructed by fusing the cleavable N-terminalsignal sequence of human alkaline phosphatase in frame with the entire extracellular domain of ECE-1, transfected into CHO-K1 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
alternative polyadenylation results in the production of enzyme transcripts with truncated 3'-untranslated regions which promote elevated protein expression
siRNA-mediated knockdown of ECE-1 results in a significant reduction in FAK phosphorylation
-
the enzyme expression is markedly inhibited by its 3'-untranslated region
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
inclusion bodies solubilized in Tris-HCl, urea, beta-mercaptoethanol, dithiotreithol, glutathione, glycine
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
medicine
drug development
-
ECE-1 is a potential target for the treatment of Alzheimers disease based on its role in amyloid-beta peptide degradation
drug development
-
ECE-1 silencing (RNAi) may be a promising ovarian carcinoma anticancer therapy
drug development
-
Inhibition of endothelin-1 production by ECE-1 is a promising target for the treatment of cardiovascular disease, but lack of substrate specificity is disadvantageous since inhibition of ECE-1 has impact on other pathways too
drug development
-
mixed ACE/ECE-1 inhibitor may lead to vasopeptide inhibitors that can reduce the levels of angiotensin-II and endothelin-1, without interfering with bradykinin cleavage
medicine
-
design of new potent and selective inhibitors might eventually lead to drugs against hypertension
medicine
-
elevated plasma levels of endothelin-1 found in several diseases like asthma, hypertension, cerebral vacospasm, congestive heart failure and chronic and acute renal failure, blockade of the ET-1 system could have therapeutic utility
medicine
-
analysis of effect of various ECE inhibitors in myocardial infarction, pulmonary hypertension, arterial hypertension. Overview is given on human studies
medicine
high enzyme expression independently predicts poor survival of patients with esophageal squamous cell carcinoma
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ahn, K.; Herman, S.B.; Fahnoe, D.C.
Soluble human endothelin-converting enzyme-1: expression, purification, and demonstration of pronounced pH sensitivity
Arch. Biochem. Biophys.
359
258-268
1998
Homo sapiens
Cronin, N.B.; Wallace, B.A.
Do the structures of big ET-1 and big ET-3 adopt a similar overall fold? Consequences for endothelin converting enzyme specificity
Biochemistry
38
1721-1726
1999
Homo sapiens
Korth, P.; Egidy, G.; Parnot, C.; LeMoullec, J.M.; Corvol, P.; Pinet, F.
Construction, expression and characterization of a soluble form of human endothelin-converting-enzyme-1
FEBS Lett.
417
365-370
1997
Homo sapiens
Wallace, E.M.; Moliterni, J.A.; Moskal, M.A.; Neubert, A.D.; Marcopulos, N.; Stamford, L.B.; Trapani, A.J.; Savage, P.; Chou, M.; Jeng, A.Y.
Design and synthesis of potent, selective inhibitors of endothelin-converting enzyme
J. Med. Chem.
41
1513-1523
1998
Homo sapiens
Bur, D.; Dale, G.E.; Oefner, C.
A three-dimensional model of endothelin-converting enzyme (ECE) based on the X-ray structure of neutral endopeptidase 24.11 (NEP)
Protein Eng.
14
337-341
2001
Homo sapiens
Brands, M.; Ergueden, J.K.; Hashimoto, K.; Heimbach, D.; Schroeder, C.; Siegel, S.; Stasch, J.P.; Weigand, S.
Novel, selective indole-based ECE inhibitors: lead optimization via solid-phase and classical synthesis
Bioorg. Med. Chem. Lett.
15
4201-4205
2005
Homo sapiens
Awano, S.; Dawson, L.A.; Hunter, A.R.; Turner, A.J.; Usmani, B.A.
Endothelin system in oral squamous carcinoma cells: specific siRNA targeting of ECE-1 blocks cell proliferation
Int. J. Cancer
118
1645-1652
2006
Homo sapiens
Gokhale, N.H.; Cowan, J.A.
