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Information on EC 1.13.11.33 - arachidonate 15-lipoxygenase and Organism(s) Homo sapiens and UniProt Accession P16050

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IUBMB Comments
The product is rapidly reduced to the corresponding 15S-hydroxy compound.
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This record set is specific for:
Homo sapiens
UNIPROT: P16050
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
15-lox, 15-lo-1, 15-lox-2, 15-lox2, arachidonate 15-lipoxygenase, soybean 15-lipoxygenase, 15-lipoxygenase-2, 15lo1, 15-hlo, 15-lipoxygenase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12/15-lipoxygenase
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15-lipoxygenase type 1
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15-lipoxygenase-1
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15-LOX type 1
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arachidonic acid 15-lipoxygenase-1
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12/15 lipoxygenase
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12/15-lipoxygenase
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12/15-LO
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12/15-LOX
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12/15LO
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15(S)-lipoxygenase-1
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15-hLO-1
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15-hLO-2
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15-lipoxygenase
15-lipoxygenase 1
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15-lipoxygenase 2
15-lipoxygenase type 2
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15-lipoxygenase type-1
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15-lipoxygenase-2
15-LO-2
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15-LOX
15-LOX-2
15-LOX-A
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15-LOX2
ALOX15-2
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ALOX15B
arachidonate 15-lipoxygenase-1
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arachidonic acid 15-lipoxygenase
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-
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endothelial 15-lipoxygenase-1
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epidermis-type 15-LOX
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human prostate epithelial 15-lipoxygenase-2
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linoleic acid omega-6-lipoxygenase
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-
-
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LO-1
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omega-6 lipoxygenase
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oxygenase, arachidonate 15-lip-
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-
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reticulocyte 15-LOX
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reticulocyte-type 15-human lipoxygenase
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reticulocyte-type of 15-LOX-1
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additional information
-
cf. EC 1.13.11.12
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
show the reaction diagram
the reaction proceeds via hydrogen abstraction, peroxide cleavage, radical rearrangement, and epoxide formation. To initiate the reaction the ferrous LOX is first activated by peroxide-dependent oxidation to a ferric form. The lipohydroperoxidase activity is initiatedwhen a lipid hydroperoxide (ROOH) is bound at the active site of the enzyme. The enzyme then catalyzes a homolytic cleavage of the hydroperoxy bond, which leads to the formation of an oxygen-centered alkoxy radical, a hydroxyl and oxidizes the ferrous iron to a ferric form. Then the enzyme binds a linoleic acid molecule (or an alterative reductant such as guaiacol) and releases a carbon-centered linoleic radical. This reaction reduces the ferric LOX back to its ferrous form to start the next catalytic cycle. The released radical intermediates may then initiate free radical secondary reactions leading to the formation of mixed oxygenated and non-oxygenated linoleic acid dimer
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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dioxygenation
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
arachidonate:oxygen 15-oxidoreductase
The product is rapidly reduced to the corresponding 15S-hydroxy compound.
CAS REGISTRY NUMBER
COMMENTARY hide
82249-77-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(14S)-hydroperoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid + ?
(13S,14S)-epoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid
show the reaction diagram
-
-
-
?
4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid + O2
(11S)-hydroperoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid + (14S)-hydroperoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid + (17S)-hydroperoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid
show the reaction diagram
-
-
-
?
5S,15S-dihydroperoxyeicosatetraenoic acid + O2
lipoxin B4
show the reaction diagram
-
-
-
?
5S-hydroperoxy-6E,8Z,10E,14Z-eicosatetraenoic acid + O2
5S,12S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid + 5S,15S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
show the reaction diagram
-
-
-
?
5S-hydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid + O2
5S,12S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid + 5S,15S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
show the reaction diagram
-
-
-
?
arachidonate + O2
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
show the reaction diagram
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(12S)-12-hydroperoxyicosa-5,8,11,13-tetraenoate + (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
show the reaction diagram
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
show the reaction diagram
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
-
?
(14S)-hydroperoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid + ?
(13S,14S)-epoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid
show the reaction diagram
-
-
-
?
4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid + O2
(11S)-hydroperoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid + (14S)-hydroperoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid + (17S)-hydroperoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid
show the reaction diagram
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-
-
?
5S-hydroperoxy-6E,8Z,10E,14Z-eicosatetraenoic acid + O2
5S,12S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
show the reaction diagram
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-
-
?
5S-hydroperoxy-6E,8Z,10E,14Z-eicosatetraenoic acid + O2
5S,12S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid + 5S,15S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
show the reaction diagram
-
-
-
?
5S-hydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid + O2
5S,12S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
show the reaction diagram
-
-
-
?
