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Information on EC 3.3.2.10 - soluble epoxide hydrolase and Organism(s) Homo sapiens and UniProt Accession P34913
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3.3.2.10 soluble epoxide hydrolaseIUBMB Comments
Catalyses the hydrolysis of trans-substituted epoxides, such as trans-stilbene oxide, as well as various aliphatic epoxides derived from fatty-acid metabolism . It is involved in the metabolism of arachidonic epoxides (epoxyicosatrienoic acids; EETs) and linoleic acid epoxides. The EETs, which are endogenous chemical mediators, act at the vascular, renal and cardiac levels to regulate blood pressure [4,5]. The enzyme from mammals is a bifunctional enzyme: the C-terminal domain exhibits epoxide-hydrolase activity and the N-terminal domain has the activity of EC 3.1.3.76, lipid-phosphate phosphatase [1,2]. Like EC 3.3.2.9, microsomal epoxide hydrolase, it is probable that the reaction involves the formation of an hydroxyalkyl---enzyme intermediate [4,6]. The enzyme can also use leukotriene A4, the substrate of EC 3.3.2.6, leukotriene-A4 hydrolase, but it forms 5,6-dihydroxy-7,9,11,14-icosatetraenoic acid rather than leukotriene B4 as the product [9,10]. In vertebrates, five epoxide-hydrolase enzymes have been identified to date: EC 3.3.2.6 (leukotriene-A4 hydrolase), EC 3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal epoxide hydrolase), EC 3.3.2.10 (soluble epoxide hydrolase) and EC 3.3.2.11 (cholesterol 5,6-oxide hydrolase) .
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Word Map
- 3.3.2.10
-
epoxyeicosatrienoic
-
arachidonic
- diol
- s-transferase
- hydrolases
- hypertension
-
benzoapyrene
- epoxygenase
- styrene
-
dihydroxyeicosatrienoic
-
enantioselectivity
- phenobarbital
-
dhets
- trans-stilbene
-
leukotriene
-
eicosanoids
-
drug-metabolizing
- cyp1a1
- 3-methylcholanthrene
-
o-deethylase
- oxylipins
-
xenobiotic-metabolizing
-
dihydrodiols
-
enantiopure
-
ethoxyresorufin
- lta4
-
glycidyl
- arene
-
urea-based
- cyclohexene
-
ethoxycoumarin
- medicine
- beta-naphthoflavone
-
oxirane
-
20-hydroxyeicosatetraenoic
-
udp-glucuronyltransferase
- 20-hete
- cyp2j2
-
udp-glucuronosyl
- 1-naphthol
- aminopyrine
-
edhfs
- analysis
- radiobacter
-
3-methylcholanthrene-treated
- butadiene
-
udpgt
-
hydroxyeicosatetraenoic
- epichlorohydrin
- aldrin
- synthesis
-
pentoxyresorufin
- drug development
- agriculture
-
adamantyl
- pharmacology
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
epoxide hydrolase, soluble epoxide hydrolase, ephx2, cytosolic epoxide hydrolase, epoxide hydrolase 1, epoxide hydrolase 2, ephx3, teso hydrolase, hepoxilin hydrolase, epoxide hydrolase-3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SEH
SEH
additional information
SEH
-
663350, 699541, 707633, 707669, 707676, 707679, 707681, 708017, 708238, 708395, 708573, 709061, 709447, 709448, 709452, 709564, 709899, 710044, 710480, 731473, 731476, 731877, 732124, 732298, 732314, 752593, 752734, 752930, 752944, 752977, 753330, 753841, 753858, 754366, 754381, 754798, 755389, 755394, 755396
SEH
-
-
SEH
-
sEH is a bifunctional enzyme with two catalytic domains: a C-terminal epoxide hydrolase domain and an N-terminal phosphatase domain
SEH
-
the enzyme plays an important role in the regulation of blood pressure and inflammation
additional information
-
the enzyme belongs to the alpha/beta-hydrolase fold family of proteins
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an epoxide + H2O = a glycol
the C-terminal part harbors the epoxide hydrolase activity, the phosphatase activity of the enzyme is located at the N-terminal part of EC 3.1.3.76, both catalytic sites act independently, the epoxide hydrolase reaction proceeds though an alkyl-enzyme intermediate involving the catalytic Asp333, and hydrogen bonds with Tyr381 and Tyr465, reaction mechanism, structure-mechanism relationship
an epoxide + H2O = a glycol
the C-terminal part harbors the epoxide hydrolase activity, the phosphatase activity of the enzyme is located at the N-terminal part of EC 3.1.3.76, both catalytic sites act independently
-
an epoxide + H2O = a glycol
two step mechanism with formation of of a hydroxyl-alkyl-enzyme intermediate, the catalytic triad is Asp334-His523-Asp495 with polarizing residues Tyr382 and Tyr465, catalytic cycle
-
an epoxide + H2O = a glycol
the catalytic mechanism involves two step processes, overview
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
epoxide hydrolase
Catalyses the hydrolysis of trans-substituted epoxides, such as trans-stilbene oxide, as well as various aliphatic epoxides derived from fatty-acid metabolism [7]. It is involved in the metabolism of arachidonic epoxides (epoxyicosatrienoic acids; EETs) and linoleic acid epoxides. The EETs, which are endogenous chemical mediators, act at the vascular, renal and cardiac levels to regulate blood pressure [4,5]. The enzyme from mammals is a bifunctional enzyme: the C-terminal domain exhibits epoxide-hydrolase activity and the N-terminal domain has the activity of EC 3.1.3.76, lipid-phosphate phosphatase [1,2]. Like EC 3.3.2.9, microsomal epoxide hydrolase, it is probable that the reaction involves the formation of an hydroxyalkyl---enzyme intermediate [4,6]. The enzyme can also use leukotriene A4, the substrate of EC 3.3.2.6, leukotriene-A4 hydrolase, but it forms 5,6-dihydroxy-7,9,11,14-icosatetraenoic acid rather than leukotriene B4 as the product [9,10]. In vertebrates, five epoxide-hydrolase enzymes have been identified to date: EC 3.3.2.6 (leukotriene-A4 hydrolase), EC 3.3.2.7 (hepoxilin-epoxide hydrolase), EC 3.3.2.9 (microsomal epoxide hydrolase), EC 3.3.2.10 (soluble epoxide hydrolase) and EC 3.3.2.11 (cholesterol 5,6-oxide hydrolase) [7].
CAS REGISTRY NUMBER
COMMENTARY
9048-63-9
-
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
(1S,2S)-beta-methylstyrene oxide + H2O
?
enzyme attacks almost exclusively at the benzylic position
-
-
?
(5Z,11Z,14Z)-8,9-epoxyeicosatrienoic acid + H2O
(5Z,11Z,14Z)-8,9-dihydroxyeicosatrienoic acid
(5Z,8Z)-N-((2-methoxy-4-(3-(trifluoromethyl)-3H-diazirin-3-yl)phenyl)sulfonyl)-10-(3-((Z)-oct-2-en-1-yl)oxiran-2-yl)deca-5,8-dienamide + H2O
?
-
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosa-5,8,11-trienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosa-5,8,11-trienoic acid
binding structure in the active site, docking analysis and molecular dynamics simulations
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
(5Z,8Z,11Z)-N-((2-methoxy-4-(3-(trifluoromethyl)-3H-diazirin-3-yl)phenyl) sulfonyl)-13-(3-pentyloxiran-2-yl)trideca-5,8,11-trienamide + H2O
?
-
-
-
?
(5Z,8Z,14Z)-11,12-epoxyeicosatrienoic acid + H2O
(5Z,8Z,14Z)-11,12-dihydroxyeicosatrienoic acid
(8Z,11Z,14Z)-5,6-epoxyeicosatrienoic acid + H2O
(8Z,11Z,14Z)-5,6-dihydroxyeicosatrienoic acid
(S)-styrene oxide + H2O
1-phenylethane-1,2-diol
preferred attack at the benzylic position
-
-
?
11,12-epoxy-eicosatrienoic acid + H2O
11,12-dihydroxy-eicosatrienoic acid
-
-
-
?
14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoic acid + H2O
14,15-dihydroxyeicosatrienoic acid
-
-
-
?
14,15-epoxyeicosatrienoic acid + H2O
14,15-dihydroxyeicosatrienoic acid
-
-
-
?
14S,15R-epoxy-eicosatrienoic acid + H2O
14S,15R-dihydroxy-eicosatrienoic acid
-
-
-
?
3-phenyl-cyano(6-methoxy-2-naphthalenyl)methyl ester-2-oxiraneacetic acid + H2O
6-methoxy-2-naphtaldehyde + ?
-
-
-
?
3-phenyl-cyano(6-methoxy-2-naphthalenyl)methyl ester-2-oxiraneacetic acid + H2O
6-methoxy-2-naphthaldehyde + ?
fluorometric activity assay substrate
-
-
?
3-phenyl-cyano(6-methoxy-2-naphthalenyl)methyl ester-2-oxiraneacetic acid + H2O
?
-
-
-
?
3-phenyl-cyano-(6-methoxy-2-naphthalenyl)methylester-2-oxirane-acetic acid + H2O
6-methoxynaphtaldehyde + ?
the non-fluorescent substrate can be hydrolyzed by enzyme sEH to the fluorescent 6-methoxynaphtaldehyde
-
-
?
3-phenylcyano-(6-methoxy-2-naphthalenyl)methyl ester 2-oxiraneacetic acid + H2O
?
-
-
-
?
6,8-difluoro-4-methylumbelliferyl trans-2,3-epoxy-3-phenylpropylcarbonate + H2O
?
-
-
-
?
9R,10R-trans-epoxy-13R-hydroxy-11E-octadecenoic acid + H2O
(9R,10S,13R)-trihydroxy-11E-octadecenoic acid
-
-
-
?
9R,10S-cis-epoxy-13R-hydroxy-11E-octadecenoic acid
(9R,10R,13R)-trihydroxy-11E-octadecenoic acid
-
-
-
?
9R,10S-cis-epoxy-13R-hydroxy-11E-octadecenoic acid + H2O
(9R,10R,13R)-trihydroxy-11E-octadecenoic acid
-
-
-
?
cis-14,15-epoxyeicosatrienoic acid + H2O
?
simulation of substrate binding, modeling
-
-
?
cis-14,15-epoxyeicosatrienoic acid + H2O
cis-14,15-dihydroxyeicosatrienoic acid
-
-
-
?
cyano(2-methoxynaphthalen-6-yl)methyl trans-(3-phenyl-oxiran-2-yl)methyl carbonate + H2O
?
a fluorogenic substrate
-
-
?
cyano(2-methoxynaphthalen-6-yl)methyl trans-(3-phenyloxyran-2-yl)methylcarbonate + H2O
6-methoxy-2-naphthaldehyde + ?
fluorometric activity assay substrate
-
-
?
cyano(6-methoxy-naphthalen-2-yl)methyl trans-[(3-phenyloxiran-2-yl)methyl] carbonate + H2O
?
i.e. CMNPC, a fluorescent substrate
-
-
?
cyano-(2-methoxynaphthalen-6-yl)-methyl trans-(3-phenyl-oxiran-2-yl)-methyl carbonate + H2O
?
Epoxy Fluor 7 + H2O
?
i.e. cyano(6-methoxy-2-naphthalenyl)methyl[(2,3)-3-phenyloxiranyl]methyl ester
-
-
?
epoxyeicosatrienoic acid + H2O
dihydroxyeicosatrienoic acid
-
-
-
?
trans-1,3-diphenylpropene oxide + H2O
trans-1,3-diphenylpropane-1,2-diol
-
-
-
?
(10R)-hydroxy-(11S,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoic acid + H2O
(10R,11R,12S)-trihydroxy-(5Z,8Z,14Z)-eicosatrienoic acid
-
i.e. hepoxilin B3
-
-
?
(3-phenyl-oxiranyl)-acetic acid cyano-(6-methoxy-naphthalen-2-yl)-methyl ester + H2O
6-methoxy-2-naphthaldehyde + ?
-
substrate for high-throughput screen
product is fluorescent
-
?
(3-phenyl-oxiranyl)-acetic acid cyano-(6-methoxynaphthalen-2-yl)-methyl ester + H2O
6-methoxy-2-naphthaldehyde + ?
-
-
-
-
?
(5Z,11Z,14Z)-8,9-epoxyeicosa-5,11,14-trienoic acid + H2O
(5Z,11Z,14Z)-8,9-dihydroxyeicosa-5,11,14-trienoic acid
-
i.e. 8,9-EET
i.e. 8,9-DHET
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosa-5,8,11-trienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosa-5,8,11-trienoic acid
-
i.e. 14,15-EET
i.e. 14,15-DHET
-
?
(5Z,8Z,14Z)-11,12-epoxyeicosa-5,8,14-trienoic acid + H2O
(5Z,8Z,14Z)-11,12-dihydroxyeicosa-5,8,14-trienoic acid
-
i.e. 11,12-EET
i.e. 11,12-DHET
-
?
(8R)-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoic acid + H2O
(8R,11R,12S)-trihydroxy-(5Z,9E,14Z)-eicosatrienoic acid
-
i.e. hepoxilin A3, hydrolysis in liver is mainly catalyzed by soluble epoxide hydrolase
-
-
?
(8Z,11Z,14Z)-5,6-epoxyeicosa-8,11,14-trienoic acid + H2O
(8Z,11Z,14Z)-5,6-dihydroxyeicosa-8,11,14-trienoic acid
-
i.e. 5,6-EET
i.e. 5,6-DHET
-
?
1,2,3,4,9,9-hexachloro-6,7-epoxy-1,4,41,5,6,7,8,8a-octahydro-1,4-methanonaphthalene + H2O
?
-
i.e. HEOM
-
-
?
11,12-epoxyeicosatrienoic acid + H2O
11,12-dihydroxyeicosatrienoic acid
-
-
-
-
?
12-phosphonooxyoctadec-9E-enoic acid + H2O
(9E)-octadecenoic acid + phosphate
-
-
-
-
?
12-phosphonooxyoctadec-9Z-enoic acid + H2O
(9Z)-octadecenoic acid + phosphate
-
-
-
-
?
14,15-epoxyeicosatrienoic acid + H2O
14,15-dihydroxyeicosatrienoic acid
-
-
-
-
?
3-phenyl-cyano(6-methoxy-2-naphthalenyl)methyl ester-2-oxiraneacetic acid + H2O
6-methoxynaphthaldehyde + ?
-
-
-
-
?
4-nitrophenyl (2R,3R)-2,3-epoxy-3-phenylpropyl carbonate + H2O
?
-
14.6% of the activity with 2,3-epoxy-1,3-diphenyl-propane, no activity with the 2S,3S-enantiomer
-
-
?
4-nitrophenyl-trans-2,3-epoxy-3-phenylpropyl carbonate + H2O
?
-
-
-
-
?
9R,10R-trans-epoxy-13R-hydroxy-11E-octadecenoic acid + H2O
(9R,10S,13R)-trihydroxy-11E-octadecenoic acid
-
-
-
?
9R,10S-cis-epoxy-13R-hydroxy-11E-octadecenoic acid
(9R,10R,13R)-trihydroxy-11E-octadecenoic acid
-
-
-
?
9R,10S-cis-epoxy-13R-hydroxy-11E-octadecenoic acid + H2O
(9R,10R,13R)-trihydroxy-11E-octadecenoic acid
-
-
-
?
cis-1,3-diphenylpropene oxide + H2O
?
-
18.1% of the activity with 2,3-epoxy-1,3-diphenyl-propane
-
-
?
cis-14,15-epoxyeicosatrienoic acid + H2O
cis-14,15-dihydroxyeicosatrienoic acid
-
-
-
?
cis-9,10-epoxy-12-octadecenoate methyl ester + H2O
?
-
5.2% of the activity with 2,3-epoxy-1,3-diphenyl-propane
-
-
?
cis-9,10-epoxystearic acid + H2O
?
-
7.9% of the activity with 2,3-epoxy-1,3-diphenyl-propane
-
-
?
cyano(2-methoxy-naphthalen-6-yl)methyl trans-2-(3-propyloxiran-2-yl) acetate + H2O
6-methoxy-2-naphthaldehyde + CN- + ?
-
-
-
-
?
cyano(2-methoxynaphthalen-6-yl)methyl trans-(3-phenyloxiran-2-yl)methylcarbonate + H2O
?
-
-
-
-
?
cyano(2-methoxynaphthalen-6-yl)methyl trans-(3-phenyloxyran-2-yl)methyl carbonate + H2O
?
-
-
-
-
?
cyano(6-methoxy-2-naphthyl)methyl (3,3-dimethyloxiran-2-yl)methyl carbonate + H2O
6-methoxy-2-naphthaldehyde + CN- + ?
-
-
-
-
?
cyano(6-methoxy-2-naphthyl)methyl (3-ethyloxiran-2-yl)methyl carbonate + H2O
6-methoxy-2-naphthaldehyde + CN- + ?
-
-
-
-
?
cyano(6-methoxy-2-naphthyl)methyl (3-phenyloxiran-2-yl)acetate + H2O
6-methoxy-2-naphthaldehyde + CN- + ?
-
-
-
-
?
cyano(6-methoxy-2-naphthyl)methyl (3-phenyloxiran-2-yl)methyl carbonate + H2O
6-methoxy-2-naphthaldehyde + CN- + ?
-
preferred fluorogenic substrate
-
-
?
cyano(6-methoxy-2-naphthyl)methyl (3-propyloxiran-2-yl)methyl carbonate + H2O
6-methoxy-2-naphthaldehyde + CN- + ?
-
-
-
-
?
cyano(6-methoxy-2-naphthyl)methyl [3-(4-nitrophenyl)oxiran-2-yl]methyl carbonate + H2O
6-methoxy-2-naphthaldehyde + CN- + ?
-
-
-
-
?
cyano(6-methoxynaphthalen-2-yl)methyl (3-phenyloxiran-2-yl)acetate + H2O
[1,2-dihydroxy-2-(3-phenyloxiran-2-yl)ethoxy](6-methoxynaphthalen-2-yl)acetonitrile
-
-
-
-
?
erythro-10-hydroxy-9-phosphonooxy-octadecanoic acid + H2O
10-hydroxy-octadecanoic acid + phosphate
-
-
-
-
?
juvenile hormone III + H2O
?
-
6.3% of the activity with 2,3-epoxy-1,3-diphenyl-propane
-
-
?
racemic 4-nitrophenyl-trans-2,3-epoxy-3-phenylpropyl carbonate + H2O
?
-
-
-
-
?
threo-10-hydroxy-9-phosphonooxy-octadecanoic acid + H2O
10-hydroxy-octadecanoic acid + phosphate
-
-
-
-
?
trans-1,2-dimethylstyrene oxide + H2O
?
-
hydration by microsomal enzyme, no activity with cytosolic enzyme
-
-
?
[3-(4-chlorophenyl)oxiran-2-yl]methyl cyano(6-methoxy-2-naphthyl)methyl carbonate + H2O
6-methoxy-2-naphthaldehyde + CN- + ?
-
-
-
-
?
(5Z,11Z,14Z)-8,9-epoxyeicosatrienoic acid + H2O
(5Z,11Z,14Z)-8,9-dihydroxyeicosatrienoic acid
-
-
-
?
(5Z,11Z,14Z)-8,9-epoxyeicosatrienoic acid + H2O
(5Z,11Z,14Z)-8,9-dihydroxyeicosatrienoic acid
-
-
-
-
?
(5Z,11Z,14Z)-8,9-epoxyeicosatrienoic acid + H2O
(5Z,11Z,14Z)-8,9-dihydroxyeicosatrienoic acid
-
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
-
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
-
-
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
-
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
-
-
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
-
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
-
-
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
-
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
preferred substrate
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
i.e. EETs, showing endothelium-derived hyperpolarizing factor effects dominating in microvessels independent of nitric oxide and prostacyclin. sEH reduces the beneficial effects of EETs
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
enzyme-substrate binding, overview
-
-
?
(5Z,8Z,14Z)-11,12-epoxyeicosatrienoic acid + H2O
(5Z,8Z,14Z)-11,12-dihydroxyeicosatrienoic acid
-
-
-
?
(5Z,8Z,14Z)-11,12-epoxyeicosatrienoic acid + H2O
(5Z,8Z,14Z)-11,12-dihydroxyeicosatrienoic acid
-
-
-
-
?
(5Z,8Z,14Z)-11,12-epoxyeicosatrienoic acid + H2O
(5Z,8Z,14Z)-11,12-dihydroxyeicosatrienoic acid
-
-
-
?
(5Z,8Z,14Z)-11,12-epoxyeicosatrienoic acid + H2O
(5Z,8Z,14Z)-11,12-dihydroxyeicosatrienoic acid
preferred substrate
-
-
?
(8Z,11Z,14Z)-5,6-epoxyeicosatrienoic acid + H2O
(8Z,11Z,14Z)-5,6-dihydroxyeicosatrienoic acid
-
-
-
?
(8Z,11Z,14Z)-5,6-epoxyeicosatrienoic acid + H2O
(8Z,11Z,14Z)-5,6-dihydroxyeicosatrienoic acid
-
-
-
-
?
(8Z,11Z,14Z)-5,6-epoxyeicosatrienoic acid + H2O
(8Z,11Z,14Z)-5,6-dihydroxyeicosatrienoic acid
-
-
-
?
cyano-(2-methoxynaphthalen-6-yl)-methyl trans-(3-phenyl-oxiran-2-yl)-methyl carbonate + H2O
?
-
-
-
?
cyano-(2-methoxynaphthalen-6-yl)-methyl trans-(3-phenyl-oxiran-2-yl)-methyl carbonate + H2O
?
CMNPC, a fluorescent substrate with an epoxide group, which releases a strong fluorophore 6-methoxy-2-naphthaldehyde after hydrolysis of the epoxide
-
-
?
epoxyeicosatrienoic acid + H2O
dihydroxyeicosatrienoic acid
-
elimination of the biological effects of the substrate, involved in regulation of renal eicosanoid levels and blood pressure, mechanism
-
-
?
trans-stilbene oxide + H2O
?
-
-
-
-
?
trans-stilbene oxide + H2O
?
-
highly selective for the trans-enantiomer. 1.2% of the activity with 2,3-epoxy-1,3-diphenyl-propane
-
-
?
additional information
?
-
activity of the sEH can be regulated by the tyrosine nitration of the protein
-
-
?
additional information
?
-
-
activity of the sEH can be regulated by the tyrosine nitration of the protein
-
-
?
additional information
?
-
contribution of hydrolase and phosphatase domains in soluble epoxide hydrolase to vascular endothelial growth factor expression and cell growth, overview
-
-
?
additional information
?
-
-
contribution of hydrolase and phosphatase domains in soluble epoxide hydrolase to vascular endothelial growth factor expression and cell growth, overview
-
-
?
additional information
?
-
EETs are important regulators of cardiovascular function, of cerebral blood flow, and exhibit a wide array of potentially beneficial actions in stroke, including vasodilation, neuroprotection, promotion of angiogenesis and suppression of platelet aggregation, oxidative stress and postischemic inflammation, detailed overview
-
-
?
additional information
?
-
sEH rapidly hydrolyzes eicosatrienoic acids to their corresponding dihydroxyeicosatrienoic acid, DHET, metabolites, which, in general, are much less biologically active than eicosatrienoic acids. Cytochrome P450 epoxygenases, soluble epoxide hydrolase, and the regulation of cardiovascular inflammation, overview. functional impact of CYP epoxygenase-derived eicosatrienoic acids biosynthesis and sEH-mediated xyeicosatrienoic acids hydrolysis on key inflammatory process in the cardiovascular system
-
-
?
additional information
?
-
Vascular actions and antiinflammatory actions of epoxyeicosatrienoic acids, overview
-
-
?
additional information
?
-
development of a high throughput cell-based assay for soluble epoxide hydrolase using BacMam technology, determination of Cy3B-fluorescence labeled product Cy3B-DAE-14,15-DHET, i.e. 14-(2-[(2-([(5Z,8Z,11Z)-14,15-dihydroxy-5,8,11-icosatrienoyl]amino)ethyl)amino]-2-oxoethyl)-16,16,18,18-tetramethyl-6,7,7a,8a,9,10,16,18-octahydrobenzo[2'',3''] indolizino[8'',7'':5',6']pyrano[3',2':3,4]pyrido[1,2-a]indol-5-ium-2-sulfonate, overview
-
-
?
additional information
?
-
sEH has phosphatase activity as well as epoxide hydrolase activity
-
-
?
additional information
?
-
-
sEH has phosphatase activity as well as epoxide hydrolase activity
-
-
?
additional information
?
-
the C-terminal domain of the soluble epoxide hydrolase metabolizes epoxyeicosatrienoic acids, EETs, to their less active diols, while the N-terminal domain demonstrates lipid phosphatase activity
-
-
?
additional information
?
-
-
the C-terminal domain of the soluble epoxide hydrolase metabolizes epoxyeicosatrienoic acids, EETs, to their less active diols, while the N-terminal domain demonstrates lipid phosphatase activity
-
-
?
additional information
?
-
human soluble EH (sEH or EPHX2) and human or murine epoxide hydrolase-3 (EH3 or EPHX3) hydrolyze cis or trans allylic epoxides to single diastereomers, identical to the major isomers detected in epidermis. Microsomal EH (mEH or EPHX1, EC 3.3.2.9) is inactive with these substrates. 12,13-trans-Epoxy-octadeca-9E-enoic acid is completely hydrolyzed by human sEH, human EH3, and N-truncated murine EH3 and mostly hydrolyzed using the N-truncated+7aa-insert murine EH3. 12,13-cis-Epoxy-octadeca-9E-enoic acid is hardly hydrolyzed by human EH3, N-truncated murine EH3, and the N-truncated+7aa-insert murine EH3, and 30% hydrolysis is observed using human sEH. At low substrate concentrations, EPHX2 hydrolyzes 14,15-epoxyeicosatrienoic acid (EET) at twice the rate of the epidermal epoxyalcohol, 9R,10R-trans-epoxy-11E-13R-hydroxy-octadecenoic acid, whereas human or murine EPHX3 hydrolyze the allylic epoxyalcohol at 31fold and 39fold higher rates, respectively
-
-
?
additional information
?
-
human soluble EH (sEH or EPHX2) and human or murine epoxide hydrolase-3 (EH3 or EPHX3) hydrolyze cis or trans allylic epoxides to single diastereomers, identical to the major isomers detected in epidermis. Microsomal EH (mEH or EPHX1, EC 3.3.2.9) is inactive with these substrates. 12,13-trans-Epoxy-octadeca-9E-enoic acid is completely hydrolyzed by human sEH, human EH3, and N-truncated murine EH3 and mostly hydrolyzed using the N-truncated+7aa-insert murine EH3. 12,13-cis-Epoxy-octadeca-9E-enoic acid is hardly hydrolyzed by human EH3, N-truncated murine EH3, and the N-truncated+7aa-insert murine EH3, and 30% hydrolysis is observed using human sEH. At low substrate concentrations, EPHX2 hydrolyzes 14,15-epoxyeicosatrienoic acid (EET) at twice the rate of the epidermal epoxyalcohol, 9R,10R-trans-epoxy-11E-13R-hydroxy-octadecenoic acid, whereas human or murine EPHX3 hydrolyze the allylic epoxyalcohol at 31fold and 39fold higher rates, respectively
-
-
?
additional information
?
-
-
human soluble EH (sEH or EPHX2) and human or murine epoxide hydrolase-3 (EH3 or EPHX3) hydrolyze cis or trans allylic epoxides to single diastereomers, identical to the major isomers detected in epidermis. Microsomal EH (mEH or EPHX1, EC 3.3.2.9) is inactive with these substrates. 12,13-trans-Epoxy-octadeca-9E-enoic acid is completely hydrolyzed by human sEH, human EH3, and N-truncated murine EH3 and mostly hydrolyzed using the N-truncated+7aa-insert murine EH3. 12,13-cis-Epoxy-octadeca-9E-enoic acid is hardly hydrolyzed by human EH3, N-truncated murine EH3, and the N-truncated+7aa-insert murine EH3, and 30% hydrolysis is observed using human sEH. At low substrate concentrations, EPHX2 hydrolyzes 14,15-epoxyeicosatrienoic acid (EET) at twice the rate of the epidermal epoxyalcohol, 9R,10R-trans-epoxy-11E-13R-hydroxy-octadecenoic acid, whereas human or murine EPHX3 hydrolyze the allylic epoxyalcohol at 31fold and 39fold higher rates, respectively
-
-
?
additional information
?
-
-
microsomal enzyme shows highest activity with trans-2-methylstyrane oxide, followed by styrene 7,8-oxide, cis-2-methylstyrene oxide, cis-1,2-dimethylstyrene oxide, trans-1,2-dimethylstyrene oxide and 2,2-dimethylstyrene oxide. With the cytosolic enzyme the same order is obtained for the first three substrates, whereas activity with 2,2-dimethylstyrene oxide is higher than with cis-1,2-dimethylstyrene oxide and no hydration occurs with trans-1,2-dimethylstyrene oxide
-
-
?
additional information
?
-
-
the N-terminal domain of the enzyme is a functional phosphatase unaffected by a number of classic phosphatase inhibitors. The phosphatase domain has high specificity for lipophilic phosphates
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of blood pressure and inflammation
-
-
?
additional information
?
-
-
reaction mechanism with flurogenic substrates
-
-
?
additional information
?
-
-
substrate specificity, 2 enzymes with different specificities termed cytosolic TESO hydrolase and cytosolic PNSO hydrolase, no activity with benz[a]pyrene 4,5-oxide
-
-
?
additional information
?
-
-
substrate specificity, the microsomal enzyme rapidly hydrolyzes epoxides on cyclic systems as well as mono, 1,1-di and cis-1,2-disubstituted epoxides
-
-
?
additional information
?
-
-
the enzyme also shows phosphatase activity, EC 3.1.3.76, sEH prefers gem-di-, trans-di-, cis-di-, tri-, and tetra-substituted epoxides
-
-
?
additional information
?
-
-
the enzyme prefers trans- over cis-epoxides of sterically hindered substrates like stilbene oxides, the C-terminal domain catalyzes epoxy fatty acid hydrolysis, the N-terminal catalytic domain has also phosphatase activity with specificity for fatty acid diol phosphates, overview
-
-
?
additional information
?
-
-
differential localization of the enzyme in the brain indicates an essential role in the central nervous system
-
-
?
additional information
?
-
-
kinetic analysis of the effects of human enzyme polymorphisms on the N-terminal phosphatase activity of soluble epoxide hydrolase activity
-
-
?
additional information
?
-
-
epoxyeicosatrienoic acids are substrates of sEH, enzyme regulation, overview
-
-
?
additional information
?
-
-
soluble epoxide hydrolase is an enzyme that catalyzes the hydrolysis of epoxyeicosatrienoic acids, EETs, which are lipid mediators derived from arachidonic acid through the cytochrome P450 epoxygenase pathway. EETs can activate multiple antiapoptotic targets through PI3K/Akt survival signaling and protect cardiomyocytes from hypoxia/anoxia
-
-
?
additional information
?
-
-
each monomer is comprised of two distinct structural domains, linked by a proline-rich segment, the 35 kDa C-terminal domain displays epoxide hydrolase activity, while the N-terminal domain exhibits phosphatase activity
-
-
?
additional information
?
-
the enzyme converts epoxyalcohols into linoleate triols
-
-
?
additional information
?
-
the enzyme converts epoxyalcohols into linoleate triols
-
-
?
additional information
?
-
-
the enzyme converts epoxyalcohols into linoleate triols
-
-
?
additional information
?
-
human soluble EH (sEH or EPHX2) and human or murine epoxide hydrolase-3 (EH3 or EPHX3) hydrolyze cis or trans allylic epoxides to single diastereomers, identical to the major isomers detected in epidermis. Microsomal EH (mEH or EPHX1, EC 3.3.2.9) is inactive with these substrates. 12,13-trans-Epoxy-octadeca-9E-enoic acid is completely hydrolyzed by human sEH, human EH3, and N-truncated murine EH3 and mostly hydrolyzed using the N-truncated+7aa-insert murine EH3. 12,13-cis-Epoxy-octadeca-9E-enoic acid is hardly hydrolyzed by human EH3, N-truncated murine EH3, and the N-truncated+7aa-insert murine EH3, and 30% hydrolysis is observed using human sEH. At low substrate concentrations, EPHX2 hydrolyzes 14,15-epoxyeicosatrienoic acid (EET) at twice the rate of the epidermal epoxyalcohol, 9R,10R-trans-epoxy-11E-13R-hydroxy-octadecenoic acid, whereas human or murine EPHX3 hydrolyze the allylic epoxyalcohol at 31fold and 39fold higher rates, respectively
-
-
?
additional information
?
-
human soluble EH (sEH or EPHX2) and human or murine epoxide hydrolase-3 (EH3 or EPHX3) hydrolyze cis or trans allylic epoxides to single diastereomers, identical to the major isomers detected in epidermis. Microsomal EH (mEH or EPHX1, EC 3.3.2.9) is inactive with these substrates. 12,13-trans-Epoxy-octadeca-9E-enoic acid is completely hydrolyzed by human sEH, human EH3, and N-truncated murine EH3 and mostly hydrolyzed using the N-truncated+7aa-insert murine EH3. 12,13-cis-Epoxy-octadeca-9E-enoic acid is hardly hydrolyzed by human EH3, N-truncated murine EH3, and the N-truncated+7aa-insert murine EH3, and 30% hydrolysis is observed using human sEH. At low substrate concentrations, EPHX2 hydrolyzes 14,15-epoxyeicosatrienoic acid (EET) at twice the rate of the epidermal epoxyalcohol, 9R,10R-trans-epoxy-11E-13R-hydroxy-octadecenoic acid, whereas human or murine EPHX3 hydrolyze the allylic epoxyalcohol at 31fold and 39fold higher rates, respectively
-
-
?
additional information
?
-
-
human soluble EH (sEH or EPHX2) and human or murine epoxide hydrolase-3 (EH3 or EPHX3) hydrolyze cis or trans allylic epoxides to single diastereomers, identical to the major isomers detected in epidermis. Microsomal EH (mEH or EPHX1, EC 3.3.2.9) is inactive with these substrates. 12,13-trans-Epoxy-octadeca-9E-enoic acid is completely hydrolyzed by human sEH, human EH3, and N-truncated murine EH3 and mostly hydrolyzed using the N-truncated+7aa-insert murine EH3. 12,13-cis-Epoxy-octadeca-9E-enoic acid is hardly hydrolyzed by human EH3, N-truncated murine EH3, and the N-truncated+7aa-insert murine EH3, and 30% hydrolysis is observed using human sEH. At low substrate concentrations, EPHX2 hydrolyzes 14,15-epoxyeicosatrienoic acid (EET) at twice the rate of the epidermal epoxyalcohol, 9R,10R-trans-epoxy-11E-13R-hydroxy-octadecenoic acid, whereas human or murine EPHX3 hydrolyze the allylic epoxyalcohol at 31fold and 39fold higher rates, respectively
-
-
?
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
(5Z,11Z,14Z)-8,9-epoxyeicosatrienoic acid + H2O
(5Z,11Z,14Z)-8,9-dihydroxyeicosatrienoic acid
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
(5Z,8Z,14Z)-11,12-epoxyeicosatrienoic acid + H2O
(5Z,8Z,14Z)-11,12-dihydroxyeicosatrienoic acid
(8Z,11Z,14Z)-5,6-epoxyeicosatrienoic acid + H2O
(8Z,11Z,14Z)-5,6-dihydroxyeicosatrienoic acid
14S,15R-epoxy-eicosatrienoic acid + H2O
14S,15R-dihydroxy-eicosatrienoic acid
-
-
-
?
9R,10R-trans-epoxy-13R-hydroxy-11E-octadecenoic acid + H2O
(9R,10S,13R)-trihydroxy-11E-octadecenoic acid
-
-
-
?