Metallopeptide-promoted inactivation of angiotensin-converting enzyme and endothelin-converting enzyme 1: Toward dual-action therapeutics
J. Biol. Inorg. Chem.
11
937-947
2006
Homo sapiens
Trapani, A.J.; Beil, M.E.; Bruseo, C.W.; Savage, P.; Firooznia, F.; Jeng, A.Y.
CGS 35601 and its orally active prodrug CGS 37808 as triple inhibitors of endothelin-converting enzyme-1, neutral endopeptidase 24.11, and angiotensin-converting enzyme
J. Cardiovasc. Pharmacol.
44
S211-S215
2004
Homo sapiens
-
Berger, Y.; Dehmlow, H.; Blum-Kaelin, D.; Kitas, E.A.; Loeffler, B.M.; Aebi, J.D.; Juillerat-Jeanneret, L.
Endothelin-converting enzyme-1 inhibition and growth of human glioblastoma cells
J. Med. Chem.
48
483-498
2005
Homo sapiens
Dibas, A.; Prasanna, G.; Yorio, T.
Characterization of endothelin-converting enzyme activities in ARPE-19 cells, a human retinal pigmented epithelial cell line
J. Ocul. Pharmacol. Ther.
21
196-204
2005
Homo sapiens
Hanessian, S.; Gauchet, C.; Charron, G.; Marin, J.; Nakache, P.
Design and synthesis of diversely substituted azacyclic inhibitors of endothelin converting enzyme
J. Org. Chem.
71
2760-2778
2006
Homo sapiens
Klipper, E.; Gilboa, T.; Levy, N.; Kisliouk, T.; Spanel-Borowski, K.; Meidan, R.
Characterization of endothelin-1 and nitric oxide generating systems in corpus luteum-derived endothelial cells
Reproduction
128
463-473
2004
Homo sapiens
Smollich, M.; Goette, M.; Yip, G.W.; Yong, E.S.; Kersting, C.; Fischgraebe, J.; Radke, I.; Kiesel, L.; Wuelfing, P.
On the role of endothelin-converting enzyme-1 (ECE-1) and neprilysin in human breast cancer
Breast Cancer Res. Treat.
106
361-369
2007
Homo sapiens
Roosterman, D.; Kempkes, C.; Cottrell, G.S.; Padilla, B.E.; Bunnett, N.W.; Turck, C.W.; Steinhoff, M.
Endothelin-converting enzyme-1 degrades internalized somatostatin-14
Endocrinology
149
2200-2207
2008
Homo sapiens
Fisk, L.; Nalivaeva, N.N.; Turner, A.J.
Regulation of endothelin-converting enzyme-1 expression in human neuroblastoma cells
Exp. Biol. Med.
231
1048-1053
2006
Homo sapiens, Rattus norvegicus
Dawson, L.A.; Maitland, N.J.; Berry, P.; Turner, A.J.; Usmani, B.A.
Expression and localization of endothelin-converting enzyme-1 in human prostate cancer
Exp. Biol. Med.
231
1106-1110
2006
Homo sapiens
Jafri, F.; Ergul, A.
Phosphorylation of endothelin converting enzyme-1 isoforms: relevance to subcellular localization
Exp. Biol. Med.
231
713-717
2006
Homo sapiens
Hunter, A.R.; Turner, A.J.
Expression and localization of endothelin-converting enzyme-1 isoforms in human endothelial cells
Exp. Biol. Med.
231
718-722
2006
Homo sapiens
Klipper, E.; Levy, N.; Gilboa, T.; Muller, L.; Meidan, R.
Identification of a novel alternatively spliced variant endothelin converting enzyme-1 lacking a transmembrane domain
Exp. Biol. Med.
231
723-728
2006
Homo sapiens
Jackson, C.D.; Barnes, K.; Homer-Vanniasinkam, S.; Turner, A.J.
Expression and localization of human endothelin-converting enzyme-1 isoforms in symptomatic atherosclerotic disease and saphenous vein
Exp. Biol. Med.
231
794-801
2006
Homo sapiens
Kuruppu, S.; Reeve, S.; Ian Smith, A.
Characterisation of endothelin converting enzyme-1 shedding from endothelial cells
FEBS Lett.