5S-hydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid + O2
5S,15S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
show the reaction diagram
-
-
-
?
arachidonate + O2
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
show the reaction diagram
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-12-hydroperoxyicosa-5,8,11,13-tetraenoate + (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
show the reaction diagram
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
show the reaction diagram
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
show the reaction diagram
arachidonate + O2
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyicosa-6,8,11,14-tetraenoate
show the reaction diagram
-
-
-
-
?
arachidonic acid + O2
(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid
show the reaction diagram
-
-
the mutant enzyme A416G converts arachidonic acid to (11R)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid and (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid in a 1.5:1 ratio
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?
arachidonic acid + O2
15S-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoic acid
show the reaction diagram
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-
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-
?
arachidonic acid + O2
?
show the reaction diagram
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-
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-
?
eicosapentaenoic acid + O2
15-hydroxyeicosapentaenoic acid
show the reaction diagram
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-
-
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
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-
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-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxy-octadeca-9,11-dienoate
show the reaction diagram
linoleic acid + O2
13-hydroperoxy-(9Z,11E)-linoleic acid
show the reaction diagram
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-
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?
linoleic acid + O2
13-hydroxylinoleic acid
show the reaction diagram
linoleic acid + O2
13-S-hydroxyoctadecadienoic acid
show the reaction diagram
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both 15-LOX-1, 15-LOX-2 reacts with linoleic acid poorly
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-
?
linoleic acid + O2
?
show the reaction diagram
lipoic acid + O2
?
show the reaction diagram
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-
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-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
show the reaction diagram
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
show the reaction diagram
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
show the reaction diagram
-
-
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxy-octadeca-9,11-dienoate
show the reaction diagram
-
-
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-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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in the presence of Mg2+, with or without calcium ionophore, the majority of 15-LO-1 is found in the membrane fraction, although significant amounts are also detected in the supernatant fraction
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(3-chlorobenzoyl)-N-(2-chlorophenyl)-1H-pyrazole-3-carboxamide
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1-acetyl-N-(3,4-dichlorophenyl)-1H-pyrazole-3-carboxamide
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1-benzyl-N-(2-chlorophenyl)-1H-pyrazole-3-carboxamide
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1-[(2H-1,3-benzodioxol-5-yl)carbamothioyl]-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
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2-(1H-pyrazol-3-yl)-1,3-benzoxazole
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3-(4-bromophenyl)-6-(4-chlorophenyl)-N-(2,4,4-trimethylpentan-2-yl)imidazo[2,1-b][1,3]thiazol-5-amine
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3-(4-bromophenyl)-6-(4-chlorophenyl)-N-cyclohexylimidazo[2,1-b][1,3]thiazol-5-amine
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3-(4-bromophenyl)-N-cyclohexyl-6-(2-nitrophenyl)imidazo[2,1-b][1,3]thiazol-5-amine
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3-(4-methoxyphenyl)-6-phenyl-N-(2,4,4-trimethylpentan-2-yl)imidazo[2,1-b][1,3]thiazol-5-amine
protective activity of compound 5i against H2O2-induced cell death in differentiated PC12 cells
4,5-dichloro-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
4-(2-benzoylhydrazinyl)benzene-1-sulfonamide
10% inhibition
4-amino-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
-
4-bromo-5-chloro-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
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4-bromo-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
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4-butyl-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
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4-chloro-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
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4-chloro-N-(2-chloro-4-fluorophenyl)-5-(difluoromethyl)-1H-pyrazole-3-carboxamide
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4-chloro-N-(2-chloro-4-fluorophenyl)-5-(trifluoromethyl)-1H-pyrazole-3-carboxamide
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4-chlorophenyl 3-[(2-chlorophenyl)carbamoyl]-1H-pyrazole-1-carboxylate
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4-methyl-2-(4-methylpiperazinyl)pyrimido[4,5-b]benzothiazine
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4-[(E)-benzoyldiazenyl]benzene-1-sulfonamide
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4-[(E)-benzoyldiazenyl]benzonitrile
80% inhibition, competitive
5-(methylamino)-2-(naphthalen-1-yl)-4,5-dihydro-1,3-oxazole-4-carbonitrile
-
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5-amino-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
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5-butyl-N3-(2-chloro-4-fluorophenyl)-N1-hexyl-1H-pyrazole-1,3-dicarboxamide
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5-chloro-2-(1H-pyrazol-3-yl)-1,3-benzoxazole
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5-chloro-N-(2,4-dichlorophenyl)-1H-pyrazole-3-carboxamide
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5-chloro-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
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5-fluoro-2-(1H-pyrazol-3-yl)-1,3-benzoxazole
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5-tert-butyl-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
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6,6a,11,11a-tetrahydro[1]benzothiopyrano[4,3-b]indole
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6-(2-bromophenyl)-N-cyclohexyl-3-phenylimidazo[2,1-b][1,3]thiazol-5-amine
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6-(2-nitrophenyl)-3-phenyl-N-(2,4,4-trimethylpentan-2-yl)imidazo[2,1-b][1,3]thiazol-5-amine
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6-(4-nitrophenyl)-3-phenyl-N-(2,4,4-trimethylpentan-2-yl)imidazo[2,1-b][1,3]thiazol-5-amine
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6-chloro-2-(1H-pyrazol-3-yl)-1,3-benzoxazole
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6-chloro-2-(4,5-dichloro-1H-pyrazol-3-yl)-1,3-benzoxazole
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6-chloro-2-(5-chloro-1H-pyrazol-3-yl)-1,3-benzoxazole
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6-fluoro-2-(1H-pyrazol-3-yl)-1,3-benzoxazole
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adamantyl caffeate
IC50 value of cytotoxicity against PC-3 cells, 24 h, is 0.074 mM
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baicalein
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bornyl vanillate
IC50 value of cytotoxicity against PC-3 cells, 24 h, is 0.401 mM
-
CDC