9R,10S-cis-epoxy-13R-hydroxy-11E-octadecenoic acid
(9R,10R,13R)-trihydroxy-11E-octadecenoic acid
-
-
-
?
cis-14,15-epoxyeicosatrienoic acid + H2O
cis-14,15-dihydroxyeicosatrienoic acid
-
-
-
?
epoxyeicosatrienoic acid + H2O
dihydroxyeicosatrienoic acid
-
-
-
?
9R,10R-trans-epoxy-13R-hydroxy-11E-octadecenoic acid + H2O
(9R,10S,13R)-trihydroxy-11E-octadecenoic acid
-
-
-
?
9R,10S-cis-epoxy-13R-hydroxy-11E-octadecenoic acid
(9R,10R,13R)-trihydroxy-11E-octadecenoic acid
-
-
-
?
cis-14,15-epoxyeicosatrienoic acid + H2O
cis-14,15-dihydroxyeicosatrienoic acid
-
-
-
?
epoxyeicosatrienoic acid + H2O
dihydroxyeicosatrienoic acid
-
elimination of the biological effects of the substrate, involved in regulation of renal eicosanoid levels and blood pressure, mechanism
-
-
?
(5Z,11Z,14Z)-8,9-epoxyeicosatrienoic acid + H2O
(5Z,11Z,14Z)-8,9-dihydroxyeicosatrienoic acid
-
-
-
?
(5Z,11Z,14Z)-8,9-epoxyeicosatrienoic acid + H2O
(5Z,11Z,14Z)-8,9-dihydroxyeicosatrienoic acid
-
-
-
-
?
(5Z,11Z,14Z)-8,9-epoxyeicosatrienoic acid + H2O
(5Z,11Z,14Z)-8,9-dihydroxyeicosatrienoic acid
-
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
-
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
-
-
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
-
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
-
-
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
-
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
-
-
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
-
-
-
?
(5Z,8Z,11Z)-14,15-epoxyeicosatrienoic acid + H2O
(5Z,8Z,11Z)-14,15-dihydroxyeicosatrienoic acid
i.e. EETs, showing endothelium-derived hyperpolarizing factor effects dominating in microvessels independent of nitric oxide and prostacyclin. sEH reduces the beneficial effects of EETs
-
-
?
(5Z,8Z,14Z)-11,12-epoxyeicosatrienoic acid + H2O
(5Z,8Z,14Z)-11,12-dihydroxyeicosatrienoic acid
-
-
-
?
(5Z,8Z,14Z)-11,12-epoxyeicosatrienoic acid + H2O
(5Z,8Z,14Z)-11,12-dihydroxyeicosatrienoic acid
-
-
-
-
?
(5Z,8Z,14Z)-11,12-epoxyeicosatrienoic acid + H2O
(5Z,8Z,14Z)-11,12-dihydroxyeicosatrienoic acid
-
-
-
?
(8Z,11Z,14Z)-5,6-epoxyeicosatrienoic acid + H2O
(8Z,11Z,14Z)-5,6-dihydroxyeicosatrienoic acid
-
-
-
?
(8Z,11Z,14Z)-5,6-epoxyeicosatrienoic acid + H2O
(8Z,11Z,14Z)-5,6-dihydroxyeicosatrienoic acid
-
-
-
-
?
(8Z,11Z,14Z)-5,6-epoxyeicosatrienoic acid + H2O
(8Z,11Z,14Z)-5,6-dihydroxyeicosatrienoic acid
-
-
-
?
additional information
?
-
activity of the sEH can be regulated by the tyrosine nitration of the protein
-
-
?
additional information
?
-
-
activity of the sEH can be regulated by the tyrosine nitration of the protein
-
-
?
additional information
?
-
contribution of hydrolase and phosphatase domains in soluble epoxide hydrolase to vascular endothelial growth factor expression and cell growth, overview
-
-
?
additional information
?
-
-
contribution of hydrolase and phosphatase domains in soluble epoxide hydrolase to vascular endothelial growth factor expression and cell growth, overview
-
-
?
additional information
?
-
EETs are important regulators of cardiovascular function, of cerebral blood flow, and exhibit a wide array of potentially beneficial actions in stroke, including vasodilation, neuroprotection, promotion of angiogenesis and suppression of platelet aggregation, oxidative stress and postischemic inflammation, detailed overview
-
-
?
additional information
?
-
sEH rapidly hydrolyzes eicosatrienoic acids to their corresponding dihydroxyeicosatrienoic acid, DHET, metabolites, which, in general, are much less biologically active than eicosatrienoic acids. Cytochrome P450 epoxygenases, soluble epoxide hydrolase, and the regulation of cardiovascular inflammation, overview. functional impact of CYP epoxygenase-derived eicosatrienoic acids biosynthesis and sEH-mediated xyeicosatrienoic acids hydrolysis on key inflammatory process in the cardiovascular system
-
-
?
additional information
?
-
Vascular actions and antiinflammatory actions of epoxyeicosatrienoic acids, overview
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of blood pressure and inflammation
-
-
?
additional information
?
-
-
differential localization of the enzyme in the brain indicates an essential role in the central nervous system
-
-
?
additional information
?
-
-
epoxyeicosatrienoic acids are substrates of sEH, enzyme regulation, overview
-
-
?
additional information
?
-
-
soluble epoxide hydrolase is an enzyme that catalyzes the hydrolysis of epoxyeicosatrienoic acids, EETs, which are lipid mediators derived from arachidonic acid through the cytochrome P450 epoxygenase pathway. EETs can activate multiple antiapoptotic targets through PI3K/Akt survival signaling and protect cardiomyocytes from hypoxia/anoxia
-
-
?
additional information
?
-
the enzyme converts epoxyalcohols into linoleate triols
-
-
?
additional information
?
-
the enzyme converts epoxyalcohols into linoleate triols
-
-
?
additional information
?
-
-
the enzyme converts epoxyalcohols into linoleate triols
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Ni2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2R,4R,5S,6R,7S)-4-[(benzyloxy)methyl]-3,8-dioxatricyclo[5.1.0.02,4]octane-5,6-diyl diacetate
5.87% inhibition
(1R,3S)-N-(4-cyano-2-(trifluoromethyl)benzyl)-3-((4-methyl-6-(methylamino)-1,3,5-triazin-2-yl)amino)cyclohexanecarboxamide
GSK2256294
(1S,3R)-N-[[4-cyano-2-(trifluoromethyl)phenyl]methyl]-3-[[4-methyl-6-(methylamino)-1,3,5-triazin-2-yl]amino]cyclohexane-1-carboxamide
GSK2256294
(1S,6S,9R)-1-(4-hydroxy-3-methoxyphenyl)-6-methoxy-9-methyl-4-(prop-2-en-1-yl)-7-oxabicyclo[4.2.1]non-4-ene-3,8-dione
75.56% inhibition
(1Z)-1-[(4aS,8aR)-2-(3-[[(2S)-2-(5-methylfuran-2-yl)-2-(pyrrolidin-1-yl)ethyl]carbamoyl]phenyl)-4-oxooctahydrophthalazin-1(2H)-ylidene]dioxidan-1-ium
-
(2E)-5-(2H-1,3-benzodioxol-5-yl)-N-(2-methylpropyl)pent-2-enamide
93.12% inhibition, uncompetitive inhibition
(2E,4E)-5-(2H-1,3-benzodioxol-5-yl)-N-(2-methylpropyl)penta-2,4-dienamide
86.54% inhibition, uncompetitive inhibition
(2E,6E)-7-(2H-1,3-benzodioxol-5-yl)-N-(2-methylpropyl)hepta-2,6-dienamide
88.58% inhibition, uncompetitive inhibition
(2R,3R)-2-(2,6-dihydroxyphenyl)-3,5,7-trihydroxy-2,3-dihydro-4H-1-benzopyran-4-one
15.47% inhibition
(2R,3R,3aS)-2-(4-hydroperoxy-3-methoxyphenyl)-3a-methoxy-3-methyl-5-(prop-2-en-1-yl)-3,3a-dihydro-1-benzofuran-6(2H)-one
86.57% inhibition
(2R,3R,4S,5S)-2,5-bis(3,4-dimethoxyphenyl)-3,4-dimethyloxolane
15.21% inhibition
(2R,3S,4S,5S)-2,5-bis(3,4-dimethoxyphenyl)-3,4-dimethyloxolane
7.12% inhibition
(2S)-5,7-dihydroxy-6-methoxy-2-phenyl-2,3-dihydro-4H-1-benzopyran-4-one
68.98% inhibition
(2S,3R,3aR)-2-(4-hydroperoxy-3-methoxyphenyl)-3a-methoxy-3-methyl-5-(prop-2-en-1-yl)-3,3a-dihydro-1-benzofuran-6(2H)-one
76.89% inhibition
(3R)-N-[(1s,2R,3S)-2,3-diphenylcyclopropyl]-3-[(4-fluorobenzene-1-sulfonyl)amino]piperidine-1-carboxamide
-
(3R)-N-[(1s,2R,3S)-2,3-diphenylcyclopropyl]-3-[(methanesulfonyl)amino]piperidine-1-carboxamide
-
(8Z)-13-[[[butyl(methyl)amino](oxo)acetyl](methyl)amino]tridec-8-enoic acid
-
(E)-4-[N-((2-trifluoromethyl)benzyl)benzamide]-alpha-ethylcinnamic acid
-
(E)-N-methoxy-N-methyl 3-[4-(N-((2-trifluoromethyl)benzyl)-benzamide)]but-2-enamide
-
(R)-1-((3,5-difluoropyridin-2-yl)methyl)-2-methyl-N-(1-phenylpropyl)-1H-benzo[d]imidazole-5-carboxamide
GSK1997132B
(R)-4-cyano-N-[3-(4-fluorophenyl)-3-(4-methanesulfonyl-phenyl)-propyl]-benzamide
-
(R)-N-[3-(4-fluorophenyl)-3-(4-methanesulfonyl-phenyl)-propyl]-6-hydroxy-nicotinamide
-
(S)-4-cyano-N-[3-(4-fluorophenyl)-3-(4-methanesulfonyl-phenyl)-propyl]-benzamide
-
(S)-N-[3-(4-fluorophenyl)-3-(4-methanesulfonyl-phenyl)-propyl]-6-hydroxy-nicotinamide
-
1-(1-isobutyrylpiperidin-4-yl)-3-(4-(3-(trifluoromethyl)-3H-diazirin-3-yl)phenyl)urea
binding structure at the enzyme's active site, docking analysis and molecular dynamics simulations using the PDB ID 4JNC structure as template
-
1-(1-methanesulfonyl-piperidin-4-yl)-3-(4-trifluoromethoxy-phenyl)-urea
-
1-(3,4-dihydro-1'H-spiro[chromene-2,4'-piperidin]-1'-yl)-3-phenylpropan-1-one
-
1-(3-(5-(hydroxyureido)methyl-2-methoxyphenoxy)propyl)-3-[4-(trifluoromethoxy)phenyl]urea
i.e. KM55, a dual inhibitor of 5-lipoxygenase (5-LO) and soluble epoxide hydrolase (sEH), synthesis and evaluation, overview. Applied to leukocytes, it strongly inhibits the lipopolysaccharide (LPS)-induced adhesion of the leukocytes to endothelial cells. KM55 is a designed multi-target ligand which inhibits the enzymatic activity of 5-LO and sEH
1-(4-(N1-methyl-N2-methyl-N2-(methyloxy)oxalamido)-benzyl)-3-adamantylurea
-
1-(4-(N2-(tetrahydro-2H-pyran-2-yloxy)oxalamido)benzyl)-3-adamantylurea
-
1-(4-acetylphenyl)-N-(5-chloro-1,3-benzoxazol-2-yl)piperidine-4-carboxamide
IC50 value in COS-7 cell assay 4.7 nM, 45% remiaining stability in human microsomes
1-(4-acetylphenyl)-N-(5-methyl-1,3-benzoxazol-2-yl)piperidine-4-carboxamide
IC50 value in COS-7 cell assay 5.8 nM, 53% remiaining stability in human microsomes
1-(4-trifluoro-methoxy-phenyl)-3-(1-propionylpiperidin-4-yl)urea
TPPU, a tight binding inhibitor of enzyme sEH
1-adamantan-1-yl-3-(5-[2-(2-ethoxyethoxy)ethoxy]pentyl)urea
i.e. 1-adamantan-1-yl-3-(5-[2-(2-ethoxyethoxy)ethoxy]pentyl)urea
1-[1-(2-methylbutanoyl)piperidin-4-yl]-3-[4-(trifluoromethoxy)phenyl]urea
-
1-[1-(2-methylbutanoyl)piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
-
1-[1-(2-methylpropanoyl)piperidin-4-yl]-3-[4-(trifluoromethoxy)phenyl]urea
-
1-[1-(2-methylpropanoyl)piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
-
1-[1-(3-methylbutanoyl)piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
-
1-[1-(4,4,4-trifluorobutanoyl)piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
-
1-[1-(cyclopropylcarbonyl)piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
-
1-[1-(cyclopropylsulfonyl)piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
-
1-[1-(methylsulfonyl)piperidin-4-yl]-3-[4-(trifluoromethoxy)phenyl]urea
-
1-[1-(propan-2-ylsulfonyl)piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
-
1-[1-[(2,2,2-trifluoroethyl)sulfonyl]piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
-
1-[1-[(2S)-2-methylbutanoyl]piperidin-4-yl]-3-[4-(trifluoromethoxy)phenyl]urea
-
1-[1-[(2S)-2-methylbutanoyl]piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
-
1-[4-(1,1,1,2,3,3,3-heptafluoropropan-2-yl)phenyl]-3-[1-(2-methylbutanoyl)piperidin-4-yl]urea
-
1-[4-(1,1,1,2,3,3,3-heptafluoropropan-2-yl)phenyl]-3-[1-(3,3,3-trifluoropropanoyl)piperidin-4-yl]urea
-
1-[4-(trifluoromethyl)phenyl]-3-[1-(3,3,3-trifluoropropanoyl)piperidin-4-yl]urea
-
1-[4-methyl-6-(methylamino)-1,3,5-triazin-2-yl]-N-[2-(trifluoromethyl)benzyl]piperidine-4-carboxamide
analysis of the crystal structure of enzyme-inhibitor complex
12-(3-adamantan-1-yl-ureido)dodecanoic acid butyl ester
AUDA-BE, displays improved bioavailability compared to AUDA
12-(3-adamantyl-ureido)-dodecanoic acid
AUDA, a tight binding inhibitor of enzyme sEH
2-(2,4-dichlorophenyl)-1-[6-(methylsulfonyl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidin]-1'-yl]ethanone
-
2-(2,6-dihydroxyphenyl)-3,5,7-trihydroxy-4H-1-benzopyran-4-one
12.34% inhibition
2-(3,4-dihydroxy-5-methoxyphenyl)-5,7-dihydroxy-1-benzopyran-1-ium-3-yl beta-D-glucopyranoside
mixed-type inhibition
2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-1-benzopyran-1-ium
noncompetitive inhibition
2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-1-benzopyran-1-ium-3-yl beta-D-glucopyranoside
noncompetitive inhibition
2-(tricyclo[3.3.1.13,7]dec-1-yl)-N-[1-(trifluoroacetyl)piperidin-4-yl]acetamide
-
2-ethyl 3-[4-(N-(4-fluoro(2-trifluoromethyl)benzyl)-benzamide)]propionic acid
-
2-ethyl-3-[4-(N-((2-bromo)benzyl)benzamide)]propionic acid
34% inhibition at 0.01 mM, pH 7.0, 22°C
2-ethyl-3-[4-(N-((2-chloro)benzyl)benzamide)]propionic acid
20% inhibition at 0.01 mM, pH 7.0, 22°C
2-ethyl-3-[4-(N-((2-methyl)benzyl)benzamide)]propionic acid
25% inhibition at 0.01 mM, pH 7.0, 22°C
2-ethyl-3-[4-(N-((2-trifluoromethoxy)benzyl)benzamide)]-propionic acid
23% inhibition at 0.01 mM, pH 7.0, 22°C
2-ethyl-3-[4-(N-((4-fluoro)benzyl)benzamide)]propionic acid
28% inhibition at 0.01 mM, pH 7.0, 22°C
2-ethyl-3-[4-(N-((4-methoxy)benzyl)benzamide)]propionic acid
34% inhibition at 0.01 mM, pH 7.0, 22°C
2-ethyl-3-[4-(N-(4-methoxy(2-trifluoromethyl)benzyl)-benzamide)]propionic acid
-
2-ethyl-3-[4-(N-benzylbenzamide)]propionic acid
4% inhibition at 0.01 mM, pH 7.0, 22°C
2-methoxy-4-[7-methoxy-3-methyl-5-[(1E)-prop-1-en-1-yl]-1-benzofuran-2-yl]phenol
82.46% inhibition
2-[(4-[3-[3-(pyridin-4-yl)-1,2,4-oxadiazol-5-yl]propanoyl]piperazin-1-yl)methyl]-4H-pyrido[1,2-a]pyrimidin-4-one
-
2-[1-[(2S)-2-methylbutanoyl]piperidin-4-yl]-N-[4-(trifluoromethoxy)phenyl]acetamide
-
2-[2-(adamantan-1-yl)ethyl]-N-(3,5-dimethyladamantan-1-yl)hydrazine-1-carboxamide
-
2-[2-(adamantan-1-yl)ethyl]-N-[(adamantan-1-yl)methyl]hydrazine-1-carboxamide
-
2-[3-(adamantan-1-yl)propyl]-N-(3,5-dimethyladamantan-1-yl)hydrazine-1-carboxamide
-
2-[4-(N-((2-trifluoromethyl)benzyl )benzamide)]-cyclopropanecarboxylic acid
-
3,4-dihydro-1'H-spiro[chromene-2,4'-piperidin]-1'-yl[4-(trifluoromethyl)phenyl]methanone
-
3-(2-amino-1,3-thiazol-4-yl)-5-methyl-1-(tetrahydrofuran-2-ylmethyl)-1H-pyrrol-2-ol
-
3-(3-amino-3-oxopropyl)-N-(4-chlorophenyl)-3-phenylpiperidine-1-carboxamide
-
3-([cis-4-[(tricyclo[3.3.1.13,7]dec-1-ylcarbamoyl)amino]cyclohexyl]oxy)benzoic acid
-
3-([[(adamantan-1-yl)methyl]carbamoyl]amino)adamantan-1-yl trifluoroacetate
-
3-methyl-3-phenyl-N-[3-[(1S,2S)-2-phenylcyclopropyl]benzyl]piperidine-1-carboxamide
-
3-methyl-3-phenyl-N-[3-[2-(quinoxalin-6-yl)ethyl]benzyl]piperidine-1-carboxamide
-
3-methyl-3-phenyl-N-[[2'-(trifluoromethyl)biphenyl-4-yl]methyl]piperidine-1-carboxamide
-
3-morpholinosydnonimine
i.e. SIN-1, a peroxonitrite generator, causes nitration on several tyrosine residues including Tyr383 and Tyr466. 1-adamantyl-3-cyclohexylurea in vitro decreases sensitivity to SIN-1
3-[1-[(4-chlorophenyl)carbamoyl]-3-(pyridin-2-yl)piperidin-3-yl]propanoic acid
-
3-[1-[(4-chlorophenyl)carbamoyl]-3-(pyridin-3-yl)piperidin-3-yl]propanoic acid
-
3-[1-[(4-chlorophenyl)carbamoyl]-3-(pyridin-4-yl)piperidin-3-yl]propanoic acid
-
3-[1-[(4-chlorophenyl)carbamoyl]-3-[3-(trifluoromethyl)phenyl]piperidin-3-yl]propanoic acid
-
3-[1-[(4-chlorophenyl)carbamoyl]-3-[4-(trifluoromethyl)phenyl]piperidin-3-yl]propanoic acid
-
3-[3-(biphenyl-4-yl)-1-[(4-chlorophenyl)carbamoyl]piperidin-3-yl]propanoic acid
-
3-[4-[(1-[[(1R,3S)-2,2-dimethyl-3-phenylcyclopropyl]carbamoyl]piperidin-4-yl)oxy]phenyl]propanoic acid
-
3-[4-[(1-[[(1S,2R)-2-phenylcyclopropyl]carbamoyl]piperidin-4-yl)oxy]phenyl]propanoic acid
-
3-[4-[(1-[[(1S,2R,3R)-2-methyl-3-phenylcyclopropyl]carbamoyl]piperidin-4-yl)oxy]phenyl]propanoic acid
-
3-[4-[(1-[[(1s,2R,3S)-2,3-bis(4-fluorophenyl)cyclopropyl]carbamoyl]piperidin-4-yl)oxy]phenyl]propanoic acid
-
3-[4-[(1-[[(1s,2R,3S)-2,3-diphenylcyclopropyl]carbamoyl]piperidin-4-yl)oxy]phenyl]propanoic acid
-
3-[4-[(1-[[(1S,2S,3R)-2-methyl-3-phenylcyclopropyl]carbamoyl]piperidin-4-yl)oxy]phenyl]propanoic acid
-
4'-hydroxy-N-(2-phenylcyclopropyl)-3',4'-dihydro-1H-spiro[piperidine-4,2'-pyrano[3,2-b]pyridine]-1-carboxamide
-
4'-[([2-(trifluoromethyl)phenyl]methyl)carbamoyl][1,1'-biphenyl]-3-carboxylic acid
-
4'-[([2-(trifluoromethyl)phenyl]methyl)carbamoyl][1,1'-biphenyl]-4-carboxylic acid
-
4-((4-[3-(3,5,7-trimethyladamant-1-yl)ureido]cyclohexyl)oxy)benzoic acid
-
4-(1,2,4-oxadiazol-3-yl)-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
-
4-(1,3,4-oxadiazol-2-yl)-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
-
4-(1,3-benzoxazol-2-yl)-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
-
4-(1-methyl-1H-1,2,3-triazol-4-yl)-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
-
4-(2,3-dihydro-1H-1,2,3-triazol-1-yl)-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
-
4-(3-hydroxy-4-methyl-1,2-oxazol-5-yl)-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
-
4-(3-methyl-1,2,4-oxadiazol-5-yl)-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
-
4-(4-methyl-4H-1,2,4-triazol-3-yl)-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
-
4-(5-phenyl-3-[3-[3-(3-trifluoromethyl-phenyl)-ureido]-propyl]-pyrazol-1-yl)-benzenesulfonamide
dual inhibitor of cyclooxygenase-2 and soluble epoxide hydrolase
4-(5-phenyl-3-[3-[3-(4-trifluoromethoxy-phenyl)-ureido]-propyl]-pyrazol-1-yl)-benzenesulfonamide
dual inhibitor of cyclooxygenase-2 and soluble epoxide hydrolase
4-(5-phenyl-3-[3-[3-(4-trifluoromethyl-phenyl)-ureido]-propyl]-pyrazol-1-yl)-benzenesulfonamide
dual inhibitor of cyclooxygenase-2 and soluble epoxide hydrolase
4-(5-[1-[(2-phenylcyclopropyl)carbamoyl]piperidin-4-yl]-1,2,4-oxadiazol-3-yl)benzoic acid
-
4-(trifluoromethyl)-N-[4-(trifluoromethyl)phenyl]-1,2-benzoxazol-3-amine
-
4-([trans-4-[(tricyclo[3.3.1.13,7]dec-1-ylcarbamoyl)amino]cyclohexyl]oxy)benzoic acid
-
4-cyano-N-[(3S)-3-(4-fluorophenyl)-3-[4-(methanesulfonyl)phenyl]propyl]benzamide
-
4-oxo-N-(1,2,3,4-tetrahydronaphthalen-2-yl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
-
4-oxo-N-(2-phenylcyclopropyl)-6-(pyridin-4-yl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
-
4-oxo-N-(3-phenylcyclopentyl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
-
4-oxo-N-(6,7,8,9-tetrahydro-5H-benzo[7]annulen-7-yl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
-
4-oxo-N-[(1S,2R)-2-phenylcyclopropyl]-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
-
4-[(4-[[(3-methyladamantan-1-yl)carbamoyl]amino]cyclohexyl)oxy]benzoic acid
-
4-[3-(isoquinolin-1-yl)-1,2,4-oxadiazol-5-yl]-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
-
4-[3-(pyridin-2-yl)-1,2,4-oxadiazol-5-yl]-N-(1,2,3,4-tetrahydronaphthalen-2-yl)piperidine-1-carboxamide
-
4-[3-(pyridin-2-yl)-1,2,4-oxadiazol-5-yl]-N-(6,7,8,9-tetrahydro-5H-benzo[7]annulen-7-yl)piperidine-1-carboxamide
-
4-[3-(pyridin-2-yl)-1,2,4-oxadiazol-5-yl]-N-[4-(trifluoromethyl)phenyl]piperidine-1-carboxamide
-
4-[3-[4-(methylsulfonyl)phenyl]-1,2,4-oxadiazol-5-yl]-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
-
4-[5-(cyclohexylamino)-2-(4-ethylpiperazin-1-yl)imidazo[2,1-b][1,3,4]thiadiazol-6-yl]-2,6-dimethoxyphenol
-
4-[[(1r,4r)-4-([[(adamantan-1-yl)methyl]carbamoyl]amino)cyclohexyl]oxy]benzoic acid
-
4-[[(1r,4r)-4-[[(3,5,7-trimethyladamantan-1-yl)carbamoyl]amino]cyclohexyl]oxy]benzoic acid
-
4-[[(1r,4r)-4-[[(3,5-dimethyladamantan-1-yl)carbamoyl]amino]cyclohexyl]oxy]benzoic acid
-
4-[[(1r,4r)-4-[[(3-chloroadamantan-1-yl)carbamoyl]amino]cyclohexyl]oxy]benzoic acid
-
4-[[(1r,4r)-4-[[(3-ethyladamantan-1-yl)carbamoyl]amino]cyclohexyl]oxy]benzoic acid
-
4-[[(1r,4r)-4-[[(3-methyladamantan-1-yl)carbamoyl]amino]cyclohexyl]oxy]benzoic acid
-
4-[[(2R,5R)-5-[[(2-oxoadamantan-1-yl)carbamoyl]amino]piperidin-2-yl]oxy]benzoic acid
-
4-[[cis-4-([[4-(trifluoromethoxy)phenyl]carbamoyl]amino)cyclohexyl]oxy]benzoic acid
-
5,6,7-trihydroxy-8-methoxy-2-phenyl-4H-1-benzopyran-4-one
35.58% inhibition
5,6-dihydroxy-4-oxo-2-phenyl-4H-1-benzopyran-7-yl D-threo-hexopyranosiduronic acid
75.86% inhibition
5,7-dihydroxy-2-(2-hydroxyphenyl)-4H-1-benzopyran-4-one
34.96% inhibition
5,7-dihydroxy-2-(2-hydroxyphenyl)-6-methoxy-4H-1-benzopyran-4-one
34.82% inhibition
5,7-dihydroxy-2-(3,4,5-trihydroxyphenyl)-1-benzopyran-1-ium-3-yl beta-D-galactopyranoside
mixed-type inhibition
5,7-dihydroxy-2-(3,4,5-trihydroxyphenyl)-1-benzopyran-1-ium-3-yl beta-D-glucopyranoside
noncompetitive inhibition
5-(trifluoromethyl)-N-[4-(trifluoromethyl)phenyl]-1,2-benzoxazol-3-amine
-
5-hydroxy-2-(2-hydroxy-6-methoxyphenyl)-6,7,8-trimethoxy-4H-1-benzopyran-4-one
20.83% inhibition
5-hydroxy-2-(4-hydroxy-3-methoxyphenyl)-7-methoxy-4H-1-benzopyran-4-one
25.64% inhibition
6'-(methylsulfonyl)-N-(2-phenylcyclopropyl)-1H,4'H-spiro[azepane-4,3'-chromene]-1-carboxamide
-
6-(1-methyl-1H-pyrazol-5-yl)-4-oxo-N-(2-phenylcyclopropyl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
-
6-(2-fluorophenyl)-N-[5-(trifluoromethyl)pyridin-2-yl]-1,2-benzoxazol-3-amine
-
6-(3-methylpyridin-2-yl)-N-[5-(trifluoromethyl)pyridin-2-yl]-1,2-benzoxazol-3-amine
-
6-(isoquinolin-5-yl)-N-[4-(trifluoromethyl)phenyl]-1,2-benzoxazol-3-amine
-
6-(methylsulfonyl)-4-oxo-N-(2-phenylcyclopropyl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
-
6-(pyridin-3-yl)-N-[5-(trifluoromethyl)pyridin-2-yl]-1,2-benzoxazol-3-amine
-
6-(pyridin-4-yl)-N-[5-(trifluoromethyl)pyridin-2-yl]-1,2-benzoxazol-3-amine
-
6-(trifluoromethyl)-N-[4-(trifluoromethyl)phenyl]-1,2-benzoxazol-3-amine
-
6-fluoro-N-(2-phenylcyclopropyl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
-
6-[(1-methyl-1H-pyrazol-5-yl)amino]-4-oxo-N-(2-phenylcyclopropyl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
-
6-[3-(trifluoromethyl)phenyl]-N-[5-(trifluoromethyl)pyridin-2-yl]-1,2-benzoxazol-3-amine
-
7-(1H-indol-5-yl)-N-[5-(trifluoromethyl)pyridin-2-yl]-1,2-benzoxazol-3-amine
-
7-(trifluoromethyl)-N-[4-(trifluoromethyl)phenyl]-1,2-benzoxazol-3-amine
-
7-(trifluoromethyl)-N-[5-(trifluoromethyl)pyridin-2-yl]-1,2-benzoxazol-3-amine
-
7-(trifluoromethyl)-N-[5-(trifluoromethyl)pyridin-2-yl][1,2]oxazolo[5,4-c]pyridin-3-amine
-
7-(trifluoromethyl)-N-[6-(trifluoromethyl)pyridin-3-yl]-1,2-benzoxazol-3-amine
-
7-[2-(trifluoromethyl)phenyl]-N-[5-(trifluoromethyl)pyridin-2-yl]-1,2-benzoxazol-3-amine
-
7-[3-(trifluoromethyl)phenyl]-N-[5-(trifluoromethyl)pyridin-2-yl]-1,2-benzoxazol-3-amine
-
cis-4-(4-[3-(4-trifluoromethoxyphenyl)ureido]cyclohexyloxy)-benzoic acid
-
ethyl (E)-3-[N-((2-trifluoromethyl)benzyl)benzamide]-alpha-ethylcinnamate
-
ethyl (E)-3-[N-((2-trifluoromethyl)benzyl)benzamide]-alpha-ethylcinnamic acid
-
ethyl (E)-4-[N-((2-(trifluoromethyl)-benzyl)benzamide]-alpha-ethylcinnamate
-
ethyl 2-ethyl 3-[3-(N-((2-trifluoromethyl)benzyl)benzamide)]-propanoate
-
ethyl 2-ethyl 3-[4-(N-((4-trifluoromethoxy)benzyl)-benzamide)]propanoate
-
ethyl 2-ethyl 3-[4-(N-((4-trifluoromethyl)benzyl)benzamide)]-propanoate
-
ethyl 2-ethyl 3-[4-(N-(4-fluoro(2-trifluoromethyl)benzyl)-benzamide)]propanoate
-
ethyl 2-ethyl 3-[4-(N-(4-methoxy(2-trifluoromethyl)benzyl)-benzamide)]propanoate
-
ethyl 2-methyl 3-[4-(N-((2-trifluoromethyl)benzyl)benzamide)]-propanoate
-
ethyl 2-phenyl 3-[4-(N-((2-trifluoromethyl)benzyl)benzamide)]-propanoate
-
ethyl 2-propyl 3-[4-(N-((2-trifluoromethyl)benzyl)benzamide)]-propanoate
-
methyl 2-([4-[(tricyclo[3.3.1.13,7]dec-2-ylcarbamoyl)amino]piperidin-1-yl]carbonyl)benzoate
-
methyl 2-hydroxy-4-[(tricyclo[3.3.1.13,7]dec-1-ylcarbamoyl)amino]benzoate
-
methyl 2-[(4-[[(tricyclo[3.3.1.13,7]dec-2-ylcarbamoyl)amino]methyl]piperidin-1-yl)carbonyl]benzoate
-
methyl 3-([4-[(tricyclo[3.3.1.13,7]dec-2-ylcarbamoyl)amino]piperidin-1-yl]carbonyl)benzoate
-
methyl 3-[(4-[[(tricyclo[3.3.1.13,7]dec-2-ylcarbamoyl)amino]methyl]piperidin-1-yl)carbonyl]benzoate
-
methyl 3-[1-[(4-chlorophenyl)carbamoyl]-3-phenylpiperidin-3-yl]propanoate
-
methyl 4-([4-[(tricyclo[3.3.1.13,7]dec-2-ylcarbamoyl)amino]piperidin-1-yl]carbonyl)benzoate
-
methyl 4-[(4-[[(tricyclo[3.3.1.13,7]dec-2-ylcarbamoyl)amino]methyl]piperidin-1-yl)carbonyl]benzoate
-
methyl 4-[(6R,12aS)-2-[3-(1H-imidazol-1-yl)propyl]-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydropyrazino[1',2':1,6]pyrido[3,4-b]indol-6-yl]benzoate
-
methyl 5-oxo-5-(4-[[(tricyclo[3.3.1.13,7]dec-2-ylcarbamoyl)amino]methyl]piperidin-1-yl)pentanoate
-
methyl 5-oxo-5-[4-[(tricyclo[3.3.1.13,7]dec-2-ylcarbamoyl)amino]piperidin-1-yl]pentanoate
-
N,N'-butane-1,4-diylbis[N'-[1-(adamantan-1-yl)-2-methylpropan-2-yl]urea]
-
N,N'-[1,4-phenylenebis(methylene)]bis[N'-(3,5-dimethyladamantan-1-yl)urea]
-
N-((4-bromo-2-[(trifluoromethyl)oxy]phenyl)-methyl)-1-[4-methyl-6-(methylamino)-1,3,5-triazin-2-yl]-4-piperidinecarboxamide
GSK2188931B
N-(2,3-dihydro-1H-inden-1-yl)-4-oxo-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
-
N-(2,3-dihydro-1H-inden-1-yl)-4-[3-(pyridin-2-yl)-1,2,4-oxadiazol-5-yl]piperidine-1-carboxamide
-
N-(2,4-dichlorobenzyl)-1-(2-ethoxyethyl)-6-oxo-1,6-dihydropyridine-3-carboxamide
-
N-(2,4-dichlorobenzyl)-6-[2-(pyrrolidin-1-yl)ethyl]pyridine-3-carboxamide
-
N-(2-chloro-4-cyanobenzyl)-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
-
N-(2-oxoadamantan-1-yl)-N'-1,3,5-triazatricyclo[3.3.1.13,7]decan-7-ylurea
-
N-(2-phenylcyclopropyl)-3',4'-dihydro-1H-spiro[piperidine-4,2'-pyrano[3,2-b]pyridine]-1-carboxamide
-
N-(2-phenylcyclopropyl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
-
N-(2-phenylcyclopropyl)-4-(1H-1,2,4-triazol-1-yl)piperidine-1-carboxamide
-
N-(2-phenylcyclopropyl)-4-[3-(pyrazin-2-yl)-1,2,4-oxadiazol-5-yl]piperidine-1-carboxamide
-
N-(2-phenylcyclopropyl)-4-[3-(pyridin-2-yl)-1,2,4-oxadiazol-5-yl]piperidine-1-carboxamide
-
N-(2-phenylcyclopropyl)-4-[3-(pyridin-3-yl)-1,2,4-oxadiazol-5-yl]piperidine-1-carboxamide
-
N-(2-phenylcyclopropyl)-4-[3-(pyridin-4-yl)-1,2,4-oxadiazol-5-yl]piperidine-1-carboxamide
-
N-(2-phenylcyclopropyl)-4-[3-(pyrimidin-2-yl)-1,2,4-oxadiazol-5-yl]piperidine-1-carboxamide
-
N-(2-phenylcyclopropyl)-4-[3-(quinolin-2-yl)-1,2,4-oxadiazol-5-yl]piperidine-1-carboxamide
-
N-(2-phenylcyclopropyl)-4-[3-[2-(trifluoromethyl)phenyl]-1,2,4-oxadiazol-5-yl]piperidine-1-carboxamide
-
N-(3,3-diphenylpropyl)-1-(2-ethoxyethyl)-6-oxo-1,6-dihydropyridine-3-carboxamide
-
N-(3,3-diphenylpropyl)-6-[2-(pyrrolidin-1-yl)ethyl]pyridine-3-carboxamide
-
N-(3,5,7-trimethyladamantan-1-yl)-4-([[(3,5,7-trimethyladamantan-1-yl)carbamoyl]amino]methyl)piperidine-1-carboxamide
-
N-(3,5-dimethyladamantan-1-yl)-N'-1,3,5-triazatricyclo[3.3.1.13,7]decan-7-ylurea
-
N-(3,5-dimethyladamantan-1-yl)-N'-[4-([[(3,5-dimethyladamantan-1-yl)carbamoyl]amino]methyl)phenyl]urea
-
N-(3-hydroxytricyclo[3.3.1.13,7]dec-1-yl)-2-(tricyclo[3.3.1.13,7]dec-1-yl)acetamide
-
N-(3-methylphenyl)-4-[[1-methyl-5-(pyrrolidine-1-carbonyl)-1H-benzimidazol-2-yl]methyl]piperazine-1-carboxamide
-
N-(4-(N1-methyl-N2-methyl-N2-(methyloxy)oxalamido)-benzyl)adamantanecarboxamide
-
N-(4-(N2-(tetrahydro-2H-pyran-2-yloxy)oxalamido)benzyl)adamantanecarboxamide
-
N-(4-bromo-2-cyanobenzyl)-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
-
N-(4-chlorophenyl)-3-(3-hydroxypropyl)-3-phenylpiperidine-1-carboxamide
-
N-(4-chlorophenyl)-3-phenyl-3-[2-(1H-tetrazol-5-yl)ethyl]piperidine-1-carboxamide
-
N-(4-chlorophenyl)-3-[2-(dimethylamino)ethyl]-3-phenylpiperidine-1-carboxamide
-
N-(4-chlorophenyl)-3-[2-oxo-2-(1H-tetrazol-5-ylamino)ethyl]-3-phenylpiperidine-1-carboxamide
-
N-(4-chlorophenyl)-3-[3-(diethylamino)-3-oxopropyl]-3-phenylpiperidine-1-carboxamide
-
N-(4-chlorophenyl)-3-[3-(methylamino)-3-oxopropyl]-3-phenylpiperidine-1-carboxamide
-
N-(4-chlorophenyl)-3-[3-(morpholin-4-yl)-3-oxopropyl]-3-phenylpiperidine-1-carboxamide
-
N-(4-chlorophenyl)-3-[3-oxo-3-(1H-tetrazol-5-ylamino)propyl]-3-phenylpiperidine-1-carboxamide
-
N-(4-[[(adamantan-1-yl)carbamoyl]amino]butyl)-N'-(3,5-dimethyladamantan-1-yl)urea
-
N-(6-[[(adamantan-1-yl)carbamoyl]amino]hexyl)-N'-(3,5-dimethyladamantan-1-yl)urea
-
N-(8-[[(adamantan-1-yl)carbamoyl]amino]octyl)-N'-(3,5-dimethyladamantan-1-yl)urea
-
N-adamantan-1-yl-N'-(5-[2-[2-(2-hydroxyethoxy)ethoxy]ethoxy]pentyl)urea
-
N-methoxy-N-methyl 3-[4-(N-((2-trifluoromethyl)benzyl)-benzamide)]cyclopropanecarboxamide
-
N-[(1s,2R,3S)-2,3-diphenylcyclopropyl]-4-methylpiperazine-1-carboxamide
-
N-[(3'-chlorobiphenyl-4-yl)methyl]-3-methyl-3-phenylpiperidine-1-carboxamide
-
N-[(3,5-dimethyladamantan-1-yl)methyl]-N'-(3,5,7-trimethyladamantan-1-yl)urea
-
N-[(3-ethyladamantan-1-yl)methyl]-N'-1,3,5-triazatricyclo[3.3.1.13,7]decan-7-ylurea
-
N-[(adamantan-1-yl)methyl]-2-[3-(adamantan-1-yl)propyl]hydrazine-1-carboxamide
-
N-[(adamantan-1-yl)methyl]-4-[([[(adamantan-1-yl)methyl]carbamoyl]amino)methyl]piperidine-1-carboxamide
-
N-[1-[(2S)-2-methylbutanoyl]piperidin-4-yl]-2-[4-(trifluoromethoxy)phenyl]acetamide
-
N-[2-(methylsulfonyl)benzyl]-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
-
N-[2-(trifluoromethoxy)benzyl]-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
-
N-[2-chloro-4-(1H-tetrazol-5-yl)benzyl]-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
-
N-[2-chloro-4-(methylsulfamoyl)benzyl]-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
-
N-[2-chloro-4-(methylsulfonyl)benzyl]-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
-
N-[3,3-bis-(4-fluorophenyl)-propyl]-2-(2,2,2-trifluoro-ethoxy)-isonicotinamide
-
N-[3,3-bis-(4-fluorophenyl)-propyl]-6-(2,2,2-trifluoro-ethoxy)-nicotinamide
-
N-[3-(4-fluorophenyl)-3-(4-methanesulfonyl-phenyl)-propyl]-4-methanesulfonyl-benzamide
-
N-[3-(4-fluorophenyl)-3-(4-methanesulfonyl-phenyl)-propyl]-6-(2,2,2-trifluoro-ethoxy)-nicotinamide
-
N-[3-(4-fluorophenyl)-3-(4-methanesulfonyl-phenyl)-propyl]-nicotinamide
-
N-[3-[(2',4'-difluorobiphenyl-4-yl)methoxy]phenyl]piperidine-4-carboxamide
-
N-[3-[2-(4-chlorophenyl)ethyl]benzyl]-3-methyl-3-phenylpiperidine-1-carboxamide
-
N-[4-(2-methylpropanoyl)cyclohexyl]-N'-[4-(trifluoromethyl)phenyl]urea
i.e. UC2389
N-[4-(methylsulfonyl)benzyl]-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
-