581
4501-4506
2007
Homo sapiens
Massai, L.; Volpi, N.; Carbotti, P.; Fruschelli, M.; Mencarelli, M.; Pecorelli, A.; Muscettola, M.; Agliano, M.; Alessandrini, C.; Grasso, G.
Endothelin-1 and endothelin-converting enzyme-1 in human granulomatous pathology of eyelid: an immunohistochemical and in situ hybridization study in chalazia
Histol. Histopathol.
22
1343-1354
2007
Homo sapiens
Padilla, B.E.; Cottrell, G.S.; Roosterman, D.; Pikios, S.; Muller, L.; Steinhoff, M.; Bunnett, N.W.
Endothelin-converting enzyme-1 regulates endosomal sorting of calcitonin receptor-like receptor and beta-arrestins
J. Cell Biol.
179
981-997
2007
Homo sapiens
Suekane, T.; Ikura, Y.; Arimoto, J.; Nakagawa, M.; Kitabayashi, C.; Naruko, T.; Watanabe, T.; Fujiwara, Y.; Oshitani, N.; Maeda, K.; Tanzawa, K.; Hirakawa, K.; Arakawa, T.; Ueda, M.
Enhanced expressions of endothelin-converting enzyme and endothelin receptors in human colonic tissues of Crohns disease
J. Clin. Biochem. Nutr.
42
126-132
2008
Homo sapiens
Iwase, A.; Ando, H.; Nagasaka, T.; Goto, M.; Harata, T.; Kikkawa, F.
Distribution of endothelin-converting enzyme-1 and neutral endopeptidase in human endometrium
J. Histochem. Cytochem.
55
1229-1235
2007
Homo sapiens
Shirai, N.; Naruko, T.; Ohsawa, M.; Ikura, Y.; Sugama, Y.; Hirayama, M.; Kitabayashi, C.; Ehara, S.; Inoue, T.; Itoh, A.; Haze, K.; Tanzawa, K.; Yoshiyama, M.; Yoshikawa, J.; Ueda, M.
Expression of endothelin-converting enzyme, endothelin-1 and endothelin receptors at the site of percutaneous coronary intervention in humans
J. Hypertens.
24
711-721
2006
Homo sapiens
Daray, F.M.; Colombo, J.R.; Kibrik, J.R.; Errasti, A.E.; Pelorosso, F.G.; Nowak, W.; Cracowski, J.L.; Rothlin, R.P.
Involvement of endothelial thromboxane A2 in the vasoconstrictor response induced by 15-E2t-isoprostane in isolated human umbilical vein
Naunyn Schmiedebergs Arch. Pharmacol.
373
367-375
2006
Homo sapiens
Buehler, K.; Ufer, M.; Mueller-Marbach, A.; Brinkmann, U.; Laule, M.; Stangl, V.; Roots, I.; Stangl, K.; Cascorbi, I.
Risk of coronary artery disease as influenced by variants of the human endothelin and endothelin-converting enzyme genes
Pharmacogenet. Genomics
17
77-83
2007
Homo sapiens
Choi, D.S.; Wang, D.; Yu, G.Q.; Zhu, G.; Kharazia, V.N.; Paredes, J.P.; Chang, W.S.; Deitchman, J.K.; Mucke, L.; Messing, R.O.
PKCepsilon increases endothelin converting enzyme activity and reduces amyloid plaque pathology in transgenic mice
Proc. Natl. Acad. Sci. USA
103
8215-8220
2006
Homo sapiens, Mus musculus
Keeble, J.E.
Re-sensitization of neuropeptide receptors: should we stop the recycling?
Br. J. Pharmacol.
156
728-729
2009
Homo sapiens
Cattaruzza, F.; Cottrell, G.S.; Vaksman, N.; Bunnett, N.W.
Endothelin-converting enzyme 1 promotes re-sensitization of neurokinin 1 receptor-dependent neurogenic inflammation
Br. J. Pharmacol.
156
730-739
2009
Homo sapiens, Rattus norvegicus
Rayhman, O.; Klipper, E.; Muller, L.; Davidson, B.; Reich, R.; Meidan, R.