N-[4-([[(adamantan-1-yl)methyl]carbamoyl]amino)butyl]-N'-[(3,5-dimethyladamantan-1-yl)methyl]urea
-
N-[4-([[(adamantan-1-yl)methyl]carbamoyl]amino)phenyl]-N'-[(3,5-dimethyladamantan-1-yl)methyl]urea
-
N-[4-chloro-2-(methylsulfonyl)benzyl]-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
-
N-[5-[2-(2-ethoxyethoxy)ethoxy]pentyl]-N'-(4-hydroxyadamantan-1-yl)urea
-
N-[6-([[(adamantan-1-yl)methyl]carbamoyl]amino)hexyl]-N'-[(3,5-dimethyladamantan-1-yl)methyl]urea
-
N-[8-([[(adamantan-1-yl)methyl]carbamoyl]amino)octyl]-N'-[(3,5-dimethyladamantan-1-yl)methyl]urea
-
N-[[4'-(methylsulfonyl)biphenyl-4-yl]methyl]-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
-
N1-(4-((2-adamantylacetamido)methyl)phenyl)-N1-methyl-N2-methyl-N2-methyloxyoxalamide
-
N1-(4-((2-adamantylacetamido)methyl)phenyl)-N2-methyl-N2-methyloxyoxalamide
-
N1-(4-(2-adamantylacetamido)phenyl)-N1-methyl-N2-methyl-N2-(methyloxy)oxalamide
-
peroxynitrite
causes nitration on several tyrosine residues including Tyr383 and Tyr466
t-butyl 4-[2-[(5-chloro-1,3-benzoxazol-2-yl)amino]-2-oxoethyl]piperidine-1-carboxylate
IC50 value in COS-7 cell assay 1.5 nM, 43% remiaining stability in human microsomes
trans-4-(4-[3-(4-trifluoromethoxyphenyl)ureido]cyclohexyloxy)benzoic acid
-
trans-4-[4-[3-(4-trifluoromethoxyphenyl)-ureido]-cyclohexyloxy]benzoic acid
-
[6-(methylsulfonyl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidin]-1'-yl][4-(trifluoromethyl)phenyl]methanone
-
(R)-N-(2-(diphenylamino)ethyl)-3-(3-(1-hydroxyureido)but-1-yn-1-yl)benzamide
-
dual 5-LOX/soluble epoxide hydrolase inhibitor
-
(R)-N-(3,3-bis(4-fluorophenyl)propyl)-3-(3-(1-hydroxyureido)but-1-yn-1-yl)benzamide
-
dual 5-LOX/soluble epoxide hydrolase inhibitor
-
1,1'-(benzene-1,3-diyldicarbonyl)bis[N-(2,4-dichlorobenzyl)piperidine-4-carboxamide]
-
55% inhibition at 200 nM
1,1'-(benzene-1,3-diyldisulfonyl)bis[N-(2,4-dichlorobenzyl)piperidine-4-carboxamide]
-
45% inhibition at 200 nM
1,3-disubstituted amides
-
potent and stable inhibition, Ki in the nanomolar range, mechanism
1,3-disubstituted carbamate derivatives
-
potent and stable inhibition, Ki in the nanomolar range, mechanism
1,3-disubstituted urea derivatives
-
potent and stable inhibition, Ki in the nanomolar range, mechanism
1-(1-methanesulfonyl-piperidin-4-yl)-3-(4-trifluoromethoxy-phenyl)-urea
-
i.e. TUPS
1-(1-methylsulfonyl-piperidin-4-yl)-3-(4-trifluoromethoxy-phenyl)-urea
-
potent inhibitor of sEH
1-(1-nicotinoylpiperidin-4-yl)-3-(4-(trifluoromethoxy)phenyl)-urea
-
i.e. AR9276
1-(2-((3-((3s,5s,7s)-adamantan-1-yl)ureido)methyl)benzyl)-1H-pyrrole-2-carboxylic acid
-
-
1-(3-((3-((3s,5s,7s)-adamantan-1-yl)ureido)methyl)benzyl)-1H-pyrrole-2-carboxylic acid
-
-
1-(4-((3-((3s,5s,7s)-adamantan-1-yl)ureido)methyl)benzyl)-1H-pyrrole-2-carboxylic acid
-
-
1-(cyclohexylsulfonyl)-N-(2,4-dichlorobenzyl)piperidine-4-carboxamide
-
27% inhibition at 200 nM
1-adamantan-1-yl-3-(5-(2-[2-(2,2,2-trifluoroethoxy)ethoxy]-ethoxy)pentyl)urea
-
-
1-adamantan-3-(5-(2-(2-ethylethoxy)ethoxy)pentyl)urea
-
highly potent and selective sEH inhibitor
1-[(1-chloroisoquinolin-5-yl)sulfonyl]-N-(2,4-dichlorobenzyl)piperidine-4-carboxamide
-
30% inhibition at 200 nM
1-[(2,4-dimethylphenyl)sulfonyl]-N-(1,2,3,4-tetrahydronaphthalen-1-yl)piperidine-4-carboxamide
-
-
1-[(2,4-dimethylphenyl)sulfonyl]-N-(2-hydroxyphenyl)piperidine-4-carboxamide
-
-
1-[(2,4-dimethylphenyl)sulfonyl]-N-(4-hydroxyphenyl)piperidine-4-carboxamide
-
-
1-[(2,4-dimethylphenyl)sulfonyl]-N-(4-methoxyphenyl)piperidine-4-carboxamide
-
-
1-[(2,4-dimethylphenyl)sulfonyl]-N-(4-phenoxyphenyl)piperidine-4-carboxamide
-
-
1-[(2,4-dimethylphenyl)sulfonyl]-N-(6-methoxy-1,3-benzodioxol-5-yl)piperidine-4-carboxamide
-
-
1-[(2,4-dimethylphenyl)sulfonyl]-N-(isoquinolin-5-yl)piperidine-4-carboxamide
-
-
1-[(2,4-dimethylphenyl)sulfonyl]-N-(naphthalen-2-yl)piperidine-4-carboxamide
-
-
1-[(2,4-dimethylphenyl)sulfonyl]-N-(tricyclo[3.3.1.13,7]dec-1-yl)piperidine-4-carboxamide
-
-
1-[(2,4-dimethylphenyl)sulfonyl]-N-[(1R,2S)-2-phenylcyclopropyl]piperidine-4-carboxamide
-
-
1-[(2,4-dimethylphenyl)sulfonyl]-N-[3-(trifluoromethyl)phenyl]piperidine-4-carboxamide
-
-
1-[(2,4-dimethylphenyl)sulfonyl]-N-[4-(morpholin-4-yl)phenyl]piperidine-4-carboxamide
-
-
1-[(2,4-dimethylphenyl)sulfonyl]-N-[4-(piperidin-1-yl)phenyl]piperidine-4-carboxamide
-
-
1-[(2,4-dimethylphenyl)sulfonyl]-N-[4-(propan-2-yl)phenyl]piperidine-4-carboxamide
-
-
1-[(2,4-dimethylphenyl)sulfonyl]-N-[4-(trifluoromethoxy)phenyl]piperidine-4-carboxamide
-
-
1-[(2,4-dimethylphenyl)sulfonyl]-N-[4-(trifluoromethyl)phenyl]piperidine-4-carboxamide
-
-
1-[(2,4-dimethylphenyl)sulfonyl]-N-[4-[(trifluoromethyl)sulfonyl]phenyl]piperidine-4-carboxamide
-
-
1-[(2-bromophenyl)sulfonyl]-N-(2,4-dichlorobenzyl)piperidine-4-carboxamide
-
63% inhibition at 200 nM
1-[(2-chloroethyl)sulfonyl]-N-(2,4-dichlorobenzyl)piperidine-4-carboxamide
-
31% inhibition at 200 nM
1-[(4-bromoisoquinolin-5-yl)sulfonyl]-N-(2,4-dichlorobenzyl)piperidine-4-carboxamide
-
37% inhibition at 200 nM
1-[(4-bromophenyl)sulfonyl]-N-(2,4-dichlorobenzyl)piperidine-4-carboxamide
-
32% inhibition at 200 nM
1-[(4-chloro-2,5-dimethylphenyl)sulfonyl]-N-(2,4-dichlorobenzyl)piperidine-4-carboxamide
-
97% inhibition at 200 nM
1-[(4-tert-butylphenyl)sulfonyl]-N-(2,4-dichlorobenzyl)piperidine-4-carboxamide
-
85% inhibition at 200 nM
1-[(5-bromothiophen-2-yl)sulfonyl]-N-(2,4-dichlorobenzyl)piperidine-4-carboxamide
-
43% inhibition at 200 nM
1-[(5-chlorothiophen-2-yl)sulfonyl]-N-(2,4-dichlorobenzyl)piperidine-4-carboxamide
-
52% inhibition at 200 nM
1-[3-(3-morpholin-4-ylpropoxy)phenyl]-3-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]thiourea
-
-
1-[3-(3-morpholin-4-ylpropoxy)phenyl]-3-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]urea
-
-
1-[3-([[4-(trifluoromethoxy)phenyl]carbamoyl]amino)benzyl]-1H-pyrrole-2-carboxylic acid
-
-
1-[4-([[4-(trifluoromethoxy)phenyl]carbamoyl]amino)benzyl]-1H-pyrrole-2-carboxylic acid
-
-
1-[[1-((adamant-1-yl)methylcarbamoyl)piperidin-4-yl]methyl]-3-[(adamant-1-yl)methyl]urea
-
-
1-[[4-(acetylamino)phenyl]sulfonyl]-N-(2,4-dichlorobenzyl)piperidine-4-carboxamide
-
53% inhibition at 200 nM
2-hydroxy-N-[3-(3-morpholin-4-ylpropoxy)phenyl]-2-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]acetamide
-
-
2-hydroxy-N-[3-(3-morpholin-4-ylpropoxy)phenyl]-3-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]propanamide
-
-
2-hydroxy-N-[3-(3-morpholin-4-ylpropoxy)phenyl]-4-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]butanamide
-
-
3-(3-(1-hydroxyureido)but-1-yn-1-yl)-N-(2-(trifluoromethyl)-benzyl)benzamide
-
dual 5-LOX/soluble epoxide hydrolase inhibitor
-
3-(3-(1-hydroxyureido)but-1-yn-1-yl)-N-(3-phenyl-3-(4-(trifluoromethoxy)phenyl)propyl)benzamide
-
dual 5-LOX/soluble epoxide hydrolase inhibitor
-
3-(3-(1-hydroxyureido)but-1-yn-1-yl)-N-(4-methoxy-2-(trifluoromethyl)benzyl)-benzamide
-
dual 5-LOX/soluble epoxide hydrolase inhibitor
-
3-(3-(1-hydroxyureido)hex-1-yn-1-yl)-N-(2-(trifluoromethyl)-benzyl)benzamide
-
dual 5-LOX/soluble epoxide hydrolase inhibitor
-
4,5-dimethoxy-2-nitrophenyl 4-[(2,4-dichlorobenzyl)carbamoyl]piperidine-1-carboxylate
-
71% inhibition at 200 nM
4-(3-(1-hydroxyureido)but-1-yn-1-yl)-N-(2-(trifluoromethyl)-benzyl)benzamide
-
dual 5-LOX/soluble epoxide hydrolase inhibitor, displays cellular activity in human polymorphonuclear leukocytes, oral bioavailability, and target engagement in vivo and demonstrates anti-inflammatory and anti-fibrotic efficiency in a kidney injury model caused by unilateral ureteral obstruction in mice
-
4-fluoro-chalcone oxide
-
0.1 mM, 87% inhibition of epoxide hydrolase activity, 8% inhibition of phosphatase activity
4-nitrophenyl 4-[(2,4-dichlorobenzyl)carbamoyl]piperidine-1-carboxylate
-
41% inhibition at 200 nM
4-phenyl-chalcone oxide
-
0.1 mM, complete inhibition of epoxide hydrolase activity, 11% inhibition of phosphatase activity
4-[([1-[(2,4-dimethylphenyl)sulfonyl]piperidin-4-yl]carbonyl)amino]benzoic acid
-
-
6-[([1-[(2,4-dimethylphenyl)sulfonyl]piperidin-4-yl]carbonyl)amino]naphthalene-2-carboxylic acid
-
-
benzil
-
inhibition of microsomal enzyme with cis-stilbene oxide, and of cytosolic enzyme forms cEHTSO and cEHCSO
carbodiimide/glycine methyl ester
-
48% inhibition at 1 mM at pH 5.2, no inhibition at pH 7.4
chalcone
-
microsomal activity with cis-stilbene oxide as substrate, cytosolic enzyme form cEHCSO and cEHTSO
ethyl 1-(2-((3-((3s,5s,7s)-adamantan-1-yl)ureido)methyl)benzyl)-1H-pyrrole-2-carboxylate
-
-
ethyl 1-(3-((3-((3s,5s,7s)-adamantan-1-yl)ureido)methyl)benzyl)-1H-pyrrole-2-carboxylate
-
-
ethyl 1-(4-((3-((3s,5s,7s)-adamantan-1-yl)ureido)methyl)benzyl)-1H-pyrrole-2-carboxylate
-
-
ethyl 1-[2-([[4-(trifluoromethoxy)phenyl]carbamoyl]amino)benzyl]-1H-pyrrole-2-carboxylate
-
-
ethyl 1-[4-([[4-(trifluoromethoxy)phenyl]carbamoyl]amino)benzyl]-1H-pyrrole-2-carboxylate
-
-
methyl 4-[([1-[(2,4-dimethylphenyl)sulfonyl]piperidin-4-yl]carbonyl)amino]benzoate
-
-
methyl 6-[([1-[(2,4-dimethylphenyl)sulfonyl]piperidin-4-yl]carbonyl)amino]naphthalene-2-carboxylate
-
-
N'-(2-chlorophenyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carbohydrazide
-
62% inhibition at 200 nM
N'-(4-fluorophenyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carbohydrazide
-
9% inhibition at 200 nM
N'-phenyl-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carbohydrazide
-
16% inhibition at 200 nM
N'-[2-(3-chlorophenyl)ethyl]-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carbohydrazide
-
65% inhibition at 200 nM
N-(1,2,3,4-tetrahydronaphthalen-1-yl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
79% inhibition at 200 nM
N-(1,3-benzodioxol-5-yl)-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
-
N-(1-tert-butoxypiperidin-4-yl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
88% inhibition at 200 nM
N-(2,3-dihydro-1H-inden-2-yl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
62% inhibition at 200 nM
N-(2,4-dichloro-6-methylbenzyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
95% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-(diphenylphosphanyl)piperidine-4-carboxamide
-
3% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-(methylsulfonyl)piperidine-4-carboxamide
-
45% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-(quinolin-5-ylsulfonyl)piperidine-4-carboxamide
-
34% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-(thiophen-2-ylcarbonyl)piperidine-4-carboxamide
-
16% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-([1-[(2,4,6-trimethylphenyl)sulfonyl]piperidin-4-yl]carbonyl)piperidine-4-carboxamide
-
31% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-[(1-methylethyl)sulfonyl]piperidine-4-carboxamide
-
13% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-[(2,4,6-tri-tert-butylphenyl)sulfonyl]piperidine-4-carboxamide
-
88% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-[(2,4,6-trimethylphenyl)carbonyl]piperidine-4-carboxamide
-
34% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
97% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
97% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-[(2-fluorophenyl)sulfonyl]piperidine-4-carboxamide
-
66% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-[(2-nitrophenyl)carbonyl]piperidine-4-carboxamide
-
44% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-[(2-nitrophenyl)sulfonyl]piperidine-4-carboxamide
-
47% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-[(3-nitrophenyl)carbonyl]piperidine-4-carboxamide
-
18% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-[(3-nitrophenyl)sulfonyl]piperidine-4-carboxamide
-
21% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-[(4-fluoro-2-nitrophenyl)sulfonyl]piperidine-4-carboxamide
-
63% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-[(4-methoxy-2,3,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
98% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-[(4-methyl-2-nitrophenyl)sulfonyl]piperidine-4-carboxamide
-
28% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-[(4-methylphenyl)sulfonyl]piperidine-4-carboxamide
-
15% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-[[2-(trifluoromethyl)phenyl]sulfonyl]piperidine-4-carboxamide
-
39% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-[[2-nitro-4-(trifluoromethyl)phenyl]sulfonyl]piperidine-4-carboxamide
-
37% inhibition at 200 nM
N-(2,4-dichlorobenzyl)-1-[[3-([4-[(2,4-dichlorobenzyl)carbamoyl]piperidin-1-yl]carbonyl)phenyl]sulfonyl]piperidine-4-carboxamide
-
45% inhibition at 200 nM
N-(2,4-difluorobenzyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
97% inhibition at 200 nM
N-(2,5-dichlorobenzyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
98% inhibition at 200 nM
N-(2-chloro-4-fluorobenzyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
98% inhibition at 200 nM
N-(2-chloro-6-fluorobenzyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
97% inhibition at 200 nM
N-(2-chlorobenzyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
90% inhibition at 200 nM
N-(2-methylcyclohexyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
77% inhibition at 200 nM
N-(2-phenylethyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
67% inhibition at 200 nM
N-(3,3-diphenylpropyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
78% inhibition at 200 nM
N-(3,4-dichlorobenzyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
97% inhibition at 200 nM
N-(3,4-dichlorophenyl)-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
-
N-(3,5-dichlorophenyl)-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
-
N-(3-(4-chlorophenyl)-3-phenylpropyl)-3-(3-(1-hydroxyureido)-but-1-yn-1-yl)benzamide
-
dual 5-LOX/soluble epoxide hydrolase inhibitor
-
N-(3-methylbutyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
87% inhibition at 200 nM
N-(4-chlorobenzyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
97% inhibition at 200 nM
N-(4-chloronaphthalen-1-yl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
44% inhibition at 200 nM
N-(4-methylcyclohexyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
86% inhibition at 200 nM
N-(cyclohexylmethyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
92% inhibition at 200 nM
N-(cyclohexylmethyl)-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
-
N-(naphthalen-1-ylmethyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
55% inhibition at 200 nM
N-(pyridin-3-ylmethyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
23% inhibition at 200 nM
N-(pyridin-4-ylmethyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
49% inhibition at 200 nM
N-benzyl-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
65% inhibition at 200 nM
N-cyclohexyl-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
87% inhibition at 200 nM
N-cyclopentyl-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
75% inhibition at 200 nM
N-morpholin-4-yl-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
14% inhibition at 200 nM
N-naphthalen-1-yl-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
50% inhibition at 200 nM
N-phenyl-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
48% inhibition at 200 nM
N-piperidin-1-yl-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
55% inhibition at 200 nM
N-piperidin-4-yl-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
15% inhibition at 200 nM
N-tert-butyl-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
3% inhibition at 200 nM
N-[(4-chlorophenyl)(phenyl)methyl]-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
7% inhibition at 200 nM
N-[1-(4-chlorophenyl)ethyl]-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
94% inhibition at 200 nM
N-[2-(4-methoxyphenyl)ethyl]-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
44% inhibition at 200 nM
N-[2-chloro-5-(trifluoromethyl)benzyl]-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
94% inhibition at 200 nM
N-[2-[4-(benzyloxy)phenyl]ethyl]-2-hydroxy-3-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]propanamide
-
-
N-[2-[4-(benzyloxy)phenyl]ethyl]-2-hydroxy-4-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]butanamide
-
-
N-[2-[4-(benzyloxy)phenyl]ethyl]-2-oxo-3-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]propanamide
-
-
N-[2-[4-(benzyloxy)phenyl]ethyl]-2-oxo-4-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]butanamide
-
-
N-[3-(3-morpholin-4-ylpropoxy)phenyl]-2-oxo-2-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]acetamide
-
-
N-[3-(3-morpholin-4-ylpropoxy)phenyl]-2-oxo-3-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]propanamide
-
-
N-[3-(3-morpholin-4-ylpropoxy)phenyl]-2-oxo-4-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]butanamide
-
-
N-[3-(3-morpholin-4-ylpropoxy)phenyl]-2-[4-(trifluoromethyl)phenyl]acetamide
-
-
N-[3-(3-morpholin-4-ylpropoxy)phenyl]-N'-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]sulfamide
-
-
N-[3-(3-morpholin-4-ylpropoxy)phenyl]-N-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-ylmethyl]formamide
-
-
N-[3-(3-morpholin-4-ylpropoxy)phenyl]-N-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]formamide
-
-
N-[3-(3-morpholin-4-ylpropoxy)phenyl]-N2-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]glycinamide
-
-
N-[3-carbamoyl-4-(piperidin-1-yl)phenyl]-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
-
N-[4-(benzyloxy)phenyl]-2-hydroxy-2-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]acetamide
-
-
N-[4-(benzyloxy)phenyl]-2-hydroxy-3-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]propanamide
-
-
N-[4-(benzyloxy)phenyl]-2-oxo-2-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]acetamide
-
-
N-[4-(benzyloxy)phenyl]-2-oxo-3-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]propanamide
-
-
N-[4-chloro-3-(trifluoromethyl)benzyl]-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
96% inhibition at 200 nM
N-[4-chloro-3-(trifluoromethyl)phenyl]-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
-
sorafenib
-
a vascular endothelial growth factor receptor, inhibits sEH, effects in vivo, causes a shift in oxylipid profile and reduces the acute inflammatory response, overview. Reverses lipopolysaccharide-induced hypotension
tert-butyl 4-[([1-[(2,4-dimethylphenyl)sulfonyl]piperidin-4-yl]carbonyl)amino]piperidine-1-carboxylate
-
-
trans-4-[4-(3-adamantan-1-yl-ureido)cyclohexyloxy]benzoic acid
-
potent sEH inhibitor
[3-(4-phenoxycyclohexa-1,5-dien-1-yl)oxiran-2-yl](phenyl)methanone
-
IC50 is 0.00051 mM
[4-(bromomethyl)phenyl][3-(2-naphthyl)oxiran-2-yl]methanone
-
IC50 is 0.00016 mM
1-(1-acetypiperidin-4-yl)-3-adamantanylurea
APAU, a tight binding inhibitor of enzyme sEH
1-[5-[2-(2-ethoxyethoxy)ethoxy]pentyl]-3-tricyclo[3.3.1.13,7]dec-1-ylurea
-
12-[(tricyclo[3.3.1.13,7]dec-1-ylcarbamoyl)amino]dodecanoic acid
-
12-[[(tricyclo[3.3.1.13,7]dec-1-ylamino)carbonyl]amino]-dodecanoic acid
AUDA
12-[[(tricyclo[3.3.1.13,7]dec-1-ylamino)carbonyl]amino]-dodecanoic acid
i.e. AUDA
5,7-dihydroxy-2-(2-hydroxy-6-methoxyphenyl)-4H-1-benzopyran-4-one
65.12% inhibition
5,7-dihydroxy-2-(2-hydroxy-6-methoxyphenyl)-4H-1-benzopyran-4-one
76.33% inhibition
N-adamantan-1-yl-N'-[5-[2-(2-ethoxyethoxy)ethoxy]pentyl]urea
AEPU, a tight binding inhibitor of enzyme sEH
trans-4-[4-(3-adamantan-1-yl-ureido)-cyclohexyloxy]-benzoic acid
i.e. t-AUCB
trans-4-[4-(3-adamantan-1-ylureido)-cyclohexyloxy]-benzoic acid
-
trans-4-[4-(3-adamantan-1-ylureido)-cyclohexyloxy]-benzoic acid
t-AUCB, a tight binding inhibitor of enzyme sEH
1,3-dicyclohexyl urea
-
0.1 mM, complete inhibition of epoxide hydrolase activity, no inhibition of phosphatase activity
1-cyclohexyl-3-dodecyl urea
-
0.1 mM, complete inhibition of epoxide hydrolase activity, no inhibition of phosphatase activity
1-cyclohexyl-3-ethyl urea
-
0.1 mM, 54% inhibition of epoxide hydrolase activity, no inhibition of phosphatase activity
1-cyclohexyl-3-hexyl urea
-
0.1 mM, complete inhibition of epoxide hydrolase activity, 4% inhibition of phosphatase activity
12-(3-adamantan-1-yl-ureido)dodecanoic acid
-
potent transition state inhibitor of sEH
Chalcone oxide
-
0.1 mM, 80% inhibition of epoxide hydrolase activity, no inhibition of phosphatase activity
N-cycloheptyl-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
-
90% inhibition at 200 nM
Zn2+
-
noncompetitive, inhibits epoxide hydrolase and phosphatase activities, allosteric mechanism
additional information
design and synthesis of a series of potent nicotinamide inhibitors of soluble epoxides hydrolase, structure-guided optimization, overview
-
additional information
-
design and synthesis of a series of potent nicotinamide inhibitors of soluble epoxides hydrolase, structure-guided optimization, overview
-
additional information
evaluation of spirocyclic secondary amine-derived trisubstituted ureas as highly potent, bioavailable and selective soluble epoxide hydrolase inhibitors, overview
-
additional information
inhibitor screening and structure-function analysis, overview
-
additional information
Inhibitors of human sEH are effective drug candidates for the treatment of cardiovascular diseases, inhibitor screening with recombinant enzyme, overview
-
additional information
-
Inhibitors of human sEH are effective drug candidates for the treatment of cardiovascular diseases, inhibitor screening with recombinant enzyme, overview
-
additional information
sEH inhibitors are developed to enhance the cardiovascular actions of epoxyeicosatrienoic acids, treatment potentials, cardiovascular therapeutic effects, antihypertensive effects, kidney-protective properties, cardiac-protective properties, and protection against ischaemic stroke and vascular disease of sEH inhibitors, overview
-
additional information
synthesis and structure-based optimization of arylamides sEH inhibitors based on the solid-state costructure of N-(3,3-diphenyl-propyl)-nicotinamide, overview. Assessment of inhibitor stability in liver microsomes, overview
-
additional information
-
synthesis and structure-based optimization of arylamides sEH inhibitors based on the solid-state costructure of N-(3,3-diphenyl-propyl)-nicotinamide, overview. Assessment of inhibitor stability in liver microsomes, overview
-
additional information
design and synthesis of three substituted cyclopropyl urea derivatives as strong sEH inhibitors using X-ray co-crystal structure of sEH catalytic domain and 3-[4-[(1-[[(1S,2R)-2-phenylcyclopropyl]carbamoyl]piperidin-4-yl)oxy]phenyl]propanoic acid, overview. cis-Configuration together with a phenyl group result in increased human and rat sEH inhibitory activity with minimal species difference
-
additional information
-
design and synthesis of three substituted cyclopropyl urea derivatives as strong sEH inhibitors using X-ray co-crystal structure of sEH catalytic domain and 3-[4-[(1-[[(1S,2R)-2-phenylcyclopropyl]carbamoyl]piperidin-4-yl)oxy]phenyl]propanoic acid, overview. cis-Configuration together with a phenyl group result in increased human and rat sEH inhibitory activity with minimal species difference
-
additional information
identification of N-ethylmethylamine as a scaffold for inhibitors of soluble epoxide hydrolase by crystallographic fragment screening, overview. N-Ethylmethylamine is identified as a promising scaffold that forms hydrogen bonds with the catalytic residues of sEH, Asp335, Tyr383, and Tyr466. Compounds containing this scaffold are selected from a chemical library and evaluated for inhibitory potency. Enzyme-inhibitor interaction analysis
-
additional information
in vitro and in vivo metabolism of N-adamantyl substituted urea-based soluble epoxide hydrolase inhibitors, identification of ligands structures by mass spectrometry and NMR spectroscopy, overview
-
additional information
-
in vitro and in vivo metabolism of N-adamantyl substituted urea-based soluble epoxide hydrolase inhibitors, identification of ligands structures by mass spectrometry and NMR spectroscopy, overview
-
additional information
inhibitory potency and metabolic stability of adamantyl ureas and diureas bearing substituents in bridgehead positions of adamantane and/or spacers between urea groups and adamantane group. Comparison of the effects of the inhibitors on human, rat, and murine enzymes, overview
-
additional information
-
inhibitory potency and metabolic stability of adamantyl ureas and diureas bearing substituents in bridgehead positions of adamantane and/or spacers between urea groups and adamantane group. Comparison of the effects of the inhibitors on human, rat, and murine enzymes, overview
-
additional information
interaction of the enzyme with anthocyanin derivatives, molecular docking study, molecular dynamics study, overview. The molecular docking study shows a small pocket next to the active site, which is thought to be a common allosteric site, which probably is the binding site of noncompetitive and mixed inhibitors. Moreover, the anthocyanin core is located at the hydrophobic position of the inner allosteric site. The sugar moiety interacts with amino acid residues on the outside of the allosteric site. In particular, the hydroxyl group in the sugar of the compounds is bonded with the nitrogen of Trp525. The amino acid residue may play a key role in forming hydrogen bonds with the anthocyanin glycoside. Additionally, the molecular dynamics study confirms that anthocyanin 4 can form hydrogen bonds with this residue for 10 ns
-
additional information
N-benzylbenzamides are a merged scaffold for orally available dual soluble epoxide hydrolase/peroxisome proliferator-activated receptor gamma modulators, synthesis and inhibitory potencies, overview. Design of dual-target ligands that target soluble epoxide hydrolase (sEH) and the peroxisome proliferator-activated receptor type gamma (PPARgamma). Simultaneous modulation of sEH and PPARgamma can improve diabetic conditions and hypertension at once
-
additional information
-
N-benzylbenzamides are a merged scaffold for orally available dual soluble epoxide hydrolase/peroxisome proliferator-activated receptor gamma modulators, synthesis and inhibitory potencies, overview. Design of dual-target ligands that target soluble epoxide hydrolase (sEH) and the peroxisome proliferator-activated receptor type gamma (PPARgamma). Simultaneous modulation of sEH and PPARgamma can improve diabetic conditions and hypertension at once
-
additional information
phytochemical constituents from Scutellaria baicalensis in soluble epoxide hydrolase inhibition: kinetics and interaction mechanism merged with simulations, overview. Extracts of Scutellaria baicalensis are separated, resulting in the isolation of thirty compounds, including six lignins, sixteen flavones, and five amides. Their structures are determined on the basis of 1H and 13C NMR and MS spectra. Molecular docking studies and inhibition mechanisms of (2E,4E)-5-(2H-1,3-benzodioxol-5-yl)-N-(2-methylpropyl)penta-2,4-dienamide, (2E)-5-(2H-1,3-benzodioxol-5-yl)-N-(2-methylpropyl)pent-2-enamide, and (2E,6E)-7-(2H-1,3-benzodioxol-5-yl)-N-(2-methylpropyl)hepta-2,6-dienamide against sEH
-
additional information
structural analysis of enzyme-inhibitor interactions, molecular interaction calculations, active site binding analysis, molecular docking, overview
-
additional information
synthesis and properties of 1-(R-adamant-1-yl)-3-(1-propionylpiperidin-4-yl)ureas and 4-({4-[3-(R-adamant-1-yl)ureido]cyclohexyl}oxy)benzoic acids, efficient target-oriented human soluble epoxide hydrolase inhibitors, overview. Determination of solubilities in water, lipophilicity coefficients, and melting points
-
additional information
synthesis and properties of symmetrical N,N-bis(R-adamantan-1-yl)ureas as target-oriented soluble epoxide hydrolase (sEH) inhibitors, structure is confirmed by 1H NMR and mass spectra and elemental analyses
-
additional information
synthesis of series of targetx02oriented competitive inhibitors of human soluble epoxide hydrolase. Molecular modeling reveals that the high inhibitory activity of this series of compounds is achieved by a unique mode of the binding to the active site of the enzyme, molecular docking study
-
additional information
-
IC50 values with different substrates and structure-activity relationships of enzyme inhibitors, development of an in vitro inhibition assay using fluorogenic substrates
-
additional information
-
inhibition mechanism of sulfates, sulfonates, and phosphonates
-
additional information
-
irreversible inhibition mechanism of chalcone oxide derivatives, quantitative structure-activity relationship, QSAR, overview
-
additional information
-
metal chelators like 1,10-phenanthroline, 1,7-phenanthroline, EDTA, EGTA, and dipicolinic acid preserve enzyme activity in presence of metal ions
-
additional information
-
most enzyme inhibitors do not influence the enzyme's phosphatase activity
-
additional information
-
N-acetyl imidazole, N-bromosuccimide, cyclohexandione, acetaldehyde/borohydride and benzaldehyde/borohydride are poor inhibitors, no inhibition by PMSF and diisopropyl fluorophosphate, no inhibition by amino-, guanido-, or activated serine-selective reagents