Small interfering RNA molecules targeting endothelin-converting enzyme-1 inhibit endothelin-1 synthesis and the invasive phenotype of ovarian carcinoma cells
Cancer Res.
68
9265-9273
2008
Homo sapiens
Peltonen, T.; Taskinen, P.; Naepaenkangas, J.; Leskinen, H.; Ohtonen, P.; Soini, Y.; Juvonen, T.; Satta, J.; Vuolteenaho, O.; Ruskoaho, H.
Increase in tissue endothelin-1 and ETA receptor levels in human aortic valve stenosis
Eur. Heart J.
30
242-249
2009
Homo sapiens
Martinez-Miguel, P.; Raoch, V.; Zaragoza, C.; Valdivielso, J.M.; Rodriguez-Puyol, M.; Rodriguez-Puyol, D.; Lopez-Ongil, S.
Endothelin-converting enzyme-1 increases in atherosclerotic mice: potential role of oxidized low density lipoproteins
J. Lipid Res.
50
364-375
2009
Bos taurus, Homo sapiens, Mus musculus, Mus musculus C57/BL6J
Schulz, H.; Dale, G.E.; Karimi-Nejad, Y.; Oefner, C.
Structure of human endothelin-converting enzyme I complexed with phosphoramidon
J. Mol. Biol.
385
178-187
2009
Homo sapiens (P42892), Homo sapiens
Cerdeira, A.S.; Bras-Silva, C.; Leite-Moreira, A.F.
Endothelin-converting enzyme inhibitors: their application in cardiovascular diseases
Rev. Port. Cardiol.
27
385-408
2008
Bos taurus, Homo sapiens, Rattus norvegicus, Sus scrofa, Cavia sp.
Cottrell, G.S.; Padilla, B.E.; Amadesi, S.; Poole, D.P.; Murphy, J.E.; Hardt, M.; Roosterman, D.; Steinhoff, M.; Bunnett, N.W.
Endosomal endothelin-converting enzyme-1: a regulator of beta-arrestin-dependent ERK signaling
J. Biol. Chem.
284
22411-22425
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Jullien, N.; Makritis, A.; Georgiadis, D.; Beau, F.; Yiotakis, A.; Dive, V.
Phosphinic tripeptides as dual angiotensin-converting enzyme C-domain and endothelin-converting enzyme-1 inhibitors
J. Med. Chem.
53
208-220
2010
Homo sapiens
Jin, Z.; Luxiang, C.; Huadong, Z.; Zhiqiang, X.; Lihua, H.; Huiyun, L.
C-338A polymorphism of the endothelin-converting enzyme-1 gene and the susceptibility to carotid atherosclerosis
Microvasc. Res.
78
128-131
2009
Homo sapiens
Palmer, J.C.; Kehoe, P.G.; Love, S.
Endothelin-converting enzyme-1 in Alzheimers disease and vascular dementia
Neuropathol. Appl. Neurobiol.
36
487-497
2010
Homo sapiens
Whyteside, A.R.; Hinsley, E.E.; Lambert, L.A.; McDermott, P.J.; Turner, A.J.
ECE-1 influences prostate cancer cell invasion via ET-1-mediated FAK phosphorylation and ET-1-independent mechanisms
Can. J. Physiol. Pharmacol.
88
850-854
2010
Homo sapiens
Wang, S.; Wang, R.; Chen, L.; Bennett, D.A.; Dickson, D.W.; Wang, D.S.
Expression and functional profiling of neprilysin, insulin-degrading enzyme, and endothelin-converting enzyme in prospectively studied elderly and Alzheimers brain
J. Neurochem.
115
47-57
2010
Homo sapiens
Hasdemir, B.; Mahajan, S.; Bunnett, N.W.; Liao, M.; Bhargava, A.
Endothelin-Converting Enzyme-1 Actions Determine Differential Trafficking and Signaling of Corticotropin-Releasing Factor Receptor 1 at High Agonist Concentrations
Mol. Endocrinol.
26
681-695
2012
Homo sapiens
Sonawane, K.; Barage, S.