-
additional information
-
poor or no inhibition by tartaric acid, sodium fluoride, and sodium molybdate
-
additional information
-
QSAR and classification in a seven-discriptor model of enzyme inhibition by 348 urea-like compounds, IC50 ranging from 60 nM to 0.5 mM, overview
-
additional information
-
the herb extract prepared from Sophora flavescens root afford the strongest inhibition of sEH with an IC50 of 0.00207 mg/ml, this is followed by other three extracts derived from the rhizome of Glycyrrhiza uralensis (IC50 0.0071 mg/ml), the root of Bupleurum chinense (IC50 0.00956 mg/ml), and the whole weed of Swertia pseudochinensis (IC50 0.01131 mg/ml)
-
additional information
-
no inhibition by sunitinib, another vascular endothelial growth factor receptor. The classical sEH inhibitors do not cause growth inhibition and apoptosis and do not synergize with sorafenib
-
additional information
-
sEH inhibition has antihypertensive and antiinflammatory actions, presumably due to the increased bioavailability of endogenous EETs and other epoxylipids, and several potent sEH inhibitors are developed and tested in animal models of cardiovascular disease including hypertension, cardiac hypertrophy, and ischemia/reperfusion injury
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-Benzylimidazole
-
activates mirosomal activity with styrene oxide as substrate
additional information
-
the enzyme is induced by several substances, e.g. 2-acetylfluorene, alpha-1-acetylmethadol, butylated hydroxyanisole, butylated hydroxytoluene, chalcone, gamma-chlordane, 1,2-dibromo-3-chloropropane, ethoxyquin, isosafrole, 3-methylcholanthrene, alpha-naphthoflavone, phenobarbital, polychlorinated and/or polybrominated biphenyls, pregnenolone-16alpha-carbonitrile, and trans-stilbene oxide
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0108
(10R)-hydroxy-(11S,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoic acid
-
pH 7.4, 37°C
0.0073
(8R)-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoic acid
-
pH 7.4, 37°C
0.006
1-myristoyl-sn-glycerol 3-phosphate
mutant enzyme C154Y, at pH 7.4 and 30°C
0.007
1-myristoyl-sn-glycerol 3-phosphate
mutant enzyme R103C, at pH 7.4 and 30°C
0.011
1-myristoyl-sn-glycerol 3-phosphate
wild type enzyme, at pH 7.4 and 30°C
0.012
1-myristoyl-sn-glycerol 3-phosphate
mutant enzyme R287Q, at pH 7.4 and 30°C
0.019
1-myristoyl-sn-glycerol 3-phosphate
mutant enzyme K55R, at pH 7.4 and 30°C
0.007
14,15-epoxyeicosatrienoic acid
wild type enzyme, at pH 7.4 and 30°C
0.0074
14,15-epoxyeicosatrienoic acid
mutant enzyme K55R, at pH 7.4 and 30°C
0.009
14,15-epoxyeicosatrienoic acid
mutant enzyme R287Q, at pH 7.4 and 30°C
0.0092
14,15-epoxyeicosatrienoic acid
mutant enzyme C154Y, at pH 7.4 and 30°C
0.01
14,15-epoxyeicosatrienoic acid
mutant enzyme R103C, at pH 7.4 and 30°C
0.0033
trans-1,3-diphenylpropene oxide
wild type enzyme, at pH 7.4 and 30°C
0.004
trans-1,3-diphenylpropene oxide
mutant enzyme C154Y, at pH 7.4 and 30°C
0.0058
trans-1,3-diphenylpropene oxide
mutant enzyme K55R, at pH 7.4 and 30°C
0.0059
trans-1,3-diphenylpropene oxide
mutant enzyme R103C, at pH 7.4 and 30°C
0.0101
trans-1,3-diphenylpropene oxide
mutant enzyme R287Q, at pH 7.4 and 30°C
additional information
additional information
steady-state enzyme kinetics study, overview
-
additional information
additional information
-
kinetics, the hydrolysis of the intermediate is the rate-limiting step
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
(10R)-hydroxy-(11S,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoic acid
-
pH 7.4, 37°C
0.42
(8R)-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoic acid
-
pH 7.4, 37°C
0.0046
1-myristoyl-sn-glycerol 3-phosphate
mutant enzyme R287Q, at pH 7.4 and 30°C
0.068
1-myristoyl-sn-glycerol 3-phosphate
mutant enzyme R103C, at pH 7.4 and 30°C
0.15
1-myristoyl-sn-glycerol 3-phosphate
wild type enzyme, at pH 7.4 and 30°C
0.32
1-myristoyl-sn-glycerol 3-phosphate
mutant enzyme C154Y, at pH 7.4 and 30°C
0.41
1-myristoyl-sn-glycerol 3-phosphate
mutant enzyme K55R, at pH 7.4 and 30°C
0.44
14,15-epoxyeicosatrienoic acid
mutant enzyme R287Q, at pH 7.4 and 30°C
2.1
14,15-epoxyeicosatrienoic acid
mutant enzyme R103C, at pH 7.4 and 30°C
7.5
14,15-epoxyeicosatrienoic acid
mutant enzyme K55R, at pH 7.4 and 30°C
15
14,15-epoxyeicosatrienoic acid
mutant enzyme C154Y, at pH 7.4 and 30°C
0.076
trans-1,3-diphenylpropene oxide
mutant enzyme R287Q, at pH 7.4 and 30°C
0.76
trans-1,3-diphenylpropene oxide
mutant enzyme R103C, at pH 7.4 and 30°C
0.99
trans-1,3-diphenylpropene oxide
wild type enzyme, at pH 7.4 and 30°C
1.72
trans-1,3-diphenylpropene oxide
mutant enzyme K55R, at pH 7.4 and 30°C
2.55
trans-1,3-diphenylpropene oxide
mutant enzyme C154Y, at pH 7.4 and 30°C
additional information
additional information
-
ratio kcat/Km value is 0.115 per s and microM
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.4
1-myristoyl-glycerol-3-phosphate
mutant enzyme R287Q, at pH 7.4 and 30°C
10
1-myristoyl-glycerol-3-phosphate
mutant enzyme R103C, at pH 7.4 and 30°C
22
1-myristoyl-glycerol-3-phosphate
mutant enzyme K55R, at pH 7.4 and 30°C
52
1-myristoyl-glycerol-3-phosphate
mutant enzyme C154Y, at pH 7.4 and 30°C
50
14,15-epoxyeicosatrienoic acid
mutant enzyme R287Q, at pH 7.4 and 30°C
210
14,15-epoxyeicosatrienoic acid
mutant enzyme R103C, at pH 7.4 and 30°C
1000
14,15-epoxyeicosatrienoic acid
mutant enzyme K55R, at pH 7.4 and 30°C
1600
14,15-epoxyeicosatrienoic acid
mutant enzyme C154Y, at pH 7.4 and 30°C
8
trans-1,3-diphenylpropene oxide
mutant enzyme R287Q, at pH 7.4 and 30°C
130
trans-1,3-diphenylpropene oxide
mutant enzyme R103C, at pH 7.4 and 30°C
300
trans-1,3-diphenylpropene oxide
mutant enzyme K55R, at pH 7.4 and 30°C
640
trans-1,3-diphenylpropene oxide
mutant enzyme C154Y, at pH 7.4 and 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00435
(2E)-5-(2H-1,3-benzodioxol-5-yl)-N-(2-methylpropyl)pent-2-enamide
pH not specified in the publication, 37°C
0.0029
(2E,4E)-5-(2H-1,3-benzodioxol-5-yl)-N-(2-methylpropyl)penta-2,4-dienamide
pH not specified in the publication, 37°C
0.00158
(2E,6E)-7-(2H-1,3-benzodioxol-5-yl)-N-(2-methylpropyl)hepta-2,6-dienamide
pH not specified in the publication, 37°C
0.0000027
1,1'-(butane-1,4-diyl)bis(3-[1-(adamantan-1-yl)ethyl]urea)
pH and temperature not specified in the publication
0.0000031
1,1'-(octane-1,8-diyl)bis(3-[1-(adamantan-1-yl)ethyl]urea)
pH and temperature not specified in the publication
0.0000146
1-(1-acetylpiperidin-4-yl)-3-[4-(trifluoromethyl)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000223
1-(1-butanoylpiperidin-4-yl)-3-[4-(trifluoromethyl)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000296
1-(1-propanoylpiperidin-4-yl)-3-[4-(trifluoromethyl)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000244
1-(4-tert-butylphenyl)-3-[1-(2-methylbutanoyl)piperidin-4-yl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000023
1-(cis-4-ethylcyclohexyl)-3-[1-(2-methylbutanoyl)piperidin-4-yl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000099
1-cycloheptyl-3-[1-(2-methylbutanoyl)piperidin-4-yl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000423
1-cyclohexyl-3-[1-(2-methylbutanoyl)piperidin-4-yl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000091
1-trifluoromethoxyphenyl-3-(1-propionylpiperidin-4-yl)-urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000117
1-[1-(2-methylbutanoyl)piperidin-4-yl]-3-[4-(propan-2-yl)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000036
1-[1-(2-methylbutanoyl)piperidin-4-yl]-3-[4-(trifluoromethoxy)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000037
1-[1-(2-methylbutanoyl)piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000031
1-[1-(2-methylpropanoyl)piperidin-4-yl]-3-[4-(trifluoromethoxy)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000066
1-[1-(2-methylpropanoyl)piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000049
1-[1-(3-methylbutanoyl)piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.0000012
1-[1-(4,4,4-trifluorobutanoyl)piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000044
1-[1-(butylsulfonyl)piperidin-4-yl]-3-[4-(trifluoromethoxy)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000098
1-[1-(butylsulfonyl)piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000049
1-[1-(cyclopropylcarbonyl)piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000122
1-[1-(cyclopropylsulfonyl)piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000174
1-[1-(ethylsulfonyl)piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000716
1-[1-(methylsulfonyl)piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000117
1-[1-(propan-2-ylsulfonyl)piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000147
1-[1-(propylsulfonyl)piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000179
1-[1-[(2,2,2-trifluoroethyl)sulfonyl]piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000019
1-[1-[(2S)-2-methylbutanoyl]piperidin-4-yl]-3-[4-(trifluoromethoxy)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000022
1-[1-[(2S)-2-methylbutanoyl]piperidin-4-yl]-3-[4-(trifluoromethyl)phenyl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000002
1-[4-(1,1,1,2,3,3,3-heptafluoropropan-2-yl)phenyl]-3-[1-(2-methylbutanoyl)piperidin-4-yl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000002
1-[4-(1,1,1,2,3,3,3-heptafluoropropan-2-yl)phenyl]-3-[1-(3,3,3-trifluoropropanoyl)piperidin-4-yl]urea
Ki below 0.00000002 mM, in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.00000043
1-[4-(trifluoromethyl)phenyl]-3-[1-(3,3,3-trifluoropropanoyl)piperidin-4-yl]urea
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.0000112
2-[1-[(2S)-2-methylbutanoyl]piperidin-4-yl]-N-[4-(trifluoromethoxy)phenyl]acetamide
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.000111
N-[1-[(2S)-2-methylbutanoyl]piperidin-4-yl]-2-[4-(trifluoromethoxy)phenyl]acetamide
in sodium phosphate buffer (0.1 M, pH 7.4), at 30°C
0.0000034
N-[6-([[(adamantan-1-yl)methyl]carbamoyl]amino)hexyl]-N'-[(3,5-dimethyladamantan-1-yl)methyl]urea
pH and temperature not specified in the publication
0.0000031
1,8-(octamethylene)bis[(adamant-1-ylethyl)urea]
-
pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
(1R,2R,4R,5S,6R,7S)-4-[(benzyloxy)methyl]-3,8-dioxatricyclo[5.1.0.02,4]octane-5,6-diyl diacetate
Homo sapiens
above, pH not specified in the publication, 37°C
0.03764
(1S,6S,9R)-1-(4-hydroxy-3-methoxyphenyl)-6-methoxy-9-methyl-4-(prop-2-en-1-yl)-7-oxabicyclo[4.2.1]non-4-ene-3,8-dione
Homo sapiens
pH not specified in the publication, 37°C
0.1
(2E)-4-[(2-methylpropyl)amino]-4-oxobut-2-enoic acid
Homo sapiens
pH not specified in the publication, 37°C
0.00783
(2E)-5-(2H-1,3-benzodioxol-5-yl)-N-(2-methylpropyl)pent-2-enamide
Homo sapiens
pH not specified in the publication, 37°C
0.00606
(2E,4E)-5-(2H-1,3-benzodioxol-5-yl)-N-(2-methylpropyl)penta-2,4-dienamide
Homo sapiens
pH not specified in the publication, 37°C
0.09368
(2E,4E)-N-(2-methylpropyl)deca-2,4-dienamide
Homo sapiens
pH not specified in the publication, 37°C
0.00632
(2E,6E)-7-(2H-1,3-benzodioxol-5-yl)-N-(2-methylpropyl)hepta-2,6-dienamide
Homo sapiens
pH not specified in the publication, 37°C
0.1
(2R,3R)-2-(2,6-dihydroxyphenyl)-3,5,7-trihydroxy-2,3-dihydro-4H-1-benzopyran-4-one
Homo sapiens
above, pH not specified in the publication, 37°C
0.02616
(2R,3R,3aS)-2-(4-hydroperoxy-3-methoxyphenyl)-3a-methoxy-3-methyl-5-(prop-2-en-1-yl)-3,3a-dihydro-1-benzofuran-6(2H)-one
Homo sapiens
pH not specified in the publication, 37°C
0.1
(2R,3R,4S,5S)-2,5-bis(3,4-dimethoxyphenyl)-3,4-dimethyloxolane
Homo sapiens
above, pH not specified in the publication, 37°C
0.1
(2R,3S,4S,5S)-2,5-bis(3,4-dimethoxyphenyl)-3,4-dimethyloxolane
Homo sapiens
above, pH not specified in the publication, 37°C
0.07619
(2S)-5,7-dihydroxy-6-methoxy-2-phenyl-2,3-dihydro-4H-1-benzopyran-4-one
Homo sapiens
pH not specified in the publication, 37°C
0.05661
(2S,3R,3aR)-2-(4-hydroperoxy-3-methoxyphenyl)-3a-methoxy-3-methyl-5-(prop-2-en-1-yl)-3,3a-dihydro-1-benzofuran-6(2H)-one
Homo sapiens
pH not specified in the publication, 37°C
0.0000007
(3R)-N-[(1s,2R,3S)-2,3-diphenylcyclopropyl]-3-[(4-fluorobenzene-1-sulfonyl)amino]piperidine-1-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0000014
(3R)-N-[(1s,2R,3S)-2,3-diphenylcyclopropyl]-3-[(methanesulfonyl)amino]piperidine-1-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00012
(E)-4-[N-((2-trifluoromethyl)benzyl)benzamide]-alpha-ethylcinnamic acid
Homo sapiens
pH 7.0, 22°C
0.00007
(E)-N-methoxy-N-methyl 3-[4-(N-((2-trifluoromethyl)benzyl)-benzamide)]but-2-enamide
Homo sapiens
pH 7.0, 22°C
0.000014
(R)-4-cyano-N-[3-(4-fluorophenyl)-3-(4-methanesulfonyl-phenyl)-propyl]-benzamide
Homo sapiens
-
0.000023
(R)-N-[3-(4-fluorophenyl)-3-(4-methanesulfonyl-phenyl)-propyl]-6-hydroxy-nicotinamide
Homo sapiens
-
0.000008
(S)-4-cyano-N-[3-(4-fluorophenyl)-3-(4-methanesulfonyl-phenyl)-propyl]-benzamide
Homo sapiens
-
0.000006
(S)-N-[3-(4-fluorophenyl)-3-(4-methanesulfonyl-phenyl)-propyl]-6-hydroxy-nicotinamide
Homo sapiens
-
0.0000026
1,1'-(butane-1,4-diyl)bis(3-[1-(adamantan-1-yl) butane-2-yl]urea)
Homo sapiens
pH and temperature not specified in the publication
0.0000012
1,1'-(butane-1,4-diyl)bis(3-[1-(adamantan-1-yl)ethyl]urea)
Homo sapiens
pH and temperature not specified in the publication
0.0000028
1,1'-(hexane-1,6-diyl)bis(3-[1-(adamantan-1-yl) butane 2 yl]urea)
Homo sapiens
pH and temperature not specified in the publication
0.0000005
1,1'-(hexane-1,6-diyl)bis(3-[1-(adamantan-1-yl)ethyl]urea)
Homo sapiens
pH and temperature not specified in the publication
0.001442
1,1'-(octane-1,8-diyl)bis(3-[1-(adamantan-1-yl)butan 2 yl]urea)
Homo sapiens
pH and temperature not specified in the publication
0.0000005
1,1'-(octane-1,8-diyl)bis(3-[1-(adamantan-1-yl)ethyl]urea)
Homo sapiens
pH and temperature not specified in the publication
0.002475
1,1'-(phenylene 1,4)bis(3-[3,5-dimethyl(adamantan-1-yl)]urea)
Homo sapiens
pH and temperature not specified in the publication
0.01
1,1'-(phenylene-1,4)bis(3-[1-(adamantan-1-yl)butan-2-yl]urea)
Homo sapiens
pH and temperature not specified in the publication
0.000162
1,1'-(phenylene-1,4)bis(3-[1-(adamantan-1-yl)ethyl]urea)
Homo sapiens
pH and temperature not specified in the publication
0.00002
1,1'-(phenylene-1,4)bis[3-([adamantan-1-yl)urea]
Homo sapiens
pH and temperature not specified in the publication
0.0074
1-(1-cyclopropylethyl)-3-phenylurea
Homo sapiens
in 25 mM Bis-Tris HCl, pH 7.0, and 0.02% (v/v) Triton X-100, at 22°C
0.0000029
1-(1-methanesulfonyl-piperidin-4-yl)-3-(4-trifluoromethoxy-phenyl)-urea
Homo sapiens
-
0.0000016
1-(1-nicotinoylpiperidin-4-yl)-3-(4-(trifluoromethoxy)phenyl)-urea
Homo sapiens
-
0.000007
1-(3,4-dihydro-1'H-spiro[chromene-2,4'-piperidin]-1'-yl)-3-phenylpropan-1-one
Homo sapiens
-
0.000029
1-(3-(5-(hydroxyureido)methyl-2-methoxyphenoxy)propyl)-3-[4-(trifluoromethoxy)phenyl]urea
Homo sapiens
recombinant enzyme, pH 7.0, 22°C
0.0000012
1-(4-(N1-methyl-N2-methyl-N2-(methyloxy)oxalamido)-benzyl)-3-adamantylurea
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.000019
1-(4-(N2-(tetrahydro-2H-pyran-2-yloxy)oxalamido)benzyl)-3-adamantylurea
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.000005
1-(4-(N2-methyl-N2-(methyloxy)oxalamido)benzyl)-3-adamantylurea
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.0000066
1-(4-(N2-methyloxyoxalamido)benzyl)-3-adamantylurea
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.000019
1-(4-(N2-tert-butyloxyoxalamido)benzyl)-3-adamantylurea
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.0000036
1-(4-acetylphenyl)-N-(5-chloro-1,3-benzoxazol-2-yl)piperidine-4-carboxamide
Homo sapiens
pH 7.4, 22°C
0.0000036
1-(4-acetylphenyl)-N-(5-methyl-1,3-benzoxazol-2-yl)piperidine-4-carboxamide
Homo sapiens
pH 7.4, 22°C
0.0000032
1-(adamantan-1-yl)-3-(1-propionylpiperidin-4-yl)urea
Homo sapiens
pH 7.4, 37°C
0.000014
1-adamantan-1-yl-3-(5-[2-(2-ethoxyethoxy)ethoxy]pentyl)urea
Homo sapiens
pH 7.4, 30°C
0.000016
1-benzyl-3-tricyclo[3.3.1.13,7]dec-1-ylurea
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.0000037
1-trifluoromethoxyphenyl-3-(1-propionylpiperidin-4-yl)urea
Homo sapiens
pH 7.4, 37°C
0.000003
1-[1-(methylsulfonyl)piperidin-4-yl]-3-[4-(trifluoromethoxy)phenyl]urea
Homo sapiens
-
0.000008 - 0.000014
1-[5-[2-(2-ethoxyethoxy)ethoxy]pentyl]-3-tricyclo[3.3.1.13,7]dec-1-ylurea
0.0000032
12-(3-adamantan-1-yl-ureido)dodecanoic acid
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.000002
12-[[(tricyclo[3.3.1.13,7]dec-1-ylamino)carbonyl]amino]-dodecanoic acid
Homo sapiens
pH 7.0, 37°C
0.127
2-(1-methyl-1H-pyrazol-4-yl)-1H-benzimidazole
Homo sapiens
in 25 mM Bis-Tris HCl, pH 7.0, and 0.02% (v/v) Triton X-100, at 22°C
0.000001
2-(2,4-dichlorophenyl)-1-[6-(methylsulfonyl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidin]-1'-yl]ethanone
Homo sapiens
-
0.1
2-(2,6-dihydroxyphenyl)-3,5,7-trihydroxy-4H-1-benzopyran-4-one
Homo sapiens
above, pH not specified in the publication, 37°C
0.009
2-(2-fluorophenyl)-N-[(5-methylthiophen-2-yl)methyl]ethan-1-amine
Homo sapiens
37°C, pH 7.0
0.0043
2-(3,4-dihydroxy-5-methoxyphenyl)-5,7-dihydroxy-1-benzopyran-1-ium-3-yl beta-D-glucopyranoside
Homo sapiens
pH 7.0, 37°C
0.0102
2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-1-benzopyran-1-ium
Homo sapiens
pH 7.0, 37°C
0.0146
2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-1-benzopyran-1-ium-3-yl beta-D-glucopyranoside
Homo sapiens
pH 7.0, 37°C
0.0000283
2-(tricyclo[3.3.1.13,7]dec-1-yl)-N-[1-(trifluoroacetyl)piperidin-4-yl]acetamide
Homo sapiens
-
0.015
2-cyclopentyl-N-(1,3-thiazol-2-yl)acetamide
Homo sapiens
in 25 mM Bis-Tris HCl, pH 7.0, and 0.02% (v/v) Triton X-100, at 22°C
0.0012
2-ethyl 3-[4-(N-(4-fluoro(2-trifluoromethyl)benzyl)-benzamide)]propionic acid
Homo sapiens
pH 7.0, 22°C
0.0009
2-ethyl-3-[3-(N-((2-trifluoromethyl)benzyl)benzamide)]-propionic acid
Homo sapiens
pH 7.0, 22°C
0.0016
2-ethyl-3-[4-(N-((2-trifluoromethyl)benzyl)benzamide)]-propionic acid
Homo sapiens
pH 7.0, 22°C
0.0015
2-ethyl-3-[4-(N-((4-chloro)benzyl)benzamide)]propionic acid
Homo sapiens
pH 7.0, 22°C
0.012
2-ethyl-3-[4-(N-((4-phenoxy)benzyl)benzamide)]propionic acid
Homo sapiens
pH 7.0, 22°C
0.014
2-ethyl-3-[4-(N-((4-trifluoromethoxy)benzyl)benzamide)]-propionic acid
Homo sapiens
pH 7.0, 22°C
0.0072
2-ethyl-3-[4-(N-((4-trifluoromethyl)benzyl)benzamide)]-propionic acid
Homo sapiens
pH 7.0, 22°C
0.00033
2-ethyl-3-[4-(N-(4-methoxy(2-trifluoromethyl)benzyl)-benzamide)]propionic acid
Homo sapiens
pH 7.0, 22°C
0.02082
2-methoxy-4-[7-methoxy-3-methyl-5-[(1E)-prop-1-en-1-yl]-1-benzofuran-2-yl]phenol
Homo sapiens
pH not specified in the publication, 37°C
0.008
2-methyl 3-[4-(N-((2-Trifluoromethyl)benzyl)benzamide)]-propionic acid
Homo sapiens
pH 7.0, 22°C
0.0025
2-phenyl-3-[4-(N-((2-trifluoromethyl)benzyl)benzamide)]-propionic acid
Homo sapiens
pH 7.0, 22°C
0.005
2-propyl-3-[4-(N-((2-trifluoromethyl)benzyl)benzamide)]-propionic acid
Homo sapiens
pH 7.0, 22°C
0.0001199
2-[2-(adamantan-1-yl)ethyl]-N-(3,5-dimethyladamantan-1-yl)hydrazine-1-carboxamide
Homo sapiens
pH 7.4, 37°C
0.0000285
2-[2-(adamantan-1-yl)ethyl]-N-[(adamantan-1-yl)methyl]hydrazine-1-carboxamide
Homo sapiens
pH 7.4, 37°C
0.0000796
2-[3-(adamantan-1-yl)propyl]-N-(3,5-dimethyladamantan-1-yl)hydrazine-1-carboxamide
Homo sapiens
pH 7.4, 37°C
0.0055
2-[4-(N-((2-trifluoromethyl)benzyl )benzamide)]-cyclopropanecarboxylic acid
Homo sapiens
pH 7.0, 22°C
0.000004
3,4-dihydro-1'H-spiro[chromene-2,4'-piperidin]-1'-yl[4-(trifluoromethyl)phenyl]methanone
Homo sapiens
-
0.195
3-(2-amino-1,3-thiazol-4-yl)-5-methyl-1-(tetrahydrofuran-2-ylmethyl)-1H-pyrrol-2-ol
Homo sapiens
in 25 mM Bis-Tris HCl, pH 7.0, and 0.02% (v/v) Triton X-100, at 22°C
0.000005
3-(3-amino-3-oxopropyl)-N-(4-chlorophenyl)-3-phenylpiperidine-1-carboxamide
Homo sapiens
-
0.000001
3-([cis-4-[(tricyclo[3.3.1.13,7]dec-1-ylcarbamoyl)amino]cyclohexyl]oxy)benzoic acid
Homo sapiens
-
0.0000004
3-([[(adamantan-1-yl)methyl]carbamoyl]amino)adamantan-1-yl trifluoroacetate
Homo sapiens
pH 7.4, 37°C
0.000001
3-methyl-3-phenyl-N-(4-(pyridin-3-yl)benzyl)piperidine-1-carboxamide
Homo sapiens
-
0.000007
3-methyl-3-phenyl-N-[3-(pyridin-3-yl)propyl]piperidine-1-carboxamide
Homo sapiens
-
0.000001
3-methyl-3-phenyl-N-[3-[(1S,2S)-2-phenylcyclopropyl]benzyl]piperidine-1-carboxamide
Homo sapiens
-
0.000005
3-methyl-3-phenyl-N-[3-[2-(quinoxalin-6-yl)ethyl]benzyl]piperidine-1-carboxamide
Homo sapiens
-
0.000008
3-methyl-3-phenyl-N-[[2'-(trifluoromethyl)biphenyl-4-yl]methyl]piperidine-1-carboxamide
Homo sapiens
-
0.000019
3-[1-[(4-chlorophenyl)carbamoyl]-3-(pyridin-2-yl)piperidin-3-yl]propanoic acid
Homo sapiens
-
0.000028
3-[1-[(4-chlorophenyl)carbamoyl]-3-(pyridin-3-yl)piperidin-3-yl]propanoic acid
Homo sapiens
-
0.00003
3-[1-[(4-chlorophenyl)carbamoyl]-3-(pyridin-4-yl)piperidin-3-yl]propanoic acid
Homo sapiens
-
0.000005 - 0.000016
3-[1-[(4-chlorophenyl)carbamoyl]-3-phenylpiperidin-3-yl]propanoic acid
0.000012
3-[1-[(4-chlorophenyl)carbamoyl]-3-[3-(trifluoromethyl)phenyl]piperidin-3-yl]propanoic acid
Homo sapiens
-
0.000005
3-[1-[(4-chlorophenyl)carbamoyl]-3-[4-(trifluoromethyl)phenyl]piperidin-3-yl]propanoic acid
Homo sapiens
-
0.000008
3-[3-(biphenyl-4-yl)-1-[(4-chlorophenyl)carbamoyl]piperidin-3-yl]propanoic acid
Homo sapiens
-
0.009
3-[4-(N-((2-trifluoromethyl)benzyl)benzamide)]propionic acid
Homo sapiens
pH 7.0, 22°C
0.0001
3-[4-[(1-[[(1R,3S)-2,2-dimethyl-3-phenylcyclopropyl]carbamoyl]piperidin-4-yl)oxy]phenyl]propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0000191
3-[4-[(1-[[(1S,2R)-2-phenylcyclopropyl]carbamoyl]piperidin-4-yl)oxy]phenyl]propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.000012
3-[4-[(1-[[(1S,2R,3R)-2-methyl-3-phenylcyclopropyl]carbamoyl]piperidin-4-yl)oxy]phenyl]propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0000021
3-[4-[(1-[[(1s,2R,3S)-2,3-bis(4-fluorophenyl)cyclopropyl]carbamoyl]piperidin-4-yl)oxy]phenyl]propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0000023
3-[4-[(1-[[(1s,2R,3S)-2,3-diphenylcyclopropyl]carbamoyl]piperidin-4-yl)oxy]phenyl]propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0000757
3-[4-[(1-[[(1S,2S,3R)-2-methyl-3-phenylcyclopropyl]carbamoyl]piperidin-4-yl)oxy]phenyl]propanoic acid
Homo sapiens
pH and temperature not specified in the publication
0.000008
4'-hydroxy-N-(2-phenylcyclopropyl)-3',4'-dihydro-1H-spiro[piperidine-4,2'-pyrano[3,2-b]pyridine]-1-carboxamide
Homo sapiens
-
0.001
4'-[([2-(trifluoromethyl)phenyl]methyl)carbamoyl][1,1'-biphenyl]-3-carboxylic acid
Homo sapiens
pH 7.0, 22°C
0.00017
4'-[([2-(trifluoromethyl)phenyl]methyl)carbamoyl][1,1'-biphenyl]-4-carboxylic acid
Homo sapiens
pH 7.0, 22°C
0.000002
4-((4-(3-(adamantan-1-yl)ureido)trans-cyclohexyl)oxy)benzoic acid
Homo sapiens
pH 7.4, 37°C
0.000054
4-(1,2,4-oxadiazol-3-yl)-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
Homo sapiens
-
0.000235
4-(1,3,4-oxadiazol-2-yl)-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
Homo sapiens
-
0.0000075
4-(1,3-benzoxazol-2-yl)-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
Homo sapiens
-
0.00012
4-(1-methyl-1H-1,2,3-triazol-4-yl)-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
Homo sapiens
-
0.00043
4-(2,3-dihydro-1H-1,2,3-triazol-1-yl)-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
Homo sapiens
-
0.0011
4-(3-hydroxy-4-methyl-1,2-oxazol-5-yl)-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
Homo sapiens
-
0.000028
4-(3-methyl-1,2,4-oxadiazol-5-yl)-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
Homo sapiens
-
0.0084
4-(4-methyl-4H-1,2,4-triazol-3-yl)-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
Homo sapiens
-
0.0000041
4-(5-phenyl-3-[3-[3-(3-trifluoromethyl-phenyl)-ureido]-propyl]-pyrazol-1-yl)-benzenesulfonamide
Homo sapiens
pH 7.0, 30°C
0.0000005
4-(5-phenyl-3-[3-[3-(4-trifluoromethoxy-phenyl)-ureido]-propyl]-pyrazol-1-yl)-benzenesulfonamide
Homo sapiens
pH 7.0, 30°C
0.0000009
4-(5-phenyl-3-[3-[3-(4-trifluoromethyl-phenyl)-ureido]-propyl]-pyrazol-1-yl)-benzenesulfonamide
Homo sapiens
pH 7.0, 30°C
0.000005
4-(5-[1-[(2-phenylcyclopropyl)carbamoyl]piperidin-4-yl]-1,2,4-oxadiazol-3-yl)benzoic acid
Homo sapiens
-
0.000008
4-(trifluoromethyl)-N-[4-(trifluoromethyl)phenyl]-1,2-benzoxazol-3-amine
Homo sapiens
-
0.000002
4-([trans-4-[(tricyclo[3.3.1.13,7]dec-1-ylcarbamoyl)amino]cyclohexyl]oxy)benzoic acid
Homo sapiens
-
0.061
4-benzyl-3,4-dihydroquinoxalin-2(1H)-one
Homo sapiens
in 25 mM Bis-Tris HCl, pH 7.0, and 0.02% (v/v) Triton X-100, at 22°C
0.1
4-hydroxy-3,5-dimethoxybenzaldehyde
Homo sapiens
above, pH not specified in the publication, 37°C
0.1
4-hydroxy-3-methoxybenzaldehyde
Homo sapiens
above, pH not specified in the publication, 37°C
0.000003
4-oxo-N-(1,2,3,4-tetrahydronaphthalen-2-yl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
Homo sapiens
-
0.000001
4-oxo-N-(2-phenylcyclopropyl)-6-(pyridin-4-yl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
Homo sapiens
-
0.000008
4-oxo-N-(3-phenylcyclopentyl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
Homo sapiens
-
0.00002
4-oxo-N-(6,7,8,9-tetrahydro-5H-benzo[7]annulen-7-yl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
Homo sapiens
-
0.000003
4-oxo-N-[(1S,2R)-2-phenylcyclopropyl]-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
Homo sapiens
-
0.0000005
4-[(4-[[(3-methyladamantan-1-yl)carbamoyl]amino]cyclohexyl)oxy]benzoic acid
Homo sapiens
pH 7.4, 37°C
0.000012
4-[1-[(4-chlorophenyl)carbamoyl]-3-phenylpiperidin-3-yl]butanoic acid
Homo sapiens
-
0.00001
4-[3-(isoquinolin-1-yl)-1,2,4-oxadiazol-5-yl]-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
Homo sapiens
-
0.000008
4-[3-(pyridin-2-yl)-1,2,4-oxadiazol-5-yl]-N-(1,2,3,4-tetrahydronaphthalen-2-yl)piperidine-1-carboxamide
Homo sapiens
-
0.000036
4-[3-(pyridin-2-yl)-1,2,4-oxadiazol-5-yl]-N-(6,7,8,9-tetrahydro-5H-benzo[7]annulen-7-yl)piperidine-1-carboxamide
Homo sapiens
-
0.000007
4-[3-(pyridin-2-yl)-1,2,4-oxadiazol-5-yl]-N-[4-(trifluoromethyl)phenyl]piperidine-1-carboxamide
Homo sapiens
-
0.000004
4-[3-[4-(methylsulfonyl)phenyl]-1,2,4-oxadiazol-5-yl]-N-(2-phenylcyclopropyl)piperidine-1-carboxamide
Homo sapiens
-
0.0000016
4-[[(1r,4r)-4-([[(adamantan-1-yl)methyl]carbamoyl]amino)cyclohexyl]oxy]benzoic acid
Homo sapiens
pH 7.4, 37°C
0.0000017
4-[[(1r,4r)-4-[[(3,5,7-trimethyladamantan-1-yl)carbamoyl]amino]cyclohexyl]oxy]benzoic acid
Homo sapiens
pH 7.4, 37°C
0.0000008
4-[[(1r,4r)-4-[[(3,5-dimethyladamantan-1-yl)carbamoyl]amino]cyclohexyl]oxy]benzoic acid
Homo sapiens
pH 7.4, 37°C
0.0000014
4-[[(1r,4r)-4-[[(3-chloroadamantan-1-yl)carbamoyl]amino]cyclohexyl]oxy]benzoic acid
Homo sapiens
pH 7.4, 37°C
0.0000018
4-[[(1r,4r)-4-[[(3-ethyladamantan-1-yl)carbamoyl]amino]cyclohexyl]oxy]benzoic acid
Homo sapiens
pH 7.4, 37°C
0.0000005
4-[[(1r,4r)-4-[[(3-methyladamantan-1-yl)carbamoyl]amino]cyclohexyl]oxy]benzoic acid
Homo sapiens
pH 7.4, 37°C
0.0000045
4-[[(2R,5R)-5-[[(2-oxoadamantan-1-yl)carbamoyl]amino]piperidin-2-yl]oxy]benzoic acid
Homo sapiens
pH 7.4, 37°C
0.000001
4-[[cis-4-([[4-(trifluoromethoxy)phenyl]carbamoyl]amino)cyclohexyl]oxy]benzoic acid
Homo sapiens
-
0.1
5,6,7-trihydroxy-2-phenyl-4H-1-benzopyran-4-one
Homo sapiens
above, pH not specified in the publication, 37°C
0.1
5,6,7-trihydroxy-8-methoxy-2-phenyl-4H-1-benzopyran-4-one
Homo sapiens
above, pH not specified in the publication, 37°C
0.03389
5,6-dihydroxy-4-oxo-2-phenyl-4H-1-benzopyran-7-yl D-threo-hexopyranosiduronic acid
Homo sapiens
pH not specified in the publication, 37°C
0.1
5,7,8-trihydroxy-2-phenyl-4H-1-benzopyran-4-one
Homo sapiens
above, pH not specified in the publication, 37°C
0.1
5,7-dihydroxy-2-(2-hydroxyphenyl)-4H-1-benzopyran-4-one
Homo sapiens
above, pH not specified in the publication, 37°C
0.1
5,7-dihydroxy-2-(2-hydroxyphenyl)-6-methoxy-4H-1-benzopyran-4-one
Homo sapiens
above, pH not specified in the publication, 37°C
0.0112
5,7-dihydroxy-2-(3,4,5-trihydroxyphenyl)-1-benzopyran-1-ium-3-yl beta-D-galactopyranoside
Homo sapiens
pH 7.0, 37°C
0.0253
5,7-dihydroxy-2-(3,4,5-trihydroxyphenyl)-1-benzopyran-1-ium-3-yl beta-D-glucopyranoside
Homo sapiens
pH 7.0, 37°C
0.1
5,7-dihydroxy-2-phenyl-4H-1-benzopyran-4-one
Homo sapiens
above, pH not specified in the publication, 37°C
0.04482
5,7-dihydroxy-6-methoxy-2-phenyl-4H-1-benzopyran-4-one
Homo sapiens
pH not specified in the publication, 37°C
0.1
5,7-dihydroxy-8-methoxy-2-phenyl-4H-1-benzopyran-4-one
Homo sapiens
above, pH not specified in the publication, 37°C
0.07
5-(4-bromobenzyl)-1,3-thiazol-2-amine
Homo sapiens
in 25 mM Bis-Tris HCl, pH 7.0, and 0.02% (v/v) Triton X-100, at 22°C
0.00004
5-(trifluoromethyl)-N-[4-(trifluoromethyl)phenyl]-1,2-benzoxazol-3-amine
Homo sapiens
-
0.1
5-hydroxy-2-(2-hydroxy-6-methoxyphenyl)-6,7,8-trimethoxy-4H-1-benzopyran-4-one
Homo sapiens
above, pH not specified in the publication, 37°C
0.1
5-hydroxy-2-(4-hydroxy-3-methoxyphenyl)-7-methoxy-4H-1-benzopyran-4-one
Homo sapiens
pH not specified in the publication, 37°C
0.0063
5-methyl-N-(2-phenylethyl)-4,5-dihydro-1,3-thiazol-2-amine
Homo sapiens
in 25 mM Bis-Tris HCl, pH 7.0, and 0.02% (v/v) Triton X-100, at 22°C
0.000005
5-[1-[(4-chlorophenyl)carbamoyl]-3-phenylpiperidin-3-yl]pentanoic acid
Homo sapiens
-
0.000008 - 0.000011
6'-(methylsulfonyl)-N-(2-phenylcyclopropyl)-1H,4'H-spiro[azepane-4,3'-chromene]-1-carboxamide
0.000004
6-(1-methyl-1H-pyrazol-5-yl)-4-oxo-N-(2-phenylcyclopropyl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
Homo sapiens
-
0.00007
6-(1H-indol-5-yl)-N-[4-(trifluoromethyl)phenyl]-1,2-benzoxazol-3-amine
Homo sapiens
-
0.000091
6-(2-fluorophenyl)-N-[5-(trifluoromethyl)pyridin-2-yl]-1,2-benzoxazol-3-amine
Homo sapiens
-
0.00007
6-(3-methylpyridin-2-yl)-N-[5-(trifluoromethyl)pyridin-2-yl]-1,2-benzoxazol-3-amine
Homo sapiens
-
0.000019
6-(isoquinolin-5-yl)-N-[4-(trifluoromethyl)phenyl]-1,2-benzoxazol-3-amine
Homo sapiens
-
0.000003 - 0.000011
6-(methylsulfonyl)-4-oxo-N-(2-phenylcyclopropyl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
0.000023
6-(pyridin-3-yl)-N-[5-(trifluoromethyl)pyridin-2-yl]-1,2-benzoxazol-3-amine
Homo sapiens
-
0.000058
6-(pyridin-4-yl)-N-[5-(trifluoromethyl)pyridin-2-yl]-1,2-benzoxazol-3-amine
Homo sapiens
-
0.049
6-(trifluoromethyl)-1,3-benzothiazol-2-amine
Homo sapiens
in 25 mM Bis-Tris HCl, pH 7.0, and 0.02% (v/v) Triton X-100, at 22°C
0.000018
6-(trifluoromethyl)-N-[4-(trifluoromethyl)phenyl]-1,2-benzoxazol-3-amine
Homo sapiens
-
0.029
6-amino-1-methyl-5-(piperidin-1-yl)pyrimidine-2,4(1H,3H)-dione
Homo sapiens
in 25 mM Bis-Tris HCl, pH 7.0, and 0.02% (v/v) Triton X-100, at 22°C
0.000003
6-fluoro-N-(2-phenylcyclopropyl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
Homo sapiens
-
0.000003
6-[(1-methyl-1H-pyrazol-5-yl)amino]-4-oxo-N-(2-phenylcyclopropyl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
Homo sapiens
-
0.00047
6-[3-(trifluoromethyl)phenyl]-N-[5-(trifluoromethyl)pyridin-2-yl]-1,2-benzoxazol-3-amine
Homo sapiens
-
0.000008
7-(1H-indol-5-yl)-N-[5-(trifluoromethyl)pyridin-2-yl]-1,2-benzoxazol-3-amine
Homo sapiens
-
0.000004
7-(trifluoromethyl)-N-[4-(trifluoromethyl)phenyl]-1,2-benzoxazol-3-amine
Homo sapiens
-
0.01
7-(trifluoromethyl)-N-[5-(trifluoromethyl)pyridin-2-yl]-1,2-benzoxazol-3-amine
Homo sapiens
above
0.000019
7-(trifluoromethyl)-N-[5-(trifluoromethyl)pyridin-2-yl][1,2]oxazolo[5,4-c]pyridin-3-amine
Homo sapiens
-
0.000074
7-(trifluoromethyl)-N-[6-(trifluoromethyl)pyridin-3-yl]-1,2-benzoxazol-3-amine
Homo sapiens
-
0.000004
7-[2-(trifluoromethyl)phenyl]-N-[5-(trifluoromethyl)pyridin-2-yl]-1,2-benzoxazol-3-amine
Homo sapiens
-
0.00001
7-[3-(trifluoromethyl)phenyl]-N-[5-(trifluoromethyl)pyridin-2-yl]-1,2-benzoxazol-3-amine
Homo sapiens
-
0.000001
butyl 12-[(tricyclo[3.3.1.13,7]dec-1-ylcarbamoyl)amino]dodecanoate
Homo sapiens
recombinant enzyme expressed in Escherichia coli or Sf9 cells
0.0000009
cis-1-adamantan-1-yl-3-(4-benzyloxycyclohexyl)urea
Homo sapiens
pH 7.4, 30°C
0.0000015
cis-1-adamantan-1-yl-3-[4-(2,6-dichlorobenzyloxy)cyclohexyl]-urea
Homo sapiens
pH 7.4, 30°C
0.0000011
cis-1-adamantan-1-yl-3-[4-(2,6-difluorobenzyloxy)cyclohexyl]-urea
Homo sapiens
pH 7.4, 30°C
0.0000013
cis-1-adamantan-1-yl-3-[4-(4-bromophenoxy)cyclohexyl]urea
Homo sapiens
pH 7.4, 30°C
0.000001
cis-1-adamantan-1-yl-3-[4-(4-fluorophenoxy)cyclohexyl]-urea
Homo sapiens
pH 7.4, 30°C
0.00000055
cis-1-adamantan-1-yl-3-[4-(4-methoxyphenoxy)cyclohexyl]-urea
Homo sapiens
pH 7.4, 30°C
0.00000072
cis-1-adamantan-1-yl-3-[4-(4-nitrophenoxy)cyclohexyl]urea
Homo sapiens
pH 7.4, 30°C
0.0000019
cis-3-[4-(3-adamantan-1-ylureido)cyclohexyloxy]benzoic acid
Homo sapiens
pH 7.4, 30°C
0.0000006
cis-4-(4-[3-(4-trifluoromethoxyphenyl)ureido]cyclohexyloxy)-benzoic acid
Homo sapiens
pH 7.4, 30°C
0.00004
ethyl (E)-3-[N-((2-trifluoromethyl)benzyl)benzamide]-alpha-ethylcinnamate
Homo sapiens
pH 7.0, 22°C
0.0004
ethyl (E)-3-[N-((2-trifluoromethyl)benzyl)benzamide]-alpha-ethylcinnamic acid
Homo sapiens
pH 7.0, 22°C
0.000063
ethyl (E)-4-[N-((2-(trifluoromethyl)-benzyl)benzamide]-alpha-ethylcinnamate
Homo sapiens
pH 7.0, 22°C
0.000027
ethyl 2-ethyl 3-[3-(N-((2-trifluoromethyl)benzyl)benzamide)]-propanoate
Homo sapiens
pH 7.0, 22°C
0.000044
ethyl 2-ethyl 3-[4-(N-((2-trifluoromethyl)benzyl)benzamide)]propanoate
Homo sapiens
pH 7.0, 22°C
0.0017
ethyl 2-ethyl 3-[4-(N-((4-chloro)benzyl)benzamide)]-propanoate
Homo sapiens
pH 7.0, 22°C
0.0022
ethyl 2-ethyl 3-[4-(N-((4-fluoro)benzyl)benzamide)]-propanoate
Homo sapiens
pH 7.0, 22°C
0.00062
ethyl 2-ethyl 3-[4-(N-((4-methoxy)benzyl)benzamide)]-propanoate
Homo sapiens
pH 7.0, 22°C
0.0009
ethyl 2-ethyl 3-[4-(N-((4-trifluoromethoxy)benzyl)-benzamide)]propanoate
Homo sapiens
pH 7.0, 22°C
0.00057
ethyl 2-ethyl 3-[4-(N-((4-trifluoromethyl)benzyl)benzamide)]-propanoate
Homo sapiens
pH 7.0, 22°C
0.00012
ethyl 2-ethyl 3-[4-(N-(4-fluoro(2-trifluoromethyl)benzyl)-benzamide)]propanoate
Homo sapiens
pH 7.0, 22°C
0.00003
ethyl 2-ethyl 3-[4-(N-(4-methoxy(2-trifluoromethyl)benzyl)-benzamide)]propanoate
Homo sapiens
pH 7.0, 22°C
0.004
ethyl 2-ethyl-3-[4-(N-((2-bromo)benzyl)benzamide)]-propanoate
Homo sapiens
pH 7.0, 22°C
0.0038
ethyl 2-ethyl-3-[4-(N-((2-chloro)benzyl)benzamide)]-propanoate
Homo sapiens
pH 7.0, 22°C
0.0009
ethyl 2-ethyl-3-[4-(N-((2-methyl)benzyl)benzamide)]-propanoate
Homo sapiens
pH 7.0, 22°C
0.00003
ethyl 2-ethyl-3-[4-(N-((2-trifluoromethoxy)benzyl)-benzamide)]prop
Homo sapiens
pH 7.0, 22°C
0.00025
ethyl 2-methyl 3-[4-(N-((2-trifluoromethyl)benzyl)benzamide)]-propanoate
Homo sapiens
pH 7.0, 22°C
0.00012
ethyl 2-phenyl 3-[4-(N-((2-trifluoromethyl)benzyl)benzamide)]-propanoate
Homo sapiens
pH 7.0, 22°C
0.00017
ethyl 2-propyl 3-[4-(N-((2-trifluoromethyl)benzyl)benzamide)]-propanoate
Homo sapiens
pH 7.0, 22°C
0.00011
ethyl 3-[4-(N-((2-trifluoromethyl)benzyl)benzamide)]-propanoate
Homo sapiens
pH 7.0, 22°C
0.0000017
methyl 2-([4-[(tricyclo[3.3.1.13,7]dec-2-ylcarbamoyl)amino]piperidin-1-yl]carbonyl)benzoate
Homo sapiens
-
0.000003
methyl 2-hydroxy-4-[(tricyclo[3.3.1.13,7]dec-1-ylcarbamoyl)amino]benzoate
Homo sapiens
-
0.0000018
methyl 2-[(4-[[(tricyclo[3.3.1.13,7]dec-2-ylcarbamoyl)amino]methyl]piperidin-1-yl)carbonyl]benzoate
Homo sapiens
-
0.0000011
methyl 3-([4-[(tricyclo[3.3.1.13,7]dec-2-ylcarbamoyl)amino]piperidin-1-yl]carbonyl)benzoate
Homo sapiens
-
0.0000041
methyl 3-[(4-[[(tricyclo[3.3.1.13,7]dec-2-ylcarbamoyl)amino]methyl]piperidin-1-yl)carbonyl]benzoate
Homo sapiens
-
0.000001
methyl 3-[1-[(4-chlorophenyl)carbamoyl]-3-phenylpiperidin-3-yl]propanoate
Homo sapiens
below
0.0000011
methyl 4-([4-[(tricyclo[3.3.1.13,7]dec-2-ylcarbamoyl)amino]piperidin-1-yl]carbonyl)benzoate
Homo sapiens
-
0.0000015
methyl 4-[(4-[[(tricyclo[3.3.1.13,7]dec-2-ylcarbamoyl)amino]methyl]piperidin-1-yl)carbonyl]benzoate
Homo sapiens
-
0.0000091
methyl 4-[[(tricyclo[3.3.1.13,7]dec-1-ylcarbonyl)amino]methyl]benzoate
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.0000034
methyl 5-oxo-5-(4-[[(tricyclo[3.3.1.13,7]dec-2-ylcarbamoyl)amino]methyl]piperidin-1-yl)pentanoate
Homo sapiens
-
0.0000027
methyl 5-oxo-5-[4-[(tricyclo[3.3.1.13,7]dec-2-ylcarbamoyl)amino]piperidin-1-yl]pentanoate
Homo sapiens
-
0.0168
N,N'-(butane-1,4-diyl)bis[4-(adamantan-2-yl)piperazine-1-carboxamide]
Homo sapiens
pH 7.4, 37°C
0.0004086
N,N'-1,2-phenylenebis[N'-(3-chloroadamantan-1-yl)urea]
Homo sapiens
pH 7.4, 37°C
0.001364
N,N'-1,2-phenylenebis[N'-[(adamantan-1-yl)methyl]urea]
Homo sapiens
pH 7.4, 37°C
0.000779
N,N'-1,4-phenylenebis[N'-[(adamantan-1-yl)methyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000234
N,N'-butane-1,4-diylbis[N'-(3,5-dimethyladamantan-1-yl)urea]
Homo sapiens
pH 7.4, 37°C
0.0000013
N,N'-butane-1,4-diylbis[N'-(3-chloroadamantan-1-yl)urea]
Homo sapiens
pH 7.4, 37°C
0.0000011
N,N'-butane-1,4-diylbis[N'-(3-ethyladamantan-1-yl)urea]
Homo sapiens
pH 7.4, 37°C
0.0000007
N,N'-butane-1,4-diylbis[N'-[(3,5-dimethyladamantan-1-yl)methyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000009
N,N'-butane-1,4-diylbis[N'-[(adamantan-1-yl)methyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000019
N,N'-butane-1,4-diylbis[N'-[1-(adamantan-1-yl)-2-methylpropan-2-yl]urea]
Homo sapiens
pH 7.4, 37°C
0.000605
N,N'-butane-1,4-diylbis[N'-[2-(adamantan-1-yl)-2-phenylethyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000034
N,N'-butane-1,4-diylbis[N'-[2-(adamantan-1-yl)ethyl]urea]
Homo sapiens
pH 7.4, 37°C
0.003299
N,N'-butane-1,4-diylbis[N'-[2-(adamantan-1-yl)pentyl]urea]
Homo sapiens
pH 7.4, 37°C
0.001792
N,N'-butane-1,4-diylbis[N'-[4-(adamantan-1-yl)phenyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000009
N,N'-decane-1,10-diylbis[N'-(3-chloroadamantan-1-yl)urea]
Homo sapiens
pH 7.4, 37°C
0.0001445
N,N'-ethane-1,2-diylbis[N'-(3-chloroadamantan-1-yl)urea]
Homo sapiens
pH 7.4, 37°C
0.0001792
N,N'-ethane-1,2-diylbis[N'-[(adamantan-1-yl)methyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000014
N,N'-heptane-1,7-diylbis[N'-(3-chloroadamantan-1-yl)urea]
Homo sapiens
pH 7.4, 37°C
0.0000004
N,N'-heptane-1,7-diylbis[N'-[(adamantan-1-yl)methyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000094
N,N'-hexane-1,6-diylbis(N'-[3-[(adamantan-1-yl)oxy]propyl]urea)
Homo sapiens
pH 7.4, 37°C
0.0000016
N,N'-hexane-1,6-diylbis[N'-(3-chloroadamantan-1-yl)urea]
Homo sapiens
pH 7.4, 37°C
0.0000085
N,N'-hexane-1,6-diylbis[N'-(3-ethyladamantan-1-yl)urea]
Homo sapiens
pH 7.4, 37°C
0.000001
N,N'-hexane-1,6-diylbis[N'-[(3,5-dimethyladamantan-1-yl)methyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000005
N,N'-hexane-1,6-diylbis[N'-[1-(adamantan-1-yl)ethyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000043
N,N'-hexane-1,6-diylbis[N'-[2-(adamantan-1-yl)-2-methylpropyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000915
N,N'-hexane-1,6-diylbis[N'-[2-(adamantan-1-yl)-2-phenylethyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000028
N,N'-hexane-1,6-diylbis[N'-[2-(adamantan-1-yl)butyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000008
N,N'-hexane-1,6-diylbis[N'-[2-(adamantan-1-yl)ethyl]urea]
Homo sapiens
pH 7.4, 37°C
0.035
N,N'-hexane-1,6-diylbis[N'-[2-(adamantan-1-yl)pentyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0005293
N,N'-hexane-1,6-diylbis[N'-[4-(adamantan-1-yl)phenyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000027
N,N'-octane-1,8-diylbis(N'-[3-[(adamantan-1-yl)oxy]propyl]urea)
Homo sapiens
pH 7.4, 37°C
0.0000037
N,N'-octane-1,8-diylbis[N'-(3,5-dimethyladamantan-1-yl)urea]
Homo sapiens
pH 7.4, 37°C
0.0000012
N,N'-octane-1,8-diylbis[N'-(3-chloroadamantan-1-yl)urea]
Homo sapiens
pH 7.4, 37°C
0.0000025
N,N'-octane-1,8-diylbis[N'-[(3,5-dimethyladamantan-1-yl)methyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000067
N,N'-octane-1,8-diylbis[N'-[2-(adamantan-1-yl)-2-methylpropyl]urea]
Homo sapiens
pH 7.4, 37°C
0.000205
N,N'-octane-1,8-diylbis[N'-[2-(adamantan-1-yl)-2-phenylethyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000015
N,N'-octane-1,8-diylbis[N'-[2-(adamantan-1-yl)ethyl]urea]
Homo sapiens
pH 7.4, 37°C
0.1
N,N'-octane-1,8-diylbis[N'-[2-(adamantan-1-yl)pentyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0002591
N,N'-octane-1,8-diylbis[N'-[4-(adamantan-1-yl)phenyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000018
N,N'-pentane-1,5-diylbis[N'-(3-chloroadamantan-1-yl)urea]
Homo sapiens
pH 7.4, 37°C
0.0000012
N,N'-pentane-1,5-diylbis[N'-(3-ethyladamantan-1-yl)urea]
Homo sapiens
pH 7.4, 37°C
0.0000009
N,N'-pentane-1,5-diylbis[N'-[(adamantan-1-yl)methyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000017
N,N'-propane-1,3-diylbis[N'-(3-chloroadamantan-1-yl)urea]
Homo sapiens
pH 7.4, 37°C
0.0000017
N,N'-propane-1,3-diylbis[N'-(3-ethyladamantan-1-yl)urea]
Homo sapiens
pH 7.4, 37°C
0.0000009
N,N'-propane-1,3-diylbis[N'-[(adamantan-1-yl)methyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000012
N,N'-undecane-1,11-diylbis[N'-[(adamantan-1-yl)methyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000019
N,N'-[1,4-phenylenebis(methylene)]bis[N'-(3,5-dimethyladamantan-1-yl)urea]
Homo sapiens
pH 7.4, 37°C
0.000059
N-(1,2-benzoxazol-3-yl)-3-methyl-3-phenylpiperidine-1-carboxamide
Homo sapiens
-
0.000274
N-(1-acetylpiperidin-4-yl)-2-(tricyclo[3.3.1.13,7]dec-1-yl)acetamide
Homo sapiens
-
0.58
N-(1-tert-butoxyethenyl)-1,2,3,4-tetrahydroquinolin-3-amine
Homo sapiens
37°C, pH 7.0
0.000005
N-(2,3-dihydro-1H-inden-1-yl)-4-oxo-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
Homo sapiens
-
0.00013
N-(2,3-dihydro-1H-inden-1-yl)-4-[3-(pyridin-2-yl)-1,2,4-oxadiazol-5-yl]piperidine-1-carboxamide
Homo sapiens
-
0.000016
N-(2,4-dichlorobenzyl)-1-(2-ethoxyethyl)-6-oxo-1,6-dihydropyridine-3-carboxamide
Homo sapiens
-
0.000001
N-(2,4-dichlorobenzyl)-3-methyl-3-phenylpiperidine-1-carboxamide
Homo sapiens
below
0.0000066
N-(2,4-dichlorobenzyl)-6-(2,2,2-trifluoroethoxy)pyridine-3-carboxamide
Homo sapiens
-
0.0015
N-(2,4-dichlorobenzyl)-6-[2-(pyrrolidin-1-yl)ethyl]pyridine-3-carboxamide
Homo sapiens
-
0.000014
N-(2-chloro-4-cyanobenzyl)-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
Homo sapiens
-
0.000021
N-(2-chlorobenzyl)-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
Homo sapiens
-
0.0000004
N-(2-oxoadamantan-1-yl)-N'-1,3,5-triazatricyclo[3.3.1.13,7]decan-7-ylurea
Homo sapiens
pH 7.4, 37°C
0.000005
N-(2-phenylcyclopropyl)-3',4'-dihydro-1H-spiro[piperidine-4,2'-pyrano[3,2-b]pyridine]-1-carboxamide
Homo sapiens
-
0.000004
N-(2-phenylcyclopropyl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
Homo sapiens
-
0.0011
N-(2-phenylcyclopropyl)-4-(1H-1,2,4-triazol-1-yl)piperidine-1-carboxamide
Homo sapiens
-
0.00048
N-(2-phenylcyclopropyl)-4-(1H-pyrazol-1-yl)piperidine-1-carboxamide
Homo sapiens
-
0.000013
N-(2-phenylcyclopropyl)-4-[3-(pyrazin-2-yl)-1,2,4-oxadiazol-5-yl]piperidine-1-carboxamide
Homo sapiens
-
0.000009
N-(2-phenylcyclopropyl)-4-[3-(pyridin-2-yl)-1,2,4-oxadiazol-5-yl]piperidine-1-carboxamide
Homo sapiens
-
0.000007
N-(2-phenylcyclopropyl)-4-[3-(pyridin-3-yl)-1,2,4-oxadiazol-5-yl]piperidine-1-carboxamide
Homo sapiens
-
0.000014
N-(2-phenylcyclopropyl)-4-[3-(pyridin-4-yl)-1,2,4-oxadiazol-5-yl]piperidine-1-carboxamide
Homo sapiens
-
0.000033
N-(2-phenylcyclopropyl)-4-[3-(pyrimidin-2-yl)-1,2,4-oxadiazol-5-yl]piperidine-1-carboxamide
Homo sapiens
-
0.000007
N-(2-phenylcyclopropyl)-4-[3-(quinolin-2-yl)-1,2,4-oxadiazol-5-yl]piperidine-1-carboxamide
Homo sapiens
-
0.000009
N-(2-phenylcyclopropyl)-4-[3-[2-(trifluoromethyl)phenyl]-1,2,4-oxadiazol-5-yl]piperidine-1-carboxamide
Homo sapiens
-
0.0000026
N-(3,3-diphenylpropyl)-1-(2-ethoxyethyl)-6-oxo-1,6-dihydropyridine-3-carboxamide
Homo sapiens
-
0.0000054
N-(3,3-diphenylpropyl)-6-(2,2,2-trifluoroethoxy)pyridine-3-carboxamide
Homo sapiens
-
0.0000081
N-(3,3-diphenylpropyl)-6-oxo-1,6-dihydropyridine-3-carboxamide
Homo sapiens
-
0.000018
N-(3,3-diphenylpropyl)-6-[2-(pyrrolidin-1-yl)ethyl]pyridine-3-carboxamide
Homo sapiens
-
0.0000065
N-(3,5,7-trimethyladamantan-1-yl)-4-([[(3,5,7-trimethyladamantan-1-yl)carbamoyl]amino]methyl)piperidine-1-carboxamide
Homo sapiens
pH 7.4, 37°C
0.0000033
N-(3,5-dimethyladamantan-1-yl)-N'-(1-propanoylpiperidin-4-yl)urea
Homo sapiens
pH 7.4, 37°C
0.00016
N-(3,5-dimethyladamantan-1-yl)-N'-(3,5,7-trimethyladamantan-1-yl)urea
Homo sapiens
pH 7.4, 37°C
0.002894
N-(3,5-dimethyladamantan-1-yl)-N'-1,3,5-triazatricyclo[3.3.1.13,7]decan-7-ylurea
Homo sapiens
pH 7.4, 37°C
0.0000015
N-(3,5-dimethyladamantan-1-yl)-N'-[(3-ethyladamantan-1-yl)methyl]urea
Homo sapiens
pH 7.4, 37°C
0.002475
N-(3,5-dimethyladamantan-1-yl)-N'-[4-([[(3,5-dimethyladamantan-1-yl)carbamoyl]amino]methyl)phenyl]urea
Homo sapiens
pH 7.4, 37°C
0.0000399
N-(3-hydroxytricyclo[3.3.1.13,7]dec-1-yl)-2-(tricyclo[3.3.1.13,7]dec-1-yl)acetamide
Homo sapiens
-
0.000204
N-(4-(N1-methyl-N2-methyl-N2-(methyloxy)oxalamido)-benzyl)adamantanecarboxamide
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.001
N-(4-(N2-(tetrahydro-2H-pyran-2-yloxy)oxalamido)benzyl)adamantanecarboxamide
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.00019
N-(4-(N2-methyl-N2-(methyloxy)oxalamido)benzyl)adamantanecarboxamide
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.00018
N-(4-(N2-methyloxyoxalamido)benzyl)adamantanecarboxamide
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.000408
N-(4-(N2-tert-butyloxyoxalamido)benzyl)adamantanecarboxamide
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.000012
N-(4-bromo-2-cyanobenzyl)-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
Homo sapiens
-
0.000077
N-(4-chlorobenzyl)-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
Homo sapiens
-
0.000003
N-(4-chlorophenyl)-3-(2-cyanoethyl)-3-phenylpiperidine-1-carboxamide
Homo sapiens
-
0.000001
N-(4-chlorophenyl)-3-(2-hydroxyethyl)-3-phenylpiperidine-1-carboxamide
Homo sapiens
-
0.0000013
N-(4-chlorophenyl)-3-(3-hydroxypropyl)-3-phenylpiperidine-1-carboxamide
Homo sapiens
-
0.000005
N-(4-chlorophenyl)-3-phenyl-3-[2-(1H-tetrazol-5-yl)ethyl]piperidine-1-carboxamide
Homo sapiens
-
0.000012
N-(4-chlorophenyl)-3-[2-(dimethylamino)ethyl]-3-phenylpiperidine-1-carboxamide
Homo sapiens
-
0.0000014
N-(4-chlorophenyl)-3-[2-oxo-2-(1H-tetrazol-5-ylamino)ethyl]-3-phenylpiperidine-1-carboxamide
Homo sapiens
-
0.000003
N-(4-chlorophenyl)-3-[3-(diethylamino)-3-oxopropyl]-3-phenylpiperidine-1-carboxamide
Homo sapiens
-
0.000005
N-(4-chlorophenyl)-3-[3-(methylamino)-3-oxopropyl]-3-phenylpiperidine-1-carboxamide
Homo sapiens
-
0.000008
N-(4-chlorophenyl)-3-[3-(morpholin-4-yl)-3-oxopropyl]-3-phenylpiperidine-1-carboxamide
Homo sapiens
-
0.000029
N-(4-chlorophenyl)-3-[3-oxo-3-(1H-tetrazol-5-ylamino)propyl]-3-phenylpiperidine-1-carboxamide
Homo sapiens
-
0.0000072
N-(4-[[(adamantan-1-yl)carbamoyl]amino]butyl)-N'-(3,5-dimethyladamantan-1-yl)urea
Homo sapiens
pH and temperature not specified in the publication
0.000032
N-(5-chloro-1,3-benzoxazol-2-yl)-2-cyclopentylacetamide
Homo sapiens
pH 7.4, 22°C
0.0000003
N-(6-[[(adamantan-1-yl)carbamoyl]amino]hexyl)-N'-(3,5-dimethyladamantan-1-yl)urea
Homo sapiens
pH and temperature not specified in the publication
0.000997
N-(8-[[(adamantan-1-yl)carbamoyl]amino]octyl)-N'-(3,5-dimethyladamantan-1-yl)urea
Homo sapiens
pH and temperature not specified in the publication
0.01
N-(benzyloxy)-2-(adamant-2-ylamino)acetamide
Homo sapiens
IC50 above 0.01 mM, in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.0000012
N-([1-(phenylcarbonyl)piperidin-4-yl]methyl)-N'-(adamant-1-yl) urea
Homo sapiens
-
0.0000032
N-([1-(trifluoroacetyl)piperidin-4-yl]methyl)-N'-(adamant-1-yl) urea
Homo sapiens
-
0.0000061
N-adamantan-1-yl-N'-(3,5,7-trimethyladamantan-1-yl)urea
Homo sapiens
pH 7.4, 37°C
0.0000096
N-adamantan-1-yl-N'-(3,5-dimethyladamantan-1-yl)urea
Homo sapiens
pH 7.4, 37°C
0.000014
N-adamantan-1-yl-N'-[5-[2-(2-ethoxyethoxy)ethoxy]pentyl]urea
Homo sapiens
pH 7.4, 37°C
0.000015
N-adamantan-1-yl-N'-[5-[2-(2-hydroxyethoxy)ethoxy]pentyl]urea
Homo sapiens
pH 7.4, 37°C
0.001
N-benzyltricyclo[3.3.1.13,7]decane-1-carboxamide
Homo sapiens
IC50 above 0.001 mM, in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.00014
N-cyclohexyl-N'-(4-iodophenyl)urea
Homo sapiens
recombinant enzyme, pH 7.0, 22°C
0.00008
N-methoxy-N-methyl 3-[4-(N-((2-trifluoromethyl)benzyl)-benzamide)]cyclopropanecarboxamide
Homo sapiens
pH 7.0, 22°C
0.8
N-[(1-methyl-1H-pyrazol-3-yl)methyl]-2-phenylethan-1-amine
Homo sapiens
37°C, pH 7.0
0.0000144
N-[(1s,2R,3S)-2,3-diphenylcyclopropyl]-4-methylpiperazine-1-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0000018
N-[(1s,2R,3S)-2,3-diphenylcyclopropyl]piperidine-1-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000014
N-[(3'-chlorobiphenyl-4-yl)methyl]-3-methyl-3-phenylpiperidine-1-carboxamide
Homo sapiens
-
0.0000028
N-[(3,5-dimethyladamantan-1-yl)methyl]-N'-(3,5,7-trimethyladamantan-1-yl)urea
Homo sapiens
pH 7.4, 37°C
0.0000018
N-[(3-ethyladamantan-1-yl)methyl]-N'-(1-propanoylpiperidin-4-yl)urea
Homo sapiens
pH 7.4, 37°C
0.0000606
N-[(3-ethyladamantan-1-yl)methyl]-N'-1,3,5-triazatricyclo[3.3.1.13,7]decan-7-ylurea
Homo sapiens
pH 7.4, 37°C
0.0000172
N-[(adamantan-1-yl)methyl]-2-[3-(adamantan-1-yl)propyl]hydrazine-1-carboxamide
Homo sapiens
pH 7.4, 37°C
0.0000397
N-[(adamantan-1-yl)methyl]-4-[([[(adamantan-1-yl)methyl]carbamoyl]amino)methyl]piperidine-1-carboxamide
Homo sapiens
pH 7.4, 37°C
0.0000008
N-[(adamantan-1-yl)methyl]-N'-(1-propanoylpiperidin-4-yl)urea
Homo sapiens
pH 7.4, 37°C
0.001992
N-[(adamantan-1-yl)methyl]-N'-[2-(adamantan-1-yl)pentyl]urea
Homo sapiens
pH 7.4, 37°C
0.0000122
N-[(adamantan-1-yl)methyl]-N'-[4-(adamantan-1-yl)phenyl]urea
Homo sapiens
pH 7.4, 37°C
0.0000254
N-[1-(adamantan-1-yl)ethyl]-N'-(3,5,7-trimethyladamantan-1-yl)urea
Homo sapiens
pH 7.4, 37°C
0.0000128
N-[1-(adamantan-1-yl)ethyl]-N'-[(3-ethyladamantan-1-yl)methyl]urea
Homo sapiens
pH 7.4, 37°C
0.0000018
N-[1-(pyridin-2-ylcarbonyl)piperidin-4-yl]-N'-(adamant-1-yl) urea
Homo sapiens
-
0.0000229
N-[2-(adamantan-1-yl)butyl]-N'-(3,5,7-trimethyladamantan-1-yl)urea
Homo sapiens
pH 7.4, 37°C
0.0000138
N-[2-(adamantan-1-yl)butyl]-N'-(3,5-dimethyladamantan-1-yl)urea
Homo sapiens
pH 7.4, 37°C
0.0000044
N-[2-(adamantan-1-yl)ethyl]-N'-[(adamantan-1-yl)methyl]urea
Homo sapiens
pH 7.4, 37°C
0.0000031
N-[2-(adamantan-1-yl)pentyl]-N'-(3-chloroadamantan-1-yl)urea
Homo sapiens
pH 7.4, 37°C
0.00027
N-[2-(methylsulfonyl)benzyl]-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
Homo sapiens
-
0.171
N-[2-(morpholin-4-yl)phenyl]thiophene-3-carboxamide
Homo sapiens
in 25 mM Bis-Tris HCl, pH 7.0, and 0.02% (v/v) Triton X-100, at 22°C
0.0000046
N-[2-(trifluoromethoxy)benzyl]-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
Homo sapiens
-
0.000021
N-[2-chloro-4-(1H-tetrazol-5-yl)benzyl]-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
Homo sapiens
-
0.000014
N-[2-chloro-4-(methylsulfamoyl)benzyl]-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
Homo sapiens
-
0.000015
N-[2-chloro-4-(methylsulfonyl)benzyl]-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
Homo sapiens
-
0.000005
N-[3,3-bis-(4-fluorophenyl)-propyl]-2-(2,2,2-trifluoro-ethoxy)-isonicotinamide
Homo sapiens
-
0.000005
N-[3,3-bis-(4-fluorophenyl)-propyl]-4-methanesulfonyl-benzamide
Homo sapiens
-
0.000005
N-[3,3-bis-(4-fluorophenyl)-propyl]-6-(2,2,2-trifluoro-ethoxy)-nicotinamide
Homo sapiens
-
0.000007
N-[3-(4-fluorophenyl)-3-(4-methanesulfonyl-phenyl)-propyl]-4-methanesulfonyl-benzamide
Homo sapiens
-
0.000004
N-[3-(4-fluorophenyl)-3-(4-methanesulfonyl-phenyl)-propyl]-6-(2,2,2-trifluoro-ethoxy)-nicotinamide
Homo sapiens
-
0.000008
N-[3-(4-fluorophenyl)-3-(4-methanesulfonyl-phenyl)-propyl]-nicotinamide
Homo sapiens
-
0.00034
N-[3-[(2',4'-difluorobiphenyl-4-yl)methoxy]phenyl]piperidine-4-carboxamide
Homo sapiens
-
0.000001
N-[3-[2-(4-chlorophenyl)ethyl]benzyl]-3-methyl-3-phenylpiperidine-1-carboxamide
Homo sapiens
-
0.000007
N-[4-(1H-indol-5-yl)benzyl]-3-methyl-3-phenylpiperidine-1-carboxamide
Homo sapiens
-
0.00011
N-[4-(methylsulfonyl)benzyl]-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
Homo sapiens
-
0.000027
N-[4-(trifluoromethyl)phenyl][1,2]oxazolo[5,4-b]pyridin-3-amine
Homo sapiens
-
0.000031
N-[4-(trifluoromethyl)phenyl][1,2]oxazolo[5,4-c]pyridin-3-amine
Homo sapiens
-
0.0000263
N-[4-([[(adamantan-1-yl)methyl]carbamoyl]amino)butyl]-N'-[(3,5-dimethyladamantan-1-yl)methyl]urea
Homo sapiens
pH and temperature not specified in the publication
0.00078
N-[4-([[(adamantan-1-yl)methyl]carbamoyl]amino)phenyl]-N'-[(3,5-dimethyladamantan-1-yl)methyl]urea
Homo sapiens
pH and temperature not specified in the publication
0.000066
N-[4-chloro-2-(methylsulfonyl)benzyl]-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
Homo sapiens
-
0.0000004
N-[6-([[(adamantan-1-yl)methyl]carbamoyl]amino)hexyl]-N'-[(3,5-dimethyladamantan-1-yl)methyl]urea
Homo sapiens
pH and temperature not specified in the publication
0.0000073
N-[8-([[(adamantan-1-yl)methyl]carbamoyl]amino)octyl]-N'-[(3,5-dimethyladamantan-1-yl)methyl]urea
Homo sapiens
pH and temperature not specified in the publication
0.000012
N-[[4'-(methylsulfonyl)biphenyl-4-yl]methyl]-6-(3,3,3-trifluoropropoxy)pyridine-3-carboxamide
Homo sapiens
-
0.002006
N1,N4-bis[(adamantan-1-yl)methyl]piperazine-1,4-dicarboxamide
Homo sapiens
pH 7.4, 37°C
0.0000079
N1-(4-((2-adamantylacetamido)methyl)phenyl)-N1-methyl-N2-methyl-N2-methyloxyoxalamide
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.000069
N1-(4-((2-adamantylacetamido)methyl)phenyl)-N2-methyl-N2-methyloxyoxalamide
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.0000044
N1-(4-(2-adamantylacetamido)phenyl)-N1-methyl-N2-methyl-N2-(methyloxy)oxalamide
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.000035
N1-(4-(2-adamantylacetamido)phenyl)-N2-methyl-N2-(methyloxy)oxalamide
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.01
N1-(adamant-1-yl)-N2-(benzyloxy)oxalamide
Homo sapiens
IC50 above 0.01 mM, in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.000838
N1-(adamant-1-ylmethyl)-N2-(benzyloxy)oxalamide
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.0044
N1-(adamant-2-yl)-N2-(2-phenylethyloxy)oxalamide
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.00055
N1-(adamant-2-yl)-N2-(3-phenylpropyloxy)oxalamide
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.0023
N1-(adamant-2-yl)-N2-(4-chlorobenzyloxy)oxalamide
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.0015
N1-(adamant-2-yl)-N2-(4-methoxycarbonylbenzyloxy)oxalamide
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.01
N1-(adamant-2-yl)-N2-(4-nitrobenzyloxy)oxalamide
Homo sapiens
IC50 above 0.01 mM, in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.0032
N1-(adamant-2-yl)-N2-(benzyloxy)-N2-methyloxalamide
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.00005
N1-(adamant-2-yl)-N2-(benzyloxy)oxalamide
Homo sapiens
in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.01
N1-(adamant-2-yl)-N2-(phenyloxy)oxalamide
Homo sapiens
IC50 above 0.01 mM, in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.01
N1-(adamant-2-yl)-N2-(tetrahydro-2H-pyran-2-yloxy)oxalamide
Homo sapiens
IC50 above 0.01 mM, in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.01
N1-(adamant-2-yl)-N2-methyl-N2-(methyloxy)oxalamide
Homo sapiens
IC50 above 0.01 mM, in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.01
N1-(benzyloxy)-N2-(3-phenylpropyl)oxalamide
Homo sapiens
IC50 above 0.01 mM, in 25 mM Bis-Tris/HCl, pH 7.0, at 30°C
0.0000069
t-butyl 4-[2-[(5-chloro-1,3-benzoxazol-2-yl)amino]-2-oxoethyl]piperidine-1-carboxylate
Homo sapiens
pH 7.4, 22°C
0.0000017
trans-1-adamantan-1-yl-3-(4-benzyloxycyclohexyl)urea
Homo sapiens
pH 7.4, 30°C
0.0000017
trans-1-adamantan-1-yl-3-[4-(2,6-dichlorobenzyloxy)cyclohexyl]-urea
Homo sapiens
pH 7.4, 30°C
0.0000017
trans-1-adamantan-1-yl-3-[4-(2,6-difluorobenzyloxy)cyclohexyl]-urea
Homo sapiens
pH 7.4, 30°C
0.0000016
trans-1-adamantan-1-yl-3-[4-(2-methylbenzyloxy)cyclohexyl]-urea
Homo sapiens
pH 7.4, 30°C
0.000001
trans-1-adamantan-1-yl-3-[4-(3,5-difluorophenoxy)cyclohexyl]-urea
Homo sapiens
pH 7.4, 30°C
0.0000017
trans-1-adamantan-1-yl-3-[4-(4-bromobenzyloxy)cyclohexyl]-urea
Homo sapiens
pH 7.4, 30°C
0.0000013
trans-4-(4-(3-adamantan-1-yl-ureido)-cyclohexyloxy)-benzoic acid
Homo sapiens
-
0.0000009
trans-4-(4-[3-(4-trifluoromethoxyphenyl)ureido]cyclohexyloxy)benzoic acid
Homo sapiens
pH 7.4, 30°C
0.0000013
trans-4-[4-(3-adamantan-1-ylureido)cyclohexyloxy]benzoic acid
Homo sapiens
pH 7.4, 30°C
0.000052
[1-[(4-chlorophenyl)carbamoyl]-3-phenylpiperidin-3-yl]acetic acid
Homo sapiens
-
0.000002
[6-(methylsulfonyl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidin]-1'-yl][4-(trifluoromethyl)phenyl]methanone
Homo sapiens
-
0.005
[N-(2-(trifluoromethyl)benzyl)benzamide]-4-(1H-tetrazole)
Homo sapiens
pH 7.0, 22°C
0.00029
(3-[4-(allyloxy)phenyl]oxiran-2-yl)(phenyl)methanone
Homo sapiens
-
IC50 is 0.00029 mM
0.00023
(3-[4-(benzyloxy)phenyl]oxiran-2-yl)(phenyl)methanone
Homo sapiens
-
IC50 is 0.00023 mM
0.00018
(4-bromophenyl)[3-(2-naphthyl)oxiran-2-yl]methanone
Homo sapiens
-
IC50 is 0.00018 mM
0.00015
(4-methylphenyl)[3-(2-naphthyl)oxiran-2-yl]methanol
Homo sapiens
-
IC50 is 0.00015 mM
0.00019
(4-methylphenyl)[3-(2-naphthyl)oxiran-2-yl]methanone
Homo sapiens
-
IC50 is 0.00019 mM
0.000005
(R)-N-(2-(diphenylamino)ethyl)-3-(3-(1-hydroxyureido)but-1-yn-1-yl)benzamide
Homo sapiens
-
pH 7, 37°C
-
0.0000012
(R)-N-(3,3-bis(4-fluorophenyl)propyl)-3-(3-(1-hydroxyureido)but-1-yn-1-yl)benzamide
Homo sapiens
-
pH 7, 37°C
-
0.0002
1,1'-(benzene-1,3-diyldicarbonyl)bis[N-(2,4-dichlorobenzyl)piperidine-4-carboxamide]
Homo sapiens
-
-
0.0001792
1,2-(ethylene)bis[[(adamant-1-yl)methyl]urea]
Homo sapiens
-
pH and temperature not specified in the publication
0.0000195
1,4-(phenylene)bis[(adamant-2-yl)urea]
Homo sapiens
-
pH and temperature not specified in the publication
0.000161
1,4-(phenylene)bis[[(adamant-1-yl)ethyl-1]urea]
Homo sapiens
-