Structural analysis of membrane-bound hECE-1 dimer using molecular modeling techniques: insights into conformational changes and Abeta1-42 peptide binding
Amino Acids
47
543-559
2015
Homo sapiens (P42892), Homo sapiens
Pacheco-Quinto, J.; Herdt, A.; Eckman, C.; Eckman, E.
Endothelin-converting enzymes and related metalloproteases in Alzheimer's disease
J. Alzheimers Dis.
33
S101
2013
Homo sapiens (P42892)
Jensen, D.; Halls, M.; Murphy, J.; Canals, M.; Cattaruzza, F.; Poole, D.; Lieu, T.; Koon, H.; Pothoulakis, C.; Bunnett, N.
Endothelin-converting enzyme 1 and beta-arrestins exert spatiotemporal control of substance P-induced inflammatory signals
J. Biol. Chem.
289
20283-20294
2014
Homo sapiens (P42892), Homo sapiens
Kido-Nakahara, M.; Buddenkotte, J.; Kempkes, C.; Ikoma, A.; Cevikbas, F.; Akiyama, T.; Nunes, F.; Seeliger, S.; Hasdemir, B.; Mess, C.; Buhl, T.; Sulk, M.; Mller, F.; Metze, D.; Bunnett, N.; Bhargava, A.; Carstens, E.; Furue, M.; Steinhoff, M.
Neural peptidase endothelin-converting enzyme 1 regulates endothelin 1-induced pruritus
J. Clin. Invest.
124
2683-2695
2014
Homo sapiens (P42892), Homo sapiens, Mus musculus (Q4PZA2), Mus musculus
Park, P.; Lee, T.; Cho, E.
Substance P stimulates endothelin 1 secretion via endothelin-converting enzyme 1 and promotes melanogenesis in human melanocytes
J. Invest. Dermatol.
135
551-559
2015
Homo sapiens (P42892), Homo sapiens
Tanneeru, K.; Sahu, I.; Guruprasad, L.
Ligand-based drug design for human endothelin converting enzyme-1 inhibitors
Med. Chem. Res.
22
4401-4409
2013
Homo sapiens (P42892)
-
Kuruppu, S.; Chou, S.; Feske, S.; Suh, S.; Hanchapola, I.; Lo, E.; Ning, M.; Smith, A.
Soluble and catalytically active endothelin converting enzyme-1 is present in cerebrospinal fluid of subarachnoid hemorrhage patients
Mol. Cell. Proteomics
13
1091-1094
2014
Homo sapiens (P42892), Homo sapiens
Whyteside, A.; Turner, A.; Lambert, D.
Endothelin-converting enzyme-1 (ECE-1) is post-transcriptionally regulated by alternative polyadenylation
PLoS ONE
9
e83260
2014
Homo sapiens (P42892)
Lu, J.; Willars, G.B.
Endothelin-converting enzyme-1 regulates glucagon-like peptide-1 receptor signalling and resensitisation
Biochem. J.
476
513-533
2019
Homo sapiens (P42892), Homo sapiens
Boratko, A.; Vereb, Z.; Petrovski, G.; Csortos, C.
TIMAP-protein phosphatase 1-complex controls endothelin-1 production via ECE-1 dephosphorylation
Int. J. Biochem. Cell Biol.
73
11-18
2016
Homo sapiens (P42892)
Smith, A.I.; Rajapakse, N.W.; Kleifeld, O.; Lomonte, B.; Sikanyika, N.L.; Spicer, A.J.; Hodgson, W.C.; Conroy, P.J.; Small, D.H.; Kaye, D.M.; Parkington, H.C.; Whisstock, J.C.; Kuruppu, S.
N-terminal domain of Bothrops asper myotoxin II enhances the activity of endothelin converting enzyme-1 and neprilysin
Sci. Rep.
6
22413
2016
Homo sapiens (P42892)
Wu, C.F.; Lee, C.T.; Kuo, Y.H.; Chen, T.H.; Chang, C.Y.; Chang, I.W.; Wang, W.L.
High endothelin-converting enzyme-1 expression independently predicts poor survival of patients with esophageal squamous cell carcinoma
Tumor Biol.
39
1010428317725922
2017
Homo sapiens (P42892), Homo sapiens
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