pH and temperature not specified in the publication
0.0007796
1,4-(phenylene)bis[[(adamant-1-yl)methyl]urea]
Homo sapiens
-
pH and temperature not specified in the publication
0.0000263
1,4-(tetramethylene)bis[(adamant-1-yl)methyl]urea
Homo sapiens
-
pH and temperature not specified in the publication
0.0000072
1,4-(tetramethylene)bis[(adamant-1-yl)urea]
Homo sapiens
-
pH and temperature not specified in the publication
0.0000012
1,4-(tetramethylene)bis[[(adamant-1-yl)ethyl-1]urea]
Homo sapiens
-
pH and temperature not specified in the publication
0.0000023
1,4-(tetramethylene)bis[[(adamant-1-yl)sec-butyl-1]urea]
Homo sapiens
-
pH and temperature not specified in the publication
0.0000104
1,4-(tetramthylene)bis[(adamant-2-yl)urea]
Homo sapiens
-
pH and temperature not specified in the publication
0.0000004
1,6-(hexamethylene)bis[[(adamant-1-yl)methyl]urea]
Homo sapiens
-
pH and temperature not specified in the publication
0.000997
1,8-(octamethylene)bis[(adamant-1-yl)urea]
Homo sapiens
-
pH and temperature not specified in the publication
0.0000005
1,8-(octamethylene)bis[(adamant-1-ylethyl)urea]
Homo sapiens
-
pH and temperature not specified in the publication
0.0000026
1,8-(octamethylene)bis[(adamant-2-yl)urea]
Homo sapiens
-
pH and temperature not specified in the publication
0.0000005
1,8-(octamethylene)bis[[(adamant-1-yl)ethyl-1]urea]
Homo sapiens
-
pH and temperature not specified in the publication
0.0000073
1,8-(octamethylene)bis[[(adamant-1-yl)methyl]urea]
Homo sapiens
-
pH and temperature not specified in the publication
0.00144
1,8-(octamethylene)bis[[(adamant-1-yl)sec-butyl-1]urea]
Homo sapiens
-
pH and temperature not specified in the publication
0.000003
1-(1-methylsulfonyl-piperidin-4-yl)-3-(4-trifluoromethoxy-phenyl)-urea
Homo sapiens
-
-
0.000178
1-(2-((3-((3s,5s,7s)-adamantan-1-yl)ureido)methyl)benzyl)-1H-pyrrole-2-carboxylic acid
Homo sapiens
-
in 25 mM Bis-Tris-HCl, pH 7.0, at 37°C
0.000304
1-(3-((3-((3s,5s,7s)-adamantan-1-yl)ureido)methyl)benzyl)-1H-pyrrole-2-carboxylic acid
Homo sapiens
-
in 25 mM Bis-Tris-HCl, pH 7.0, at 37°C
0.000073
1-(4-((3-((3s,5s,7s)-adamantan-1-yl)ureido)methyl)benzyl)-1H-pyrrole-2-carboxylic acid
Homo sapiens
-
in 25 mM Bis-Tris-HCl, pH 7.0, at 37°C
0.0000014
1-adamantan-1-yl-3-(5-(2-[2-(2,2,2-trifluoroethoxy)ethoxy]-ethoxy)pentyl)urea
Homo sapiens
-
30°C, pH 7.0
0.0000017
1-adamantan-1-yl-3-(5-(2-[2-(4-ethylphenoxy)ethoxy]-ethoxy)pentyl)urea
Homo sapiens
-
30°C, pH 7.0
0.000014
1-adamantan-3-(5-(2-(2-ethylethoxy)ethoxy)pentyl)urea
Homo sapiens
-
purified recombinant enzyme
0.000012
1-trifluoromethoxyphenyl-3-(1-acetylpiperidin-4-yl)urea
Homo sapiens
-
in bis-Tris/HCl buffer, pH 7.0, at 25°C
0.000041
1-[(2,4-dimethylphenyl)sulfonyl]-N-(1,2,3,4-tetrahydronaphthalen-1-yl)piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000011
1-[(2,4-dimethylphenyl)sulfonyl]-N-(2-fluorophenyl)piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000012
1-[(2,4-dimethylphenyl)sulfonyl]-N-(2-hydroxyphenyl)piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00002
1-[(2,4-dimethylphenyl)sulfonyl]-N-(2-methylphenyl)piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000018
1-[(2,4-dimethylphenyl)sulfonyl]-N-(2-methylpropyl)piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00029
1-[(2,4-dimethylphenyl)sulfonyl]-N-(4-fluorophenyl)piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000004
1-[(2,4-dimethylphenyl)sulfonyl]-N-(4-hydroxyphenyl)piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000025
1-[(2,4-dimethylphenyl)sulfonyl]-N-(4-methoxyphenyl)piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000012
1-[(2,4-dimethylphenyl)sulfonyl]-N-(4-nitrophenyl)piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00002
1-[(2,4-dimethylphenyl)sulfonyl]-N-(4-phenoxyphenyl)piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.03
1-[(2,4-dimethylphenyl)sulfonyl]-N-(6-methoxy-1,3-benzodioxol-5-yl)piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000023
1-[(2,4-dimethylphenyl)sulfonyl]-N-(isoquinolin-5-yl)piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000083
1-[(2,4-dimethylphenyl)sulfonyl]-N-(naphthalen-2-yl)piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000023
1-[(2,4-dimethylphenyl)sulfonyl]-N-(quinolin-3-yl)piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000013
1-[(2,4-dimethylphenyl)sulfonyl]-N-(quinolin-6-yl)piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000006
1-[(2,4-dimethylphenyl)sulfonyl]-N-(quinolin-8-yl)piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000017
1-[(2,4-dimethylphenyl)sulfonyl]-N-(tricyclo[3.3.1.13,7]dec-1-yl)piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000069
1-[(2,4-dimethylphenyl)sulfonyl]-N-phenylpiperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0069
1-[(2,4-dimethylphenyl)sulfonyl]-N-[(1R,2S)-2-phenylcyclopropyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00064
1-[(2,4-dimethylphenyl)sulfonyl]-N-[3-(trifluoromethyl)phenyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00025
1-[(2,4-dimethylphenyl)sulfonyl]-N-[4-(morpholin-4-yl)phenyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00002
1-[(2,4-dimethylphenyl)sulfonyl]-N-[4-(piperidin-1-yl)phenyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000067
1-[(2,4-dimethylphenyl)sulfonyl]-N-[4-(propan-2-yl)phenyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000023
1-[(2,4-dimethylphenyl)sulfonyl]-N-[4-(trifluoromethoxy)phenyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00003
1-[(2,4-dimethylphenyl)sulfonyl]-N-[4-(trifluoromethyl)phenyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000016
1-[(2,4-dimethylphenyl)sulfonyl]-N-[4-[(trifluoromethyl)sulfonyl]phenyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000911
1-[(2-bromophenyl)sulfonyl]-N-(2,4-dichlorobenzyl)piperidine-4-carboxamide
Homo sapiens
-
-
0.0000521
1-[(4-chloro-2,5-dimethylphenyl)sulfonyl]-N-(2,4-dichlorobenzyl)piperidine-4-carboxamide
Homo sapiens
-
-
0.000164
1-[(4-tert-butylphenyl)sulfonyl]-N-(2,4-dichlorobenzyl)piperidine-4-carboxamide
Homo sapiens
-
-
0.0002
1-[(5-chlorothiophen-2-yl)sulfonyl]-N-(2,4-dichlorobenzyl)piperidine-4-carboxamide
Homo sapiens
-
-
0.000747
1-[2-[(cyclohexylcarbamoyl)amino]benzyl]-1H-pyrrole-2-carboxylic acid
Homo sapiens
-
in 25 mM Bis-Tris-HCl, pH 7.0, at 37°C
0.000022
1-[3-(3-morpholin-4-ylpropoxy)phenyl]-3-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]thiourea
Homo sapiens
-
-
0.0000008
1-[3-(3-morpholin-4-ylpropoxy)phenyl]-3-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]urea
Homo sapiens
-
-
0.0000082
1-[3-(3-morpholin-4-ylpropoxy)phenyl]-3-[4-(trifluoromethoxy)phenyl]urea
Homo sapiens
-
-
0.0000012
1-[3-(3-morpholin-4-ylpropoxy)phenyl]-3-[4-(trifluoromethyl)phenyl]urea
Homo sapiens
-
-
0.000943
1-[3-([[4-(trifluoromethoxy)phenyl]carbamoyl]amino)benzyl]-1H-pyrrole-2-carboxylic acid
Homo sapiens
-
in 25 mM Bis-Tris-HCl, pH 7.0, at 37°C
0.001923
1-[3-[(cyclohexylcarbamoyl)amino]benzyl]-1H-pyrrole-2-carboxylic acid
Homo sapiens
-
in 25 mM Bis-Tris-HCl, pH 7.0, at 37°C
0.000258
1-[4-([[4-(trifluoromethoxy)phenyl]carbamoyl]amino)benzyl]-1H-pyrrole-2-carboxylic acid
Homo sapiens
-
in 25 mM Bis-Tris-HCl, pH 7.0, at 37°C
0.000252
1-[4-[(cyclohexylcarbamoyl)amino]benzyl]-1H-pyrrole-2-carboxylic acid
Homo sapiens
-
in 25 mM Bis-Tris-HCl, pH 7.0, at 37°C
0.0000397
1-[[1-((adamant-1-yl)methylcarbamoyl)piperidin-4-yl]methyl]-3-[(adamant-1-yl)methyl]urea
Homo sapiens
-
pH and temperature not specified in the publication
0.000003
12-(3-adamantan-1-ylureido)dodecanoic acid
Homo sapiens
-
in bis-Tris/HCl buffer, pH 7.0, at 25°C
0.0000008
12-(3-adamantan-1-ylureido)dodecanoic acid butyl ester
Homo sapiens
-
in bis-Tris/HCl buffer, pH 7.0, at 25°C
0.00031
2-cyclohexa-1,5-dien-1-yl-3-(phenylsulfinyl)oxirane
Homo sapiens
-
IC50 is 0.00031 mM
0.034
2-cyclohexa-1,5-dien-1-yl-3-[methoxy(phenyl)methyl]oxirane
Homo sapiens
-
IC50 is 0.034 mM
0.002
2-hydroxy-N-[3-(3-morpholin-4-ylpropoxy)phenyl]-2-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]acetamide
Homo sapiens
-
IC50 above 0.02 mM
0.000023
2-hydroxy-N-[3-(3-morpholin-4-ylpropoxy)phenyl]-3-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]propanamide
Homo sapiens
-
-
0.00053
2-hydroxy-N-[3-(3-morpholin-4-ylpropoxy)phenyl]-4-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]butanamide
Homo sapiens
-
-
0.00009
3-(3-(1-hydroxyureido)but-1-yn-1-yl)-N-(2-(trifluoromethyl)-benzyl)benzamide
Homo sapiens
-
pH 7, 37°C
-
0.00007
3-(3-(1-hydroxyureido)but-1-yn-1-yl)-N-(3-phenyl-3-(4-(trifluoromethoxy)phenyl)propyl)benzamide
Homo sapiens
-
pH 7, 37°C
-
0.000004
3-(3-(1-hydroxyureido)but-1-yn-1-yl)-N-(4-methoxy-2-(trifluoromethyl)benzyl)-benzamide
Homo sapiens
-
pH 7, 37°C
-
0.0003
3-(3-(1-hydroxyureido)hex-1-yn-1-yl)-N-(2-(trifluoromethyl)-benzyl)benzamide
Homo sapiens
-
pH 7, 37°C
-
0.0000753
4,5-dimethoxy-2-nitrophenyl 4-[(2,4-dichlorobenzyl)carbamoyl]piperidine-1-carboxylate
Homo sapiens
-
-
0.0026
4-(3-(1-hydroxyureido)but-1-yn-1-yl)-N-(2-(trifluoromethyl)-benzyl)benzamide
Homo sapiens
-
pH 7, 37°C
-
0.00016
4-([3-(2-naphthyl)oxiran-2-yl]carbonyl)benzoic acid
Homo sapiens
-
IC50 is 0.00016 mM
0.113
4-([3-(4-fluorophenyl)oxiran-2-yl]carbonyl)benzoic acid
Homo sapiens
-
IC50 is 0.113 mM
0.000017
4-[([1-[(2,4-dimethylphenyl)sulfonyl]piperidin-4-yl]carbonyl)amino]benzoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0000006
6-[([1-[(2,4-dimethylphenyl)sulfonyl]piperidin-4-yl]carbonyl)amino]naphthalene-2-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0000009
cis-4-[4-(3-adamantan-1-yl-ureido)cyclohexyloxy]benzoic acid
Homo sapiens
-
in bis-Tris/HCl buffer, pH 7.0, at 25°C
0.000043
ethyl 1-(2-((3-((3s,5s,7s)-adamantan-1-yl)ureido)methyl)benzyl)-1H-pyrrole-2-carboxylate
Homo sapiens
-
in 25 mM Bis-Tris-HCl, pH 7.0, at 37°C
0.000046
ethyl 1-(3-((3-((3s,5s,7s)-adamantan-1-yl)ureido)methyl)benzyl)-1H-pyrrole-2-carboxylate
Homo sapiens
-
in 25 mM Bis-Tris-HCl, pH 7.0, at 37°C
0.000087
ethyl 1-(4-((3-((3s,5s,7s)-adamantan-1-yl)ureido)methyl)benzyl)-1H-pyrrole-2-carboxylate
Homo sapiens
-
in 25 mM Bis-Tris-HCl, pH 7.0, at 37°C
0.002009
ethyl 1-[2-([[4-(trifluoromethoxy)phenyl]carbamoyl]amino)benzyl]-1H-pyrrole-2-carboxylate
Homo sapiens
-
in 25 mM Bis-Tris-HCl, pH 7.0, at 37°C
0.000039
ethyl 1-[2-[(cyclohexylcarbamoyl)amino]benzyl]-1H-pyrrole-2-carboxylate
Homo sapiens
-
in 25 mM Bis-Tris-HCl, pH 7.0, at 37°C
0.000027
ethyl 1-[3-[(cyclohexylcarbamoyl)amino]benzyl]-1H-pyrrole-2-carboxylate
Homo sapiens
-
in 25 mM Bis-Tris-HCl, pH 7.0, at 37°C
0.000611
ethyl 1-[4-([[4-(trifluoromethoxy)phenyl]carbamoyl]amino)benzyl]-1H-pyrrole-2-carboxylate
Homo sapiens
-
in 25 mM Bis-Tris-HCl, pH 7.0, at 37°C
0.000023
ethyl 1-[4-[(cyclohexylcarbamoyl)amino]benzyl]-1H-pyrrole-2-carboxylate
Homo sapiens
-
in 25 mM Bis-Tris-HCl, pH 7.0, at 37°C
0.0000021
methyl 4-((1,2,3,4-tetrahydronaphthalene-2-carboxamido)methyl)benzoic acid
Homo sapiens
-
pH 7.0, 30°C
0.0000018
methyl 4-([[(6-hydroxynaphthalen-2-yl)carbonyl]amino]methyl)benzoate
Homo sapiens
-
pH 7.0, 30°C
0.0000024
methyl 4-([[(6-methoxynaphthalen-2-yl)carbonyl]amino]methyl)benzoate
Homo sapiens
-
pH 7.0, 30°C
0.0000085
methyl 4-[([1-[(2,4-dimethylphenyl)sulfonyl]piperidin-4-yl]carbonyl)amino]benzoate
Homo sapiens
-
pH and temperature not specified in the publication
0.00011
methyl 6-[([1-[(2,4-dimethylphenyl)sulfonyl]piperidin-4-yl]carbonyl)amino]naphthalene-2-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0000336
N'-(2-chlorophenyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carbohydrazide
Homo sapiens
-
-
0.000064
N'-[2-(3-chlorophenyl)ethyl]-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carbohydrazide
Homo sapiens
-
-
0.0000201
N-(1,2,3,4-tetrahydronaphthalen-1-yl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000052
N-(1,3-benzodioxol-5-yl)-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000007
N-(1-acetylpiperidin-4-yl)-N'-(adamant-1-yl)urea
Homo sapiens
-
in bis-Tris/HCl buffer, pH 7.0, at 25°C
0.000011
N-(1-tert-butoxypiperidin-4-yl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000491
N-(2,3-dihydro-1H-inden-2-yl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.000128
N-(2,4-dichloro-6-methylbenzyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000445
N-(2,4-dichlorobenzyl)-1-[(2,4,6-tri-tert-butylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.00002
N-(2,4-dichlorobenzyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000469
N-(2,4-dichlorobenzyl)-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000876
N-(2,4-dichlorobenzyl)-1-[(2-fluorophenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.00015
N-(2,4-dichlorobenzyl)-1-[(4-fluoro-2-nitrophenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000239
N-(2,4-dichlorobenzyl)-1-[(4-methoxy-2,3,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000322
N-(2,4-difluorobenzyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000591
N-(2,5-dichlorobenzyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000006
N-(2-bromophenyl)-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000541
N-(2-chloro-4-fluorobenzyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000127
N-(2-chloro-6-fluorobenzyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000274
N-(2-chlorobenzyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000087
N-(2-chlorophenyl)-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000372
N-(2-methylcyclohexyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000433
N-(2-phenylethyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.000035
N-(3,3-diphenylpropyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.000032
N-(3,4-dichlorobenzyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.000055
N-(3,4-dichlorophenyl)-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000025
N-(3,5-dichlorophenyl)-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000002
N-(3-(4-chlorophenyl)-3-phenylpropyl)-3-(3-(1-hydroxyureido)-but-1-yn-1-yl)benzamide
Homo sapiens
-
pH 7, 37°C
-
0.0000251
N-(3-methylbutyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.000045
N-(4-bromophenyl)-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00005
N-(4-chlorobenzyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0022
N-(4-chlorophenyl)-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000396
N-(4-methylcyclohexyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.00014
N-(4-[(3-phenyloxiran-2-yl)carbonyl]phenyl)acetamide
Homo sapiens
-
IC50 is 0.00014 mM
0.0000126
N-(cyclohexylmethyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000058
N-(cyclohexylmethyl)-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000394
N-(naphthalen-1-ylmethyl)-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.000042
N-benzyl-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.000029
N-cyclobutyl-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000026
N-cycloheptyl-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000164
N-cyclohexyl-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.000102
N-cyclohexyl-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000028
N-cyclooctyl-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000373
N-cyclopentyl-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000052
N-cyclopentyl-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000046
N-cyclopropyl-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0002
N-naphthalen-1-yl-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0002
N-piperidin-1-yl-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000291
N-[1-(4-chlorophenyl)ethyl]-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000287
N-[2-chloro-5-(trifluoromethyl)benzyl]-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.000185
N-[2-[4-(benzyloxy)phenyl]ethyl]-2-hydroxy-3-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]propanamide
Homo sapiens
-
-
0.000011
N-[2-[4-(benzyloxy)phenyl]ethyl]-2-hydroxy-4-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]butanamide
Homo sapiens
-
-
0.00154
N-[2-[4-(benzyloxy)phenyl]ethyl]-2-oxo-3-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]propanamide
Homo sapiens
-
-
0.000685
N-[2-[4-(benzyloxy)phenyl]ethyl]-2-oxo-4-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]butanamide
Homo sapiens
-
-
0.002
N-[3-(3-morpholin-4-ylpropoxy)phenyl]-2-oxo-2-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]acetamide
Homo sapiens
-
IC50 above 0.02 mM
0.000049
N-[3-(3-morpholin-4-ylpropoxy)phenyl]-2-oxo-3-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]propanamide
Homo sapiens
-
-
0.000048
N-[3-(3-morpholin-4-ylpropoxy)phenyl]-2-oxo-4-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]butanamide
Homo sapiens
-
-
0.000055
N-[3-(3-morpholin-4-ylpropoxy)phenyl]-2-[4-(trifluoromethyl)phenyl]acetamide
Homo sapiens
-
-
0.015
N-[3-(3-morpholin-4-ylpropoxy)phenyl]-4-(trifluoromethyl)benzenesulfonamide
Homo sapiens
-
-
0.0036
N-[3-(3-morpholin-4-ylpropoxy)phenyl]-N'-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]sulfamide
Homo sapiens
-
-
0.0000025
N-[3-(3-morpholin-4-ylpropoxy)phenyl]-N-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-ylmethyl]formamide
Homo sapiens
-
-
0.000088
N-[3-(3-morpholin-4-ylpropoxy)phenyl]-N-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]formamide
Homo sapiens
-
-
0.00011
N-[3-(3-morpholin-4-ylpropoxy)phenyl]-N2-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]glycinamide
Homo sapiens
-
-
0.000043
N-[3-carbamoyl-4-(piperidin-1-yl)phenyl]-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00031
N-[4-(benzyloxy)phenyl]-2-hydroxy-2-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]acetamide
Homo sapiens
-
-
0.00027
N-[4-(benzyloxy)phenyl]-2-hydroxy-3-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]propanamide
Homo sapiens
-
-
0.00021
N-[4-(benzyloxy)phenyl]-2-oxo-2-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]acetamide
Homo sapiens
-
-
0.0011
N-[4-(benzyloxy)phenyl]-2-oxo-3-[(3S,5S)-tricyclo[3.3.1.13,7]dec-1-yl]propanamide
Homo sapiens
-
-
0.000173
N-[4-chloro-3-(trifluoromethyl)benzyl]-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.000078
N-[4-chloro-3-(trifluoromethyl)phenyl]-1-[(2,4-dimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000263
tert-butyl 4-[([1-[(2,4-dimethylphenyl)sulfonyl]piperidin-4-yl]carbonyl)amino]piperidine-1-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0000013
trans-4-[4-(3-adamantan-1-yl-ureido)cyclohexyloxy]benzoic acid
Homo sapiens
-
in bis-Tris/HCl buffer, pH 7.0, at 25°C
0.00016
[3-(2-naphthyl)oxiran-2-yl](4-nitrophenyl)methanone
Homo sapiens
-
IC50 is 0.00016 mM
0.00048
[3-(4-isopropylphenyl)oxiran-2-yl](phenyl)methanone
Homo sapiens
-
IC50 is 0.00048 mM
0.00051
[3-(4-phenoxycyclohexa-1,5-dien-1-yl)oxiran-2-yl](phenyl)methanone
Homo sapiens
-
IC50 is 0.00051 mM
0.00016
[4-(bromomethyl)phenyl][3-(2-naphthyl)oxiran-2-yl]methanone
Homo sapiens
-
IC50 is 0.00016 mM
0.00006 - 0.5
additional information
Homo sapiens
-
QSAR and classification in a seven-discriptor model of enzyme inhibition by 348 urea-like compounds, IC50 ranging from 60 nM to 0.5 mM, overview
-
0.000206
1-(2-hydroxyphenyl)-3-tricyclo[3.3.1.13,7]dec-1-ylurea
Homo sapiens
recombinant enzyme expressed in Escherichia coli
0.000258
1-(2-hydroxyphenyl)-3-tricyclo[3.3.1.13,7]dec-1-ylurea
Homo sapiens
recombinant enzyme expressed in Sf9 cells
0.000613
1-(3-hydroxypropyl)-3-tricyclo[3.3.1.13,7]dec-1-ylurea
Homo sapiens
recombinant enzyme expressed in Escherichia coli
0.000813
1-(3-hydroxypropyl)-3-tricyclo[3.3.1.13,7]dec-1-ylurea
Homo sapiens
recombinant enzyme expressed in Sf9 cells
0.00012
1-(5-hydroxypentyl)-3-tricyclo[3.3.1.13,7]dec-1-ylurea
Homo sapiens
recombinant enzyme expressed in Escherichia coli
0.000128
1-(5-hydroxypentyl)-3-tricyclo[3.3.1.13,7]dec-1-ylurea
Homo sapiens
recombinant enzyme expressed in Sf9 cells
0.000008
1-[5-[2-(2-ethoxyethoxy)ethoxy]pentyl]-3-tricyclo[3.3.1.13,7]dec-1-ylurea
Homo sapiens
recombinant enzyme expressed in Escherichia coli
0.000009
1-[5-[2-(2-ethoxyethoxy)ethoxy]pentyl]-3-tricyclo[3.3.1.13,7]dec-1-ylurea
Homo sapiens
recombinant enzyme expressed in Sf9 cells
0.000014
1-[5-[2-(2-ethoxyethoxy)ethoxy]pentyl]-3-tricyclo[3.3.1.13,7]dec-1-ylurea
Homo sapiens
-
0.0000022
12-[(tricyclo[3.3.1.13,7]dec-1-ylcarbamoyl)amino]dodecanoic acid
Homo sapiens
recombinant enzyme expressed in Escherichia coli
0.0000023
12-[(tricyclo[3.3.1.13,7]dec-1-ylcarbamoyl)amino]dodecanoic acid
Homo sapiens
recombinant enzyme expressed in Sf9 cells
0.000003
12-[(tricyclo[3.3.1.13,7]dec-1-ylcarbamoyl)amino]dodecanoic acid
Homo sapiens
-
0.000005
3-[1-[(4-chlorophenyl)carbamoyl]-3-phenylpiperidin-3-yl]propanoic acid
Homo sapiens
-
0.000016
3-[1-[(4-chlorophenyl)carbamoyl]-3-phenylpiperidin-3-yl]propanoic acid
Homo sapiens
-
0.03391
5,7-dihydroxy-2-(2-hydroxy-6-methoxyphenyl)-4H-1-benzopyran-4-one
Homo sapiens
pH not specified in the publication, 37°C
0.08008
5,7-dihydroxy-2-(2-hydroxy-6-methoxyphenyl)-4H-1-benzopyran-4-one
Homo sapiens
pH not specified in the publication, 37°C
0.000008
6'-(methylsulfonyl)-N-(2-phenylcyclopropyl)-1H,4'H-spiro[azepane-4,3'-chromene]-1-carboxamide
Homo sapiens
-
0.000011
6'-(methylsulfonyl)-N-(2-phenylcyclopropyl)-1H,4'H-spiro[azepane-4,3'-chromene]-1-carboxamide
Homo sapiens
-
0.000003
6-(methylsulfonyl)-4-oxo-N-(2-phenylcyclopropyl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
Homo sapiens
-
0.000004
6-(methylsulfonyl)-4-oxo-N-(2-phenylcyclopropyl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
Homo sapiens
-
0.000011
6-(methylsulfonyl)-4-oxo-N-(2-phenylcyclopropyl)-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidine]-1'-carboxamide
Homo sapiens
-
0.0000006
N,N'-octane-1,8-diylbis[N'-[(adamantan-1-yl)methyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000007
N,N'-octane-1,8-diylbis[N'-[(adamantan-1-yl)methyl]urea]
Homo sapiens
pH 7.4, 37°C
0.0000038
N-(3-ethyladamantan-1-yl)-N'-(1-propanoylpiperidin-4-yl)urea
Homo sapiens
pH 7.4, 37°C
0.0002686
N-(3-ethyladamantan-1-yl)-N'-(1-propanoylpiperidin-4-yl)urea
Homo sapiens
pH 7.4, 37°C
0.0000024
N-adamantan-1-yl-N'-[(3-ethyladamantan-1-yl)methyl]urea
Homo sapiens
pH 7.4, 37°C
0.0000027
N-adamantan-1-yl-N'-[(3-ethyladamantan-1-yl)methyl]urea
Homo sapiens
pH 7.4, 37°C
0.00048
N-[5-[2-(2-ethoxyethoxy)ethoxy]pentyl]-N'-(4-hydroxyadamantan-1-yl)urea
Homo sapiens
pH 7.4, 37°C
0.00087
N-[5-[2-(2-ethoxyethoxy)ethoxy]pentyl]-N'-(4-hydroxyadamantan-1-yl)urea
Homo sapiens
pH 7.4, 37°C
0.000003
12-(3-adamantan-1-yl-ureido)dodecanoic acid
Homo sapiens
-
purified recombinant enzyme
0.000107
12-(3-adamantan-1-yl-ureido)dodecanoic acid
Homo sapiens
-
in 25 mM Bis-Tris-HCl, pH 7.0, at 37°C
0.0000079
N-cycloheptyl-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
-
0.0000079
N-cycloheptyl-1-[(2,4,6-trimethylphenyl)sulfonyl]piperidine-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.12
-
purified recombinant enzyme, substrate cyano(6-methoxy-2-naphthyl)methyl (3,3-dimethyloxiran-2-yl)methyl carbonate
0.36
-
purified recombinant enzyme, substrate [3-(4-chlorophenyl)oxiran-2-yl]methyl cyano(6-methoxy-2-naphthyl)methyl carbonate
0.38
-
purified recombinant enzyme, substrate cyano(6-methoxy-2-naphthyl)methyl [3-(4-nitrophenyl)oxiran-2-yl]methyl carbonate
0.41
-
purified recombinant enzyme, substrate cyano(6-methoxy-2-naphthyl)methyl (3-ethyloxiran-2-yl)methyl carbonate
0.53
-
purified recombinant enzyme, substrate cyano(2-methoxy-naphthalen-6-yl)methyl trans-2-(3-propyloxiran-2-yl) acetate
0.71
-
purified recombinant enzyme, substrate cyano(6-methoxy-2-naphthyl)methyl (3-phenyloxiran-2-yl)acetate
1.02
-
purified recombinant enzyme, substrate cyano(6-methoxy-2-naphthyl)methyl (3-propyloxiran-2-yl)methyl carbonate
2.69
-
purified recombinant enzyme, substrate cyano(6-methoxy-2-naphthyl)methyl (3-phenyloxiran-2-yl)methyl carbonate
additional information
additional information
-
substrate specificity, 2 enzymes with different specificities termed cytosolic TESO hydrolase and cytosolic PNSO hydrolase
additional information
-
development of a high-throughput screen assay for soluble epoxide hydrolase inhibition using (3-phenyl-oxiranyl)-acetic acid cyano-(6-methoxy-naphthalen-2-yl)-methyl ester as a substrate. Assay is accurate and precise
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.4
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
maximal activity at pH 5.0, 70% of maximal activity at pH 6.0, no activity at pH 7.0-8.0, with allylic epoxyalcohols as substrates
7.4 - 9
-
cytosolic enzyme shows higher activity at pH 7.4, microsomal enzyme shows higher activity at pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
30
37
37
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
654749, 663350, 683240, 683760, 683815, 699541, 699556, 700601, 707633, 707669, 707676, 707679, 707681, 708017, 708395, 709447, 709448, 709452, 709899, 710044, 710480, 715853, 715861, 731473, 731476, 731877, 732124, 732298, 732314, 752593, 752734, 752930, 752944, 752977, 753330, 753841, 753858, 754366, 754381, 754798, 755313, 755389, 755394, 755396
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
treatment with angiotensin II results in increased expression of soluble epoxide hydrolase at both the mRNA and protein level
-
liver malignant neoplastic tissue and their surrounding non-neoplastic tissues show loss of sEH. Liver cholangiocarcinoma shows significant increase in sEH staining as compared to low or absent staining in corresponding non-neoplastic tissue samples
-
no staining in adenocarcinoma cells and islet cell tumors but high staining of matched benigns
-
sEH expression in renal malignant neoplasms and surrounding non-neoplastic tissues is significantly decreased
EH3 is highly expressed in the skin, the highest expression of EH3 mRNA is in the outer epidermis where the water permeability barrier is formed
additional information
in vascular smooth muscle and endothelial cell layers, in white matter
sEH is expressed in the wall of pulmonary arteries, however, sEH expression is absent in samples from patients with pulmonary hypertension
-
distribution of enzyme mainly in the neuronal cell bodies, oligodendrocytes and scattered astrocytes. High expression of enzyme in ependymal cells of choroid plexus
-
diseased and healthy, primarily vascular localization, low enzyme levels in the surrounding tubules
-
-
208900, 208917, 208931, 208934, 660713, 661511, 663199, 663275, 663434, 695933, 708022, 708324, 715837
additional information
sEH is expressed and metabolically active in various tissues and cell types, including endothelial cells and cardiomyocytes
additional information
-
stomach adenocarcinoma cells with low sEH staining. Skin basal cell carcinoma with low to moderate sEH staining. Testis seminoma with increased sEH expression. Ovary cystadenocarcinoma with low to moderate sEH staining. sEH absent from uterine endometrium. Squamous cell carcinoma of mouth/tongue with low to high sEH staining. Pharynx and larync squamous cell carcinoma with low to moderate sEH staining
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
208900, 208917, 208931, 208934, 660713, 661511, 662565, 663199, 663275, 663434, 695933, 700587, 708022
-
-
-
657156, 660664, 660702, 660789, 660799, 662594, 700587, 708022, 708324, 709908, 731107, 731442, 731448, 732196, 732301, 732722
additional information
sEH shows both, peroxisomal and cytosolic localizations in vivo
sEH shows both, peroxisomal and cytosolic localizations in vivo, peroxisomal import occurs when expression levels are high or when the Ser-Lys-Met motif (amino acids 553-555) is accessible
-
in some cell types sEH shows a dual localisation, both cytosolic and peroxisomal
additional information
-
highest level found in smooth endoplasmic reticulum, lower levels observed in rough endoplasmic reticulum, Golgi apparatus, nuclear membrane and plasma membrane. The enzyme is synthesized in membrane-bound polysomes and inserted cotranslationally into the endoplasmic reticulum
-
additional information
-
human sEH subcellular localization is tissue dependent, not detectable in mitochondria or nucleus
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
physiological function
additional information
malfunction
association of sEH gene Ephx2 polymorphisms with increased risk of atherosclerosis and cardiovascular diseases, role of epoxyeicosatrienoic acids, EETs, and sEH in the pathogenesis of atherosclerosis, overview
malfunction
inhibition of sEH has beneficial effects on vascular inflammation and hypertension
malfunction
polymorphimsm in gene EPHX2 are associated with ischemic stroke risk. sEH inhibition and gene deletion reduce infarct size after focal cerebral ischemia in mice
malfunction
sEH expression is absent in samples from patients with pulmonary hypertension. As sEH inhibitors do not promote the development of pulmonary hypertension it seems likely that the N-terminal lipid phosphatase may play a role in the development of this disease
malfunction
enzyme single nucleotide polymorphisms are associated with cardiovascular disease
metabolism
the enzyme is involved in the arachidonate cascade, pathways overview
physiological function
conversion of epoxyeicosatrienoic acids to their corresponding diols, dihydroxyeicosatrienoic acids, DHETS, by sEH is responsible for decreasing EET levels and thereby diminishing their beneficial cardiovascular properties, detailed overview
physiological function
sEH plays an important role in the physiology of cells including proliferation. The epoxide hydrolase and phosphatase domains of sEH have different biological functions
physiological function
soluble epoxide hydrolase is a key enzyme in the metabolic conversion and degradation of P450 eicosanoids called epoxyeicosatrienoic acids, EETs
physiological function
soluble epoxide hydrolase is a key enzyme involved in the metabolism of epoxy fatty acid mediators such as epoxyeicosatrienoic acids with emerging roles in the regulations of hypertension and inflammation
physiological function
through its metabolism of the epoxyeicosatrienoic acids and other lipid mediators, the enzyme contributes to the regulation of vascular tone, nociception, angiogenesis and the inflammatory response. The enzyme plays a role in either the initiation of corpus luteum formation, and/or in the regression of the structure. The enzyme is implicated in the pathology of pulmonary hypertension
physiological function
activities of EPHX2 and EPHX3 in production of the linoleate triols detected as end products of the 12R-LOX pathway in the epidermis and functioning in formation of the mammalian water permeability barrier
physiological function
mammalian soluble epoxide hydrolase (sEH) is involved in mediating the metabolism of the endogenous lipids epoxides such as epoxyeicosatrienoic acids (EETs) that are derived from arachidonic acid. The sEH converts epoxide-containing substrates into the corresponding more polar and less potent vicinal diols. EETs are vasodilation mediators through the activation of the Ca2+-activated K+-channels in endothelial cells which benefit many renal and cardiovascular diseases. EETs are reported to be involved in the cell angiogenesis and proliferation which may offer a protective role in ischemic and reperfusion injury. Furthermore, the EETs are anti-inflammatory mediators in endothelial cells by inhibiting the expression of the proatherogenic mediator vascular cell adhesion molecule-1 that is induced by tumor necrosis factor-alpha (TNF-alpha). In addition, EETs suppress the NF-kappaB-mediated expression of cytokines by activating PPARgamma
physiological function
the human soluble Epoxide Hydrolase (hsEH) is an enzyme involved in the hydrolysis of endogenous anti-inflammatory and cardio-protective signalling mediators known as epoxyeicosatrienoic acids (EETs). EETs' conversion into the corresponding diols by hsEH generates non-bioactive molecules, thereby the enzyme inhibition is be expected to enhance the EETs bioavailability, and their beneficial properties
physiological function
the role of the C-terminal (epoxide hydrolase) domain is confirmed by its participation in the metabolism of epoxy fatty acids to vicinal diols that are endogenous mediators of various undesirable physiological processes. Inhibition of sEH is efficient in inflammatory and neuropathic pains
malfunction
-
diabetes is one of the main factors responsible for end-stage renal disease caused by impaired endothelium
malfunction
-
sEH inhibitor treatment is effectively preventing pressure overload- and angiotensin II-induced cardiac hypertrophy and reverses the pre-established cardiac hypertrophy caused by chronic pressure overload, overview
physiological function
-
sEH is a xenobiotic-metabolizing enzyme that metabolizes epoxides to produce vicinal diols. Epoxyeicosatrienoic acids are substrates of sEH and have important roles in renal function such as ion transport and the proliferation of cells and the action of epoxyeicosatrienoic acids is important for maintaining renal and vascular homeostasis
physiological function
-
transgenic enzyme expression in endothelium results in impaired endothelium-dependent vasodilation in the cerebral circulation. Females are more susceptible to enhanced ischemic damage as a result of increased endothelial soluble epoxide hydrolase than males, especially in end-arteriolar striatal region
physiological function
activities of EPHX2 and EPHX3 in production of the linoleate triols detected as end products of the 12R-lipoxygenase pathway in the epidermis and functioning in formation of the mammalian water permeability barrier
additional information
enzyme inhibition protects against ischemic stroke, mechanism and cytoprotective, anti-inflammatory, and other effects, overview
additional information
evaluation of different epoxide hydrolase (EH) enzymes in the hydrolysis of skin-relevant fatty acid epoxides and comparison to the products to those of acid-catalyzed hydrolysis
additional information
evaluation of different epoxide hydrolase (EH) enzymes in the hydrolysis of skin-relevant fatty acid epoxides and comparison to the products to those of acid-catalyzed hydrolysis
additional information
-
evaluation of different epoxide hydrolase (EH) enzymes in the hydrolysis of skin-relevant fatty acid epoxides and comparison to the products to those of acid-catalyzed hydrolysis
additional information
the enzyme is bifunctional possessing C-terminal epoxide hydrolase and N-terminal phosphatase activities
additional information
-
cardioprotective roles of sEH inhibition in myocardial ischemia-reperfusion injury
additional information
evaluation of different epoxide hydrolase (EH) enzymes in the hydrolysis of skin-relevant fatty acid epoxides and comparison to the products to those of acid-catalyzed hydrolysis
additional information
evaluation of different epoxide hydrolase (EH) enzymes in the hydrolysis of skin-relevant fatty acid epoxides and comparison to the products to those of acid-catalyzed hydrolysis
additional information
-
evaluation of different epoxide hydrolase (EH) enzymes in the hydrolysis of skin-relevant fatty acid epoxides and comparison to the products to those of acid-catalyzed hydrolysis
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). HYES_HUMAN
555
0
62616
Swiss-Prot
Secretory Pathway (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
2 * 80000, SDS-PAGE, dimerization is required for enzymatic activity
130000
62000
62500
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
the monomer of the antiparallel sEH homodimer consists of two globular proteins connected through a bridge containing excess proline, and each protein possesses its own domain (C-terminal epoxide hydrolase and N-terminal phosphatase) for binding to various substrates
homodimer
dimer
homodimer
monomer
additional information
homodimer
2 * 80000, SDS-PAGE, dimerization is required for enzymatic activity
additional information
the 25 kDa C-terminal part, with a hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity, the enzyme's phosphatase activity of EC3.1.3.76 is located at the 35 kDa N-terminal part which has a different alpha/beta-fold, quarternary structure analysis, structure-mechanism relationship
additional information
-
the 25 kDa C-terminal part, with a hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity, the enzyme's phosphatase activity of EC3.1.3.76 is located at the 35 kDa N-terminal part which has a different alpha/beta-fold, quarternary structure analysis, structure-mechanism relationship
additional information
-
quarternary structure, monomers interact in a head-to-tail manner, the enzyme contains the DXDX(T/V) motif
additional information
-
the 25 kDa C-terminal part, with a different hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity, the enzyme's phosphatase activity of EC3.1.3.76 is located at the 35 kDa N-terminal part which has a alpha/beta-fold, structure analysis
additional information
-
the 25 kDa C-terminal part, with a hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity, the enzyme's phosphatase activity of EC3.1.3.76 is located at the 35 kDa N-terminal part which has a different alpha/beta-fold, structure analysis
additional information
-
the C-terminal domain catalyzes epoxy fatty acid hydrolysis, the N-terminal catalytic domain has also phosphatase activity with specificity for fatty acid diol phosphates
additional information
-
the C-terminal part harbors the epoxide hydrolase activity, the enzyme's phosphatase activity of EC 3.1.3.76 is located at the N-terminal part, Arg287 may be involved in formation of the quaternary enzyme structure
additional information
-
the C-terminal part, with a hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity, the enzyme's phosphatase activity of EC3.1.3.76 is located at the N-terminal part which has a different alpha/beta-fold
additional information
-
each monomer is comprised of two distinct structural domains, linked by a proline-rich segment, the 35 kDa C-terminal domain displays epoxide hydrolase activity, while the N-terminal domain exhibits phosphatase activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 30% (w/v) PEG 3350, 0-10% (w/v) sucrose, at 4°C
His-tagged hydrolase domain, in complex with inhibitor N-(5-chloro-1,3-benzoxazol-2-yl)-2-cyclopentylacetamide. The compound binds deeply within the active site of sEH, forming a network of hydrogen-bonding interactionswith key protein atoms
modeling of structure in complex with inhibitor N-(1-trifluoroacetylpiperidin-4-yl)-N'-(adamant-1-yl) urea
purified recombinant apoenzyme in complex with inhibitors N-(3,3-diphenyl-propyl)-nicotinamide and 4-cyano-N-[3-(4-fluorophenyl)-3-(4-methanesulfonyl-phenyl)-propyl]-benzamide, hanging drop vapour diffusion method, 0.005 ml of protein solution containing 12 mg/ml protein in 100 mM sodium phosphate pH 7.4, 50 mM NaCl and 3 mM DTT, is mixed with 0.005 ml of reservoir solution containing 0.2 M lithium sulfate, 36% PEG 3350, and 0.1 M Tris pH 8.4, and 500 nl of 0.006 mM beta-D-hexadecyl maltoside, 4°C, 1 week, X-ray diffraction structure determination and analysis at 1.95-2.5 A resolution
purified recombinant enzyme as apo-crystals of sEH by sitting drop vapor diffusion method, mixing of 15-20 mg/ml protein with reservoir solution containing 0.1 M potassium phosphate, pH 7.5, 0.2 M ammonium dihydrogen phosphate, and 22% w/v PEG 3350, 3-4 days, for inhibitor complexed crystals, soaking in 10 mM ligand in mother liquor for 4 h at room temperature, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement method using PDB ID 1S8O as a search model
purified recombinant enzyme in complex with inhibitors 4-(3-cyclohexylureido)-ethanoic acid, N-cyclohexyl-N'-iodophenyl urea, 4-(3-cyclohexylureido)-butyric acid, 4-(3-cyclohexylureido)-hexanoic acid, and 4-(3-cyclohexylureido)-heptanoic acid, vapour diffusion method, 0.005 ml sitting drops of protein solution containing 12-16 mg/ml enzyme, 3 mM DTT, 0.1 M sodium phosphate, pH 7.4, mixed with 0.005 ml precipitant solution containing 0.1 M Tris, pH 8.4, and 34% w/v PEG3350, and 0.005 ml n-hexadecyl-beta-D-maltoside solution, versus 1 ml reservoir solution, 4°C, 7 days, soaking of crystals in precipitation solution containing 30 mM inhibitor, 3 days, 4°C, cryoprotection by 20% sucrose, X-ray diffraction structure determination and analysis at 2.3-3.0 A resolution
purified recombinant enzyme in complex with N-cyclohexyl-N'-(iodophenyl)urea, sitting drop vapour diffusion method, 0.005 ml of 12-16 mg/ml protein in 3 mM DTT, 0.1 M sodium phosphate, pH 7.4, is mixed with 0.005 ml precipitation solution containing 0.1 M Tris, pH 9.0, 30% w/v PEG 4000, and 0.2 M Li2SO4, versus 1 ml reservoir of precipitation solution, 4°C, 10 days, soaking of crystals in inhibitor solution and n-hexadecyl-beta-D-maltoside, X-ray diffraction structure determination and analysis at 2.35 A resolution, modeling
sitting drop vapour diffusion method, X-ray crystal structure determined at 2.6 A resolution, structure of the complex with the inhibitor N-cyclohexyl-N-(iodophenyl)urea determine at 2.35 A resolution
using 0.1 M potassium phosphate, pH 7.5, 0.2 M ammonium dihydrogen phosphate, and 22% (w/v) polyethylene glycol PEG3350
wild-type and mutants Y381F, Y465F, Y381F/Y465F. The two active site tyrosine residues act in concert to lower the activation barrier for the alkylation step
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C154Y
D11N
mutant with strongly reduced phosphatase activity of sEH (2fold decrease in Km and 9fold decrease in kcat compared to the wild type enzyme), the N-terminal domain has phosphatase activity, the C-terminal domain has epoxide hydrolase activity
D184A
the mutation results in a complete loss of the phosphatase activity of sEH, the N-terminal domain has phosphatase activity, the C-terminal domain has epoxide hydrolase activity
D184N
the mutation results in a complete loss of the phosphatase activity of sEH, the N-terminal domain has phosphatase activity, the C-terminal domain has epoxide hydrolase activity
D185A
D185N
the mutation reduces Vmax of the enzyme to 35% while leaving the Km unchanged, the N-terminal domain has phosphatase activity, the C-terminal domain has epoxide hydrolase activity
D335S
site-directed mutagensis, the mutant lacks epoxide hydrolase activity. The mutant looses the effects of wild-type sEH on cell growth
D9A
D9N
the mutation results in a complete loss of the phosphatase activity of sEH, the N-terminal domain has phosphatase activity, the C-terminal domain has epoxide hydrolase activity
E470G
a naturally occuring polymorphism, the substitutions results in an enzyme with increased epoxide hydrolase activity, the mutation is associated with with ischemic stroke risk
G860A
the mutation is associated with ischemic stroke risk in a Chinese population showing a protective influence on ischemic stroke
K160A
the mutation results in a complete loss of the phosphatase activity of sEH, the N-terminal domain has phosphatase activity, the C-terminal domain has epoxide hydrolase activity
K160N
the mutation results in a complete loss of the phosphatase activity of sEH, the N-terminal domain has phosphatase activity, the C-terminal domain has epoxide hydrolase activity
K160R
the mutation results in a complete loss of the phosphatase activity of sEH, the N-terminal domain has phosphatase activity, the C-terminal domain has epoxide hydrolase activity
K55R
N123D
the mutation results in a complete loss of the phosphatase activity of sEH, the N-terminal domain has phosphatase activity, the C-terminal domain has epoxide hydrolase activity
N124D
mutant with strongly reduced phosphatase activity of she, the N-terminal domain has phosphatase activity, the C-terminal domain has epoxide hydrolase activity
N189A
the mutation results in a complete loss of the phosphatase activity of sEH, the N-terminal domain has phosphatase activity, the C-terminal domain has epoxide hydrolase activity
N189D
the mutation results in a complete loss of the phosphatase activity of sEH, the N-terminal domain has phosphatase activity, the C-terminal domain has epoxide hydrolase activity
R103C
the mutant has a significantly lower phosphatase activity than wild type
R287Q
S402R
a naturally occuring polymorphism, the substitutions results in an enzyme with reduced epoxide hydrolase activity
T123A
mutant with strongly reduced phosphatase activity of she, the N-terminal domain has phosphatase activity, the C-terminal domain has epoxide hydrolase activity
T123N
mutant with strongly reduced phosphatase activity of sEH, the N-terminal domain has phosphatase activity, the C-terminal domain has epoxide hydrolase activity
Y381F
crystallization data, optimized transition state distances. Stronger preference for attack at the benzylic position than mutant Y465F
Y465F
crystallization data, optimized transition state distances. Stronger preference for attack at the terminal position than mutant Y381F
C154Y
-
site-directed mutagenesis, the mutant shows a hydrolase/phosphatase ratio of 2.2, compared to the wild-type ratio of 1.0
D335S
-
hydrolase knock-out construct, the mutant enzyme displays only phosphatase activity
D9A
-
phosphatase knock-out construct, the mutant enzyme displays only hydrolase activity
D9A/D335S
-
sEH protein with mutated phosphatase and hydrolase active sites, the mutant is inactive
E470G
-
site-directed mutagenesis, the mutant shows a hydrolase/phosphatase ratio of 0.9, compared to the wild-type ratio of 1.0
K55R
R103C
-
site-directed mutagenesis, the mutant shows a hydrolase/phosphatase ratio of 1.3, compared to the wild-type ratio of 1.0
R103C/R287Q
-
site-directed mutagenesis, the mutant shows a hydrolase/phosphatase ratio of 1.2, compared to the wild-type ratio of 1.0
R287E
-
naturally occuring mutation of gene EPXH2 leads to elevated plasma cholesterol and triglycerides
R287Q
V422A
-
site-directed mutagenesis, the mutant shows a hydrolase/phosphatase ratio of 0.8, compared to the wild-type ratio of 1.0
Y465F
-
site-directed mutagenesis, mutant enzyme shows phosphatase, but no epoxide hydrolase activity
additional information
C154Y
a naturally occuring polymorphism, the substitutions results in an enzyme with increased epoxide hydrolase activity, the mutation is associated with with ischemic stroke risk
C154Y
the mutant has a significantly higher phosphatase activity than wild type
D185A
the mutation leads to a completely inactive sEH phosphatase, the N-terminal domain has phosphatase activity, the C-terminal domain has epoxide hydrolase activity
D185A
the mutation results in a complete loss of the phosphatase activity of sEH, the N-terminal domain has phosphatase activity, the C-terminal domain has epoxide hydrolase activity
D9A
the mutation results in a complete loss of the phosphatase activity of sEH, the N-terminal domain has phosphatase activity, the C-terminal domain has epoxide hydrolase activity
D9A
site-directed mutagensis, the mutant lacks phosphatase activity. The mutant looses the effects of wild-type sEH on cell growth
K55R
a naturally occuring polymorphism, the substitutions results in an enzyme with increased epoxide hydrolase activity, the mutation is associated with with ischemic stroke risk
K55R
naturally occuring polymorphism, rs41507953, the mutation is not associated with restenosis after percutaneous coronary intervention, with incidence of coronary heart disease, or with an increased risk of hypertension and therefore, can not serve as a predictor for risk of coronary heart disease or restenosis after percutaneous coronary intervention
K55R
the mutant has a significantly higher phosphatase activity than wild type
K55R
the mutant has reduced phosphatase activity compared to the wild type. The mutant is associated with the risk of developing coronary heart disease in Caucasians, but not African Americans
R287Q
a naturally occuring polymorphism, the substitutions results in an enzyme with reduced epoxide hydrolase activity
R287Q
the mutant has decreased epoxide hydrolase and phosphatase activity compared to the wild type. The mutant is associated with lower vascular resistance in response to bradykinin in black, but not white Americans
R287Q
the mutation affects enzyme activity through reducing formation of a catalytically active dimer. The mutant has a significantly lower phosphatase activity than wild type
K55R
-
site-directed mutagenesis, the mutant shows a hydrolase/phosphatase ratio of 1.9, compared to the wild-type ratio of 1.0
K55R
-
the sEH variant K55R has increased epoxide hydrolase activity and is associated with coronary artery disease
R287Q
-
naturally occuring mutation of gene EPXH2 leads to elevated risk of coronary artery calcification found in African Americans
R287Q
-
site-directed mutagenesis, the mutant shows the same hydrolase/phosphatase ratio of 1.0 as the wild-type, but reduced stability at 37°C
R287Q
-
the mutation reduces the activity of sEH, there is an association with increased risk for ischemic stroke for the 287Q allele
R287Q
-
the polymorphism is associated with carotid artery calcified plaque in European American families
R287Q
-
the R287Q mutation results in sEH protein with reduced stability and reduced epoxide hydrolase activity, as well as decreased ability of homodimer formation
additional information
gene EPHX2 contains several naturally occuring polymorphisms within study populations, some of which resulted in non-synonymous amino acid substitutions
additional information
knockdown of sEH in He-p3B cells induces the vascular endothelial growth factor, VEGF, mRNA and cell growth, both of which are suppressed by overexpression of sEH in transfected male BALB/c mice
additional information
-
knockdown of sEH in He-p3B cells induces the vascular endothelial growth factor, VEGF, mRNA and cell growth, both of which are suppressed by overexpression of sEH in transfected male BALB/c mice
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Ni-NTA column chromatography, Q-Sepharose column chromatography, and Superdex 200 gel filtration
recombinant C-terminally His6-tagged full-length enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, followed by gel filtration
recombinant enzyme and C-terminal domain from Escherichia coli by nickel or benzylthio affinity chromatography and gel filtration
recombinant enzyme from insect cells in several steps including a final gel filtration step
recombinant His-tagged sEH from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant soluble epoxide hydrolase (sEH) from insect cells by affinity chromatography
2 cytosolic enzyme forms: 1. cEHTSO, epoxide hydrolase with diagnostic substrate specificity for trans-stilbene oxide and 2. cEHCSO, epoxide hydrolase with diagnostic substrate specificity for cis-stilbene oxide
-
425fold from liver cytosol to homogeneity by ammonium sulfate fractionation, cellulose resin, hydroxylapaptite, and ion exchange chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21-AI by nickel affinity chromatography, recombinant strep-tagged wild-type enzyme from Escherichia coli strain XL1-Blue by streptavidin affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Sf21 insect cells by nickel affinity chromatography
-
recombinant wild-type and mutant enzymes from insect cells by affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene EPHX2, recombinant expression of C-terminally His6-tagged full-length enzyme in Escherichia coli strain BL21(DE3)
recombinant expression of human soluble epoxide hydrolase (sEH) in insect cells via baculovirus transfection system
recombinant expression of soluble full-length enzyme in HEK293-F cells via baculovirus transfection system, recombinant expression of the C-terminal domain in Escherichia coli strain Ros2(DE3) and of N-terminally His-tagged full-length enzyme in Escherichia coli strain DH5alpha C2987, method optimization
sEH cloning from liver, expression of N-terminal His-tagged sEH in Escherichia coli strain BL21(DE3) by auto-induction, subcloning in Escherichia coli strain DH5alpha, method development, overview. Expression of sEH in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system, Method comparisons, overview
sEH expression in HEK-293 cells under the control of the cytomegalo virus promoter, tissue expression analysis by real-time quantitative reverse transcription PCR
expression of His-tagged wild-type and mutant enzymes from cDNA in Escherichia coli strain BL21-AI, expression of strep-tagged enzyme from full-length gene in Escherichia coli strain XL1-Blue
-
expression of wild-type and mutant enzymes in insect cells using the baculovirus infection system
-
gene EPHX2, expression of His-tagged wild-type and mutant enzymes in Spodoptera frugiperda Sf21 cells using the baculovirus infection system
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
homocysteine significantly upregulates enzyme mRNA expression. PPARgamma activation is linked to enzyme expression in human endothelial cells. Angiotensin-II treatment of HUVECs results in an over 2fold increase in mRNA expression
there is a significant reduction in protein expression in renal and liver malignant neoplasms compared to healthy tissue
high glucose and high concentration of reactive oxygen species suppresses sEH mRNA and protein expression in Hep-3B cells. Inhibition of NADPH oxidase inhibits the decrease in sEH by high glucose and the addition of hydrogen peroxide to Hep3B cells suppresses the expression of sEH
-
pharmacological induction of sEH by exposure to peroxisome-proliferating activated receptor alpha ligands like clofibrate, tiadenol, or acetylsalicylic acid
-
relative expression of sEH is lower at both the mRNAand protein levels in HepG2 cells than in other cells with the same amount of total RNA or protein loaded. Transcription factor SP-1 is involved in the decrease in the transcription of sEH as a result of DNA methylation in HepG2 cells, which might contribute to epigenetic mechanism-induced carcinogenesis in hepatocytes
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
medicine
pharmacology
the enzyme is a promising therapeutic strategy for cardiovascular disease
analysis
-
development of a high-throughput screen assay for soluble epoxide hydrolase inhibition using (3-phenyl-oxiranyl)-acetic acid cyano-(6-methoxy-naphthalen-2-yl)-methyl ester as a substrate. Assay is accurate and precise
medicine
pharmacology
additional information
-
sEH may have tissue- or cell-type-specific functionality
drug development
sEH is a target for drug design, since inhibition of sEH leads to an increase in circulating levels of epoxyeicosatrienoic acids, resulting in the potentiation of their in vivo pharmacological properties
drug development
soluble epoxide hydrolase (sEH) is a potential target for the treatment of inflammation and hypertension
medicine
sEH is a potential therapeutic target in the treatment of ischemic stroke. Treatment of acute ischemic stroke with sEH inhibition, overview
medicine
because of its central physiological role in disease states such as cardiac hypertrophy, diabetes, hypertension, and pain, the enzym is used as a therapeutic target
medicine
-
the enzyme is a target for regulation of blood pressure, and inhibition of inflammation, atherosclerosis, kidney failure, and cancer progression
medicine
-
the enzyme is a therapeutic target in therapeutic intervention in renal hydrodynamic regulation and blood pressure control
medicine
-
kinetic analysis of the effects of human enzyme polymorphisms on the N-terminal phosphatase activity of soluble epoxide hydrolase activity
medicine
-
semi-quantitative evaluation of staining intensity of soluble epoxide hydrolase and several cytochromes in different malignant tissues. Soluble epoxide hydrolase expression in renal and hepatic malignant neoplasms and surrounding non-malignant tissues is significantly decreased, whereas expression is increased in seminoma
medicine
-
genetic variation in or near the EPHX2 gene contributes to the risk of ischemic stroke
medicine
-
sEH inhibitors may be useful in the treatment of patients with atherosclerotic cardiovascular disease
medicine
-
sEH is a target for the treatment of hypertension and vascular inflammation
medicine
-
sEH is a target for the treatment of hypertension, inflammatory diseases, pain, diabetes, and stroke
medicine
-
soluble epoxide hydrolase is a susceptibility factor for heart failure, EPHX2 mRNA expression is down-regulated in individuals with heart failure
medicine
-
the presence of the rs1042032 variant allele (polymorphism of 3'-untranslated region A/G) in EPHX2 is associated with a protective role for allograft function
medicine
-
sEH enzyme gains considerable attention as a therapeutic target for cardiovascular diseases
medicine
-
relative expression of sEH is lower at both the mRNAand protein levels in HepG2 cells than in other cells with the same amount of total RNA or protein loaded. Transcription factor SP-1 is involved in the decrease in the transcription of sEH as a result of DNA methylation in HepG2 cells, which might contribute to epigenetic mechanism-induced carcinogenesis in hepatocytes
medicine
-
upregulation of the enzyme in proximal tubular cells in chronic proteinuric kidney diseases may mediate proteinuria-induced renal damage, while enzyme inhibition by increasing renal eicosanoid levels can prevent the progression of chronic proteinuric kidney diseases
pharmacology
-
the enzyme is a target for inhibition in therapy of disorders resulting from hypertension and vascular inflammation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wixtrom, R.N.; Hammock, B.D.
Membrane-bound and soluble-fraction epoxide hydrolases
Biochem. Pharmacol. Toxicol.
1
1-93
1985
Oryctolagus cuniculus, Homo sapiens, Macaca mulatta, Mus musculus, Rattus norvegicus
-
Wang, P.; Meijer, J.; Guengerich, F.P.
Purification of human liver cytosolic epoxide hydrolase and comparison to the microsomal enzyme
Biochemistry
21
5769-5776
1982
Homo sapiens, Rattus norvegicus
Meijer, J.; DePierre, J.W.
Cytosolic epoxide hydrolase
Chem. Biol. Interact.
64
207-249
1988
Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus
Schladt, L.; Thomas, H.; Hartmann, R.; Oesch, F.
Human liver cytosolic epoxide hydrolases
Eur. J. Biochem.
176
715-723
1988
Homo sapiens
Dietze, E.C.; Magdalou, J.; Hammock, B.D.
Human and murine cytosolic epoxide hydrolase: Physical and structural properties
Int. J. Biochem.
22
461-470
1990
Homo sapiens, Mus musculus
Morisseau, C.; Beetham, J.K.; Pinot, F.; Debernard, S.; Newman, J.W.; Hammock, B.D.
Cress and potato soluble epoxide hydrolases: purification, biochemical characterization, and comparison to mammalian enzymes
Arch. Biochem. Biophys.
378
321-332
2000
Arabidopsis thaliana, cress, Homo sapiens, Mus musculus, Rattus norvegicus, Solanum tuberosum
Thomas, H.; Schladt, L.; Doehmer, J.; Knehr, M.; Oesch, F.
Rat and human liver cytosolic epoxide hydrolases: evidence for multiple forms at the level of protein and mRNA
Environ. Health Perspect.
88
49-55
1990
Homo sapiens, Rattus norvegicus
Gomez, G.A.; Morisseau, C.; Hammock, B.D.; Christianson, D.W.
Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis
Biochemistry
43
4716-4723
2004
Homo sapiens (P34913), Homo sapiens
Newman, J.W.; Morisseau, C.; Harris, T.R.; Hammock, B.D.
The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity
Proc. Natl. Acad. Sci. USA
100
1558-1563
2003
Homo sapiens
Yu, Z.; Davis, B.B.; Morisseau, C.; Hammock, B.D.; Olson, J.L.; Kroetz, D.L.; Weiss, R.H.
Vascular localization of soluble epoxide hydrolase in the human kidney
Am. J. Physiol.
286
F720-726
2004
Homo sapiens
Jones, P.D.; Wolf, N.M.; Morisseau, C.; Whetstone, P.; Hock, B.; Hammock, B.D.
Fluorescent substrates for soluble epoxide hydrolase and application to inhibition studies
Anal. Biochem.
343
66-75
2005
Homo sapiens, Mus musculus
Morisseau, C.; Hammock, B.D.
Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles
Annu. Rev. Pharmacol. Toxicol.
45
311-333
2005
Homo sapiens, Mus musculus, Rattus norvegicus
Morisseau, C.; Du, G.; Newman, J.W.; Hammock, B.D.
Mechanism of mammalian soluble epoxide hydrolase inhibition by chalcone oxide derivatives
Arch. Biochem. Biophys.
356
214-228
1998
Homo sapiens, Mus musculus
Srivastava, P.K.; Sharma, V.K.; Kalonia, D.S.; Grant, D.F.
Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quarternary structure
Arch. Biochem. Biophys.
427
164-169
2004
Homo sapiens
Enayetallah, A.E.; Grant, D.F.
Effects of human soluble epoxide hydrolase polymorphisms on isoprenoid phosphate hydrolysis
Biochem. Biophys. Res. Commun.
341
254-260
2006
Homo sapiens
Tran, K.L.; Aronov, P.A.; Tanaka, H.; Newman, J.W.; Hammock, B.D.; Morisseau, C.
Lipid sulfates and sulfonates are allosteric competitive inhibitors of the N-terminal phosphatase activity of the mammalian soluble poxide hydrolase
Biochemistry
44
12179-12187
2005
Homo sapiens
Dietze, E.C.; Stephens, J.; Magdalou, J.; Bender, D.M.; Moyer, M.; Fowler, B.; Hammock, B.D.
Inhibition of human and murine cytosolic epoxide hydrolase by group-selective reagents
Comp. Biochem. Physiol. B
104
299-308
1993
Homo sapiens, Mus musculus
Enayetallah, A.E.; French, R.A.; Barber, M.; Grant, D.F.
Cell-specific subcellular localization of soluble epoxide hydrolase in human tissues
J. Histochem. Cytochem.
54
329-335
2006
Homo sapiens
McElroy, N.R.; Jurs, P.C.
QSAR and classification of murine and human soluble epoxide hydrolase inhibition by urea-like compounds
J. Med. Chem.
46
1066-1080
2003
Homo sapiens, Mus musculus
Cronin, A.; Mowbray, S.; Duerk, H.; Homburg, S.; Fleming, I.; Fisslthaler, B.; Oesch, F.; Arand, M.
The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase
Proc. Natl. Acad. Sci. USA
100
1552-1557
2003
Homo sapiens, Rattus norvegicus, Mus musculus (P34914)
Newman, J.W.; Morisseau, C.; Hammock, B.D.
Epoxide hydrolases: their roles and interactions with lipid metabolism
Prog. Lipid Res.
44
1-51
2005
Ananas comosus, Apium graveolens, Arabidopsis thaliana, Papio sp., Brassica napus, Ricinus communis, Cavia porcellus, Oryctolagus cuniculus, Equus caballus, Euphorbia lagascae, Glycine max, Homo sapiens, Macaca mulatta, Oryzias latipes, Mesocricetus auratus, Nicotiana tabacum, Oncorhynchus mykiss, Oryza sativa, Rattus norvegicus, Solanum tuberosum, Spinacia oleracea, Sus scrofa, Triticum aestivum, Vicia sativa, Zea mays, Citrus jambhiri, Malus pumila, Pimephales promelas, Stenotomus chrysops, Mus musculus (P34914)
Gomez, G.A.; Morisseau, C.; Hammock, B.D.; Christianson, D.W.
Human soluble epoxide hydrolase: structural basis of inhibition by 4-(3-cyclohexylureido)-carboxylic acids
Protein Sci.
15
58-64
2006
Homo sapiens (P34913), Homo sapiens
Draper, A.J.; Hammock, B.D.
Inhibition of soluble and microsomal epoxide hydrolase by zinc and other metals
Toxicol. Sci.
52
26-32
1999
Homo sapiens, Mus musculus, Rattus norvegicus, Solanum tuberosum
Enayetallah, A.E.; French, R.A.; Grant, D.F.
Distribution of soluble epoxide hydrolase, cytochrome P450 2C8, 2C9, and 2J2 in human malignant neoplasms
J. Mol. Histol.
37
133-141
2006
Homo sapiens
Wolf, N.M.; Morisseau, C.; Jones, P.D.; Hock, B.; Hammock, B.D.
Development of a high-throughput screen for soluble epoxide hydrolase inhibition
Anal. Biochem.
355
71-80
2006
Homo sapiens
Kim, I.H.; Nishi, K.; Tsai, H.J.; Bradford, T.; Koda, Y.; Watanabe, T.; Morisseau, C.; Blanchfield, J.; Toth, I.; Hammock, B.D.
Design of bioavailable derivatives of 12-(3-adamantan-1-yl-ureido)dodecanoic acid, a potent inhibitor of the soluble epoxide hydrolase
Bioorg. Med. Chem.
15
312-323
2007
Homo sapiens
Jones, P.D.; Tsai, H.J.; Do, Z.N.; Morisseau, C.; Hammock, B.D.
Synthesis and SAR of conformationally restricted inhibitors of soluble epoxide hydrolase
Bioorg. Med. Chem. Lett.
16
5212-5216
2006
Homo sapiens (P34913), Homo sapiens
Sura, P.; Sura, R.; Enayetallah, A.E.; Grant, D.F.
Distribution and expression of soluble epoxide hydrolase in human brain
J. Histochem. Cytochem.
56
551-559
2008
Homo sapiens
Hwang, S.H.; Tsai, H.J.; Liu, J.Y.; Morisseau, C.; Hammock, B.D.
Orally bioavailable potent soluble epoxide hydrolase inhibitors
J. Med. Chem.
50
3825-3840
2007
Canis lupus, Felis catus, Mesocricetus auratus, Mus musculus, Rattus norvegicus, Homo sapiens (P34913), Homo sapiens
Kim, I.H.; Tsai, H.J.; Nishi, K.; Kasagami, T.; Morisseau, C.; Hammock, B.D.
1,3-disubstituted ureas functionalized with ether groups are potent inhibitors of the soluble epoxide hydrolase with improved pharmacokinetic properties
J. Med. Chem.
50
5217-5226
2007
Homo sapiens
Hopmann, K.H.; Himo, F.
Insights into the reaction mechanism of soluble epoxide hydrolase from theoretical active site mutants
J. Phys. Chem. B
110
21299-21310
2006
Homo sapiens (P34913), Homo sapiens
Ai, D.; Fu, Y.; Guo, D.; Tanaka, H.; Wang, N.; Tang, C.; Hammock, B.D.; Shyy, J.Y.; Zhu, Y.
Angiotensin II up-regulates soluble epoxide hydrolase in vascular endothelium in vitro and in vivo
Proc. Natl. Acad. Sci. USA
104
9018-9023
2007
Bos taurus, Homo sapiens, Rattus norvegicus
Decker, M.; Arand, M.; Cronin, A.
Mammalian epoxide hydrolases in xenobiotic metabolism and signalling
Arch. Toxicol.
83
297-318
2009
Homo sapiens, Mus musculus (P34914)
Anandan, S.K.; Do, Z.N.; Webb, H.K.; Patel, D.V.; Gless, R.D.
Non-urea functionality as the primary pharmacophore in soluble epoxide hydrolase inhibitors
Bioorg. Med. Chem. Lett.
19
1066-1070
2009
Homo sapiens
Xie, Y.; Liu, Y.; Gong, G.; Smith, D.H.; Yan, F.; Rinderspacher, A.; Feng, Y.; Zhu, Z.; Li, X.; Deng, S.X.; Branden, L.; Vidovi?, D.; Chung, C.; Schuerer, S.; Morisseau, C.; Hammock, B.D.; Landry, D.W.
Discovery of potent non-urea inhibitors of soluble epoxide hydrolase
Bioorg. Med. Chem. Lett.
19
2354-2359
2009
Homo sapiens
Liu, J.Y.; Tsai, H.J.; Hwang, S.H.; Jones, P.D.; Morisseau, C.; Hammock, B.D.
Pharmacokinetic optimization of four soluble epoxide hydrolase inhibitors for use in a murine model of inflammation
Br. J. Pharmacol.
156
284-296
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Burdon, K.P.; Lehtinen, A.B.; Langefeld, C.D.; Carr, J.J.; Rich, S.S.; Freedman, B.I.; Herrington, D.; Bowden, D.W.
Genetic analysis of the soluble epoxide hydrolase gene, EPHX2, in subclinical cardiovascular disease in the Diabetes Heart Study
Diab. Vasc. Dis. Res.
5
128-134
2008
Homo sapiens
EnayetAllah, A.E.; Luria, A.; Luo, B.; Tsai, H.J.; Sura, P.; Hammock, B.D.; Grant, D.F.
Opposite regulation of cholesterol levels by the phosphatase and hydrolase domains of soluble epoxide hydrolase
J. Biol. Chem.
283
36592-36598
2008
Homo sapiens, Mus musculus
Ulu, A.; Davis, B.B.; Tsai, H.J.; Kim, I.H.; Morisseau, C.; Inceoglu, B.; Fiehn, O.; Hammock, B.D.; Weiss, R.H.
Soluble epoxide hydrolase inhibitors reduce the development of atherosclerosis in apolipoprotein e-knockout mouse model
J. Cardiovasc. Pharmacol.
52
314-323
2008
Homo sapiens, Mus musculus
Luo, B.; Norris, C.; Bolstad, E.S.; Knecht, D.A.; Grant, D.F.
Protein quaternary structure and expression levels contribute to peroxisomal-targeting-sequence-1-mediated peroxisomal import of human soluble epoxide hydrolase
J. Mol. Biol.
380
31-41
2008
Homo sapiens (P34913), Homo sapiens
Cronin, A.; Homburg, S.; Duerk, H.; Richter, I.; Adamska, M.; Frere, F.; Arand, M.
Insights into the catalytic mechanism of human sEH phosphatase by site-directed mutagenesis and LC-MS/MS analysis
J. Mol. Biol.
383
627-640
2008
Homo sapiens (P34913), Homo sapiens
Monti, J.; Fischer, J.; Paskas, S.; Heinig, M.; Schulz, H.; Goesele, C.; Heuser, A.; Fischer, R.; Schmidt, C.; Schirdewan, A.; Gross, V.; Hummel, O.; Maatz, H.; Patone, G.; Saar, K.; Vingron, M.; Weldon, S.M.; Lindpaintner, K.; Hammock, B.D.; Rohde, K.; Dietz, R.; Cook, S.A.; Schunck, W.H.; Luft, F.C.; Hub, H.u.b.n.
Soluble epoxide hydrolase is a susceptibility factor for heart failure in a rat model of human disease
Nat. Genet.
40
529-537
2008
Homo sapiens, Rattus norvegicus
Morisseau, C.; Hammock, B.D.
Gerry Brooks and epoxide hydrolases: four decades to a pharmaceutical
Pest Manag. Sci.
64
594-609
2008
Homo sapiens
Zhang, L.; Ding, H.; Yan, J.; Hui, R.; Wang, W.; Kissling, G.E.; Zeldin, D.C.; Wang, D.W.
Genetic variation in cytochrome P450 2J2 and soluble epoxide hydrolase and risk of ischemic stroke in a Chinese population
Pharmacogenet. Genomics
18
45-51
2008
Homo sapiens (P34913), Homo sapiens
Shi, D.H.; Xu, C.; Guo, B.X.; Wang, X.T.; Chen, Y.X.; Tan, R.X.
Inhibition of soluble epoxide hydrolase by extracts derived from inflammation-treating Chinese medicinal herbs
Phytother. Res.
22
1264-1268
2008
Homo sapiens
Gschwendtner, A.; Ripke, S.; Freilinger, T.; Lichtner, P.; Mueller-Myhsok, B.; Wichmann, H.E.; Meitinger, T.; Dichgans, M.
Genetic variation in soluble epoxide hydrolase (EPHX2) is associated with an increased risk of ischemic stroke in white Europeans
Stroke
39
1593-1596
2008
Homo sapiens
Lee, S.H.; Lee, J.; Cha, R.; Park, M.H.; Ha, J.W.; Kim, S.; Kim, Y.S.
Genetic variations in soluble epoxide hydrolase and graft function in kidney transplantation
Transplant. Proc.
40
1353-1356
2008
Homo sapiens
Oguro, A.; Sakamoto, K.; Suzuki, S.; Imaoka, S.
Contribution of hydrolase and phosphatase domains in soluble epoxide hydrolase to vascular endothelial growth factor expression and cell growth
Biol. Pharm. Bull.
32
1962-1967
2009
Homo sapiens (P34913), Homo sapiens
Shen, H.C.; Ding, F.X.; Wang, S.; Xu, S.; Chen, H.S.; Tong, X.; Tong, V.; Mitra, K.; Kumar, S.; Zhang, X.; Chen, Y.; Zhou, G.; Pai, L.Y.; Alonso-Galicia, M.; Chen, X.; Zhang, B.; Tata, J.R.; Berger, J.P.; Colletti, S.L.
Discovery of spirocyclic secondary amine-derived tertiary ureas as highly potent, selective and bioavailable soluble epoxide hydrolase inhibitors
Bioorg. Med. Chem. Lett.
19
3398-3404
2009
Homo sapiens (P34913), Rattus norvegicus (P80299)
Shen, H.C.; Ding, F.X.; Deng, Q.; Xu, S.; Chen, H.S.; Tong, X.; Tong, V.; Zhang, X.; Chen, Y.; Zhou, G.; Pai, L.Y.; Alonso-Galicia, M.; Zhang, B.; Roy, S.; Tata, J.R.; Berger, J.P.; Colletti, S.L.
Discovery of 3,3-disubstituted piperidine-derived trisubstituted ureas as highly potent soluble epoxide hydrolase inhibitors
Bioorg. Med. Chem. Lett.
19
5314-5320
2009
Homo sapiens (P34913), Homo sapiens, Rattus norvegicus (P80299)
Shen, H.C.; Ding, F.X.; Deng, Q.; Xu, S.; Tong, X.; Zhang, X.; Chen, Y.; Zhou, G.; Pai, L.Y.; Alonso-Galicia, M.; Roy, S.; Zhang, B.; Tata, J.R.; Berger, J.P.; Colletti, S.L.
A strategy of employing aminoheterocycles as amide mimics to identify novel, potent and bioavailable soluble epoxide hydrolase inhibitors
Bioorg. Med. Chem. Lett.
19
5716-5721
2009
Homo sapiens (P34913), Homo sapiens
Taylor, S.J.; Soleymanzadeh, F.; Eldrup, A.B.; Farrow, N.A.; Muegge, I.; Kukulka, A.; Kabcenell, A.K.; De Lombaert, S.
Design and synthesis of substituted nicotinamides as inhibitors of soluble epoxide hydrolase
Bioorg. Med. Chem. Lett.
19
5864-5868
2009
Homo sapiens (P34913), Homo sapiens, Rattus norvegicus (P80299)
Kullmann, S.; Binner, P.; Rackebrandt, K.; Huge, A.; Haltern, G.; Lankisch, M.; Fueth, R.; von Hodenberg, E.; Bestehorn, H.P.; Scheffold, T.
Variation in the human soluble epoxide hydrolase gene and risk of restenosis after percutaneous coronary intervention
BMC Cardiovasc. Disord.
9
48
2009
Homo sapiens (P34913), Homo sapiens
Keserue, B.; Barbosa-Sicard, E.; Schermuly, R.T.; Tanaka, H.; Hammock, B.D.; Weissmann, N.; Fisslthaler, B.; Fleming, I.
Hypoxia-induced pulmonary hypertension: comparison of soluble epoxide hydrolase deletion vs. inhibition
Cardiovasc. Res.
85
232-240
2010
Homo sapiens (P34913), Homo sapiens, Mus musculus (P34914), Mus musculus C57BL/6 (P34914)
Qiu, H.; Li, N.; Liu, J.Y.; Harris, T.R.; Hammock, B.D.; Chiamvimonvat, N.
Soluble epoxide hydrolase inhibitors and heart failure
Cardiovasc. Ther.
29
99-111
2011
Homo sapiens, Mus musculus (P34914)
Wang, Y.X.; Ulu, A.; Zhang, L.N.; Hammock, B.
Soluble epoxide hydrolase in atherosclerosis
Curr. Atheroscler. Rep.
12
174-183
2010
Homo sapiens (P34913), Homo sapiens, Mus musculus (P34914), Rattus norvegicus (P80299)
Oguro, A.; Fujita, N.; Imaoka, S.
Regulation of soluble epoxide hydrolase (sEH) in mice with diabetes: high glucose suppresses sEH expression
Drug Metab. Pharmacokinet.
24
438-445
2009
Homo sapiens, Mus musculus (P34914)
Tsai, H.J.; Hwang, S.H.; Morisseau, C.; Yang, J.; Jones, P.D.; Kasagami, T.; Kim, I.H.; Hammock, B.D.
Pharmacokinetic screening of soluble epoxide hydrolase inhibitors in dogs
Eur. J. Pharm. Sci.
40
222-238
2010
Canis lupus familiaris, Homo sapiens (P34913)
Iliff, J.J.; Alkayed, N.J.
Soluble epoxide hydrolase inhibition: targeting multiple mechanisms of ischemic brain injury with a single agent
Future Neurol.
4
179-199
2009
Homo sapiens (P34913), Mus musculus (P34914), Rattus norvegicus (P80299)
Barbosa-Sicard, E.; Froemel, T.; Keserue, B.; Brandes, R.P.; Morisseau, C.; Hammock, B.D.; Braun, T.; Krueger, M.; Fleming, I.
Inhibition of the soluble epoxide hydrolase by tyrosine nitration
J. Biol. Chem.
284
28156-28163
2009
Homo sapiens (P34913), Homo sapiens, Mus musculus (P34914), Mus musculus, Mus musculus C57BL/6 (P34914)
Shen, H.; Ding, F.; Wang, S.; Deng, Q.; Zhang, X.; Chen, Y.; Zhou, G.; Xu, S.; Chen, H.; Tong, X.; Tong, V.; Mitra, K.; Kumar, S.; Tsai, C.; Stevenson, A.; Pai, L.; Alonso-Galicia, M.; Chen, X.; Soisson, S.; Roy, S.; Zhang, B.; Tata, J.; Berger, J.; Colle
Discovery of a highly potent, selective, and bioavailable soluble epoxide hydrolase inhibitor with excellent ex vivo target engagement
J. Med. Chem.
52
5009-5012
2009
Homo sapiens (P34913)
Falck, J.; Kodela, R.; Manne, R.; Atcha, K.; Puli, N.; Dubasi, N.; Manthati, V.; Capdevila, J.; Yi, X.; Goldman, D.; Morisseau, C.; Hammock, B.; Campbell, W.
14,15-Epoxyeicosa-5,8,11-trienoic acid (14,15-EET) surrogates containing epoxide bioisosteres: Influence upon vascular relaxation and soluble epoxide hydrolase inhibition
J. Med. Chem.
52
5069-5075
2009
Bos taurus, Homo sapiens (P34913)
Eldrup, A.B.; Soleymanzadeh, F.; Taylor, S.J.; Muegge, I.; Farrow, N.A.; Joseph, D.; McKellop, K.; Man, C.C.; Kukulka, A.; De Lombaert, S.
Structure-based optimization of arylamides as inhibitors of soluble epoxide hydrolase
J. Med. Chem.
52
5880-5895
2009
Homo sapiens (P34913), Homo sapiens, Rattus norvegicus (P80299)
Deng, Y.; Theken, K.N.; Lee, C.R.
Cytochrome P450 epoxygenases, soluble epoxide hydrolase, and the regulation of cardiovascular inflammation
J. Mol. Cell. Cardiol.
48
331-341
2010
Homo sapiens (P34913), Mus musculus (P34914)
Xie, W.; Tang, X.; Lu, Q.; Ames, R.S.; Ratcliffe, S.J.; Li, H.
Development of a high throughput cell-based assay for soluble epoxide hydrolase using BacMam technology
Mol. Biotechnol.
45
207-217
2010
Homo sapiens (P34913)
Liu, J.Y.; Park, S.H.; Morisseau, C.; Hwang, S.H.; Hammock, B.D.; Weiss, R.H.
Sorafenib has soluble epoxide hydrolase inhibitory activity, which contributes to its effect profile in vivo
Mol. Cancer Ther.
8
2193-2203
2009
Homo sapiens
Imig, J.D.; Hammock, B.D.
Soluble epoxide hydrolase as a therapeutic target for cardiovascular diseases
Nat. Rev. Drug Discov.
8
794-805
2009
Homo sapiens (P34913)
Nishi, K.; Kim, I.H.; Ma, S.J.
Expression of the human soluble epoxide hydrolase in Escherichia coli by auto-induction for the study of high-throughput inhibition assays
Protein Expr. Purif.
69
34-38
2010
Homo sapiens (P34913), Homo sapiens
Zhang, D.; Ai, D.; Tanaka, H.; Hammock, B.D.; Zhu, Y.
DNA methylation of the promoter of soluble epoxide hydrolase silences its expression by an SP-1-dependent mechanism
Biochim. Biophys. Acta
1799
659-667
2010
Homo sapiens
Cronin, A.; Decker, M.; Arand, M.
Mammalian soluble epoxide hydrolase is identical to liver hepoxilin hydrolase
J. Lipid Res.
52
712-719
2011
Homo sapiens, Mus musculus, Rattus norvegicus
Xing, L.; McDonald, J.J.; Kolodziej, S.A.; Kurumbail, R.G.; Williams, J.M.; Warren, C.J.; ONeal, J.M.; Skepner, J.E.; Roberds, S.L.
Discovery of potent inhibitors of soluble epoxide hydrolase by combinatorial library design and structure-based virtual screening
J. Med. Chem.
54
1211-1222
2011
Homo sapiens (P34913)
Kim, I.H.; Park, Y.K.; Hammock, B.D.; Nishi, K.
Structure-activity relationships of cycloalkylamide derivatives as inhibitors of the soluble epoxide hydrolase
J. Med. Chem.
54
1752-1761
2011
Homo sapiens
Hwang, S.H.; Wagner, K.M.; Morisseau, C.; Liu, J.Y.; Dong, H.; Wecksler, A.T.; Hammock, B.D.
Synthesis and structure-activity relationship studies of urea-containing pyrazoles as dual inhibitors of cyclooxygenase-2 and soluble epoxide hydrolase
J. Med. Chem.
54
3037-3050
2011
Mus musculus, Homo sapiens (P34913)
Wang, Q.; Pang, W.; Cui, Z.; Shi, J.; Liu, Y.; Liu, B.; Zhou, Y.; Guan, Y.; Hammock, B.D.; Wang, Y.; Zhu, Y.
Upregulation of soluble epoxide hydrolase in proximal tubular cells mediated proteinuria-induced renal damage
Am. J. Physiol. Renal Physiol.
304
F168-F176
2013
Homo sapiens
Pecic, S.; Pakhomova, S.; Newcomer, M.E.; Morisseau, C.; Hammock, B.D.; Zhu, Z.; Rinderspacher, A.; Deng, S.X.
Synthesis and structure-activity relationship of piperidine-derived non-urea soluble epoxide hydrolase inhibitors
Bioorg. Med. Chem. Lett.
23
417-421
2013
Homo sapiens
Burmistrov, V.; Morisseau, C.; Lee, K.S.; Shihadih, D.S.; Harris, T.R.; Butov, G.M.; Hammock, B.D.
Symmetric adamantyl-diureas as soluble epoxide hydrolase inhibitors
Bioorg. Med. Chem. Lett.
24
2193-2197
2014
Homo sapiens
Kim, I.H.; Lee, I.H.; Nishiwaki, H.; Hammock, B.D.; Nishi, K.
Structure-activity relationships of substituted oxyoxalamides as inhibitors of the human soluble epoxide hydrolase
Bioorg. Med. Chem.
22
1163-1175
2014
Homo sapiens (P34913), Homo sapiens
Amano, Y.; Yamaguchi, T.; Tanabe, E.
Structural insights into binding of inhibitors to soluble epoxide hydrolase gained by fragment screening and X-ray crystallography
Bioorg. Med. Chem.
22
2427-2434
2014
Homo sapiens (P34913)
Harris, T.R.; Hammock, B.D.
Soluble epoxide hydrolase: gene structure, expression and deletion
Gene
526
61-74
2013
Homo sapiens (P34913), Homo sapiens
Nelson, J.W.; Subrahmanyan, R.M.; Summers, S.A.; Xiao, X.; Alkayed, N.J.
Soluble epoxide hydrolase dimerization is required for hydrolase activity
J. Biol. Chem.
288
7697-7703
2013
Homo sapiens (P34913), Homo sapiens
Chen, H.; Zhang, Y.; Ye, C.; Feng, T.T.; Han, J.G.
Insight into the binding modes and inhibition mechanisms of adamantyl-based 1,3-disubstituted urea inhibitors in the active site of the human soluble epoxide hydrolase
J. Biomol. Struct. Dyn.
32
1231-1247
2014
Homo sapiens
Morisseau, C.; Wecksler, A.T.; Deng, C.; Dong, H.; Yang, J.; Lee, K.S.; Kodani, S.D.; Hammock, B.D.
Effect of soluble epoxide hydrolase polymorphism on substrate and inhibitor selectivity and dimer formation
J. Lipid Res.
55
1131-1138
2014
Homo sapiens (P34913), Homo sapiens
la Buscato, E.; Bloecher, R.; Lamers, C.; Klingler, F.M.; Hahn, S.; Steinhilber, D.; Schubert-Zsilavecz, M.; Proschak, E.
Design and synthesis of dual modulators of soluble epoxide hydrolase and peroxisome proliferator-activated receptors
J. Med. Chem.
55
10771-10775
2012
Homo sapiens
Lee, K.S.; Liu, J.Y.; Wagner, K.M.; Pakhomova, S.; Dong, H.; Morisseau, C.; Fu, S.H.; Yang, J.; Wang, P.; Ulu, A.; Mate, C.A.; Nguyen, L.V.; Hwang, S.H.; Edin, M.L.; Mara, A.A.; Wulff, H.; Newcomer, M.E.; Zeldin, D.C.; Hammock, B.D.
Optimized inhibitors of soluble epoxide hydrolase improve in vitro target residence time and in vivo efficacy
J. Med. Chem.
57
7016-7030
2014
Rattus norvegicus, Homo sapiens (P34913), Homo sapiens
Zhang, W.; Davis, C.M.; Edin, M.L.; Lee, C.R.; Zeldin, D.C.; Alkayed, N.J.
Role of endothelial soluble epoxide hydrolase in cerebrovascular function and ischemic injury
PLoS ONE
8
e61244
2013
Homo sapiens
Lee, K.S.; Henriksen, N.M.; Ng, C.J.; Yang, J.; Jia, W.; Morisseau, C.; Andaya, A.; Gilson, M.K.; Hammock, B.D.
Probing the orientation of inhibitor and epoxy-eicosatrienoic acid binding in the active site of soluble epoxide hydrolase
Arch. Biochem. Biophys.
613
1-11
2017
Homo sapiens (P34913)
Liu, J.Y.; Tsai, H.J.; Morisseau, C.; Lango, J.; Hwang, S.H.; Watanabe, T.; Kim, I.H.; Hammock, B.D.
In vitro and in vivo metabolism of N-adamantyl substituted urea-based soluble epoxide hydrolase inhibitors
Biochem. Pharmacol.
98
718-731
2015
Homo sapiens (P34913), Homo sapiens, Mus musculus (P34914), Rattus norvegicus (P80299), Mus musculus C57BL/6 (P34914), Rattus norvegicus Sprague Dawley (P80299)
Burmistrov, V.; Morisseau, C.; Harris, T.R.; Butov, G.; Hammock, B.D.
Effects of adamantane alterations on soluble epoxide hydrolase inhibition potency, physical properties and metabolic stability
Bioorg. Chem.
76
510-527
2018
Homo sapiens (P34913), Homo sapiens, Mus musculus (P34914), Mus musculus, Rattus norvegicus (P80299)
Amano, Y.; Tanabe, E.; Yamaguchi, T.
Identification of N-ethylmethylamine as a novel scaffold for inhibitors of soluble epoxide hydrolase by crystallographic fragment screening
Bioorg. Med. Chem.
23
2310-2317
2015
Homo sapiens (P34913)
Takai, K.; Chiyo, N.; Nakajima, T.; Nariai, T.; Ishikawa, C.; Nakatani, S.; Ikeno, A.; Yamamoto, S.; Sone, T.
Three-dimensional rational approach to the discovery of potent substituted cyclopropyl urea soluble epoxide hydrolase inhibitors
Bioorg. Med. Chem. Lett.
25
1705-1708
2015
Homo sapiens (P34913), Homo sapiens, Rattus norvegicus (P80299)
Gurung, A.B.; Mayengbam, B.; Bhattacharjee, A.
Discovery of novel drug candidates for inhibition of soluble epoxide hydrolase of arachidonic acid cascade pathway implicated in atherosclerosis
Comput. Biol. Chem.
74
1-11
2018
Homo sapiens (P34913)
Kim, J.H.; Cho, I.S.; Ryu, J.; Lee, J.S.; Kang, J.S.; Kang, S.Y.; Kim, Y.H.
In vitro and in silico investigation of anthocyanin derivatives as soluble epoxide hydrolase inhibitors
Int. J. Biol. Macromol.
112
961-967
2018
Homo sapiens (P34913)
Liu, Z.B.; Sun, C.P.; Xu, J.X.; Morisseau, C.; Hammock, B.D.; Qiu, F.
Phytochemical constituents from Scutellaria baicalensis in soluble epoxide hydrolase inhibition kinetics and interaction mechanism merged with simulations
Int. J. Biol. Macromol.
133
1187-1193
2019
Homo sapiens (P34913)
Yamanashi, H.; Boeglin, W.E.; Morisseau, C.; Davis, R.W.; Sulikowski, G.A.; Hammock, B.D.; Brash, A.R.
Catalytic activities of mammalian epoxide hydrolases with cis and trans fatty acid epoxides relevant to skin barrier function
J. Lipid Res.
59
684-695
2018
Homo sapiens (P34913), Homo sapiens (Q9H6B9), Homo sapiens, Mus musculus (Q3V1F8), Mus musculus
Bloecher, R.; Lamers, C.; Wittmann, S.K.; Merk, D.; Hartmann, M.; Weizel, L.; Diehl, O.; Brueggerhoff, A.; Boss, M.; Kaiser, A.; Schader, T.; Goebel, T.; Grundmann, M.; Angioni, C.; Heering, J.; Geisslinger, G.; Wurglics, M.; Kostenis, E.; Bruene, B.; Steinhilber, D.; Schubert-Zsilavecz, M.; Kahn, K.a.h.n.t.
N-Benzylbenzamides a novel merged scaffold for orally available dual soluble epoxide hydrolase/peroxisome proliferator-activated receptor gamma modulators
J. Med. Chem.
59
61-81
2016
Homo sapiens (P34913), Homo sapiens
Meirer, K.; Glatzel, D.; Kretschmer, S.; Wittmann, S.K.; Hartmann, M.; Bloecher, R.; Angioni, C.; Geisslinger, G.; Steinhilber, D.; Hofmann, B.; Fuerst, R.; Proschak, E.
Design, synthesis and cellular characterization of a dual inhibitor of 5-lipoxygenase and soluble epoxide hydrolase
Molecules
22
45-54
2016
Homo sapiens (P34913)
Abis, G.; Charles, R.L.; Eaton, P.; Conte, M.R.
Expression, purification, and characterisation of human soluble epoxide hydrolase (hsEH) and of its functional C-terminal domain
Protein Expr. Purif.
153
105-113
2019
Homo sapiens (P34913), Homo sapiens
Butov, G.; Burmistrov, V.; Danilov, D.
Synthesis and properties of 1-(R-adamant-1-yl)-3-(1-propionylpiperidin-4-yl)ureas and 4-({4-[3-(R-adamant-1-yl)ureido]cyclohexyl}oxy)benzoic acids, efficient target-oriented human soluble epoxide hydrolase inhibitors
Russ. Chem. Bull.
66
1876-1880
2017
Homo sapiens (P34913)
-
Burmistrov, V.; Butov, G.; Karlov, D.; Palyulin, V.; Zefirov, N.; Morisseau, C.; Hammock, B.
Synthesis and properties of diadamantyl-containing symmetric diureas as target-oriented inhibitors of human soluble epoxide hydrolase
Russ. J. Bioorg. Chem.
42
404-414
2016
Homo sapiens (P34913)
-
Butov, G.; Burmistrov, V.; D'yachenko, V.
Synthesis and properties of symmetrical N,N-bis(R-adamantan-1-yl)ureas as target-oriented soluble epoxide hydrolase (sEH) inhibitors
Russ. J. Org. Chem.
53
977-980
2017
Homo sapiens (P34913)
-
Hiesinger, K.; Kramer, J.S.; Beyer, S.; Eckes, T.; Brunst, S.; Flauaus, C.; Wittmann, S.K.; Weizel, L.; Kaiser, A.; Kretschmer, S.B.M.; George, S.; Angioni, C.; Heering, J.; Geisslinger, G.; Schubert-Zsilavecz, M.; Schmidtko, A.; Pogoryelov, D.; Pfeilschifter, J.; Hofmann, B.; Steinhilber, D.; Sch, S.c.h.w.
Design, synthesis, and structure-activity relationship studies of dual inhibitors of soluble epoxide hydrolase and 5-lipoxygenase
J. Med. Chem.
63
11498-11521
2020
Homo sapiens
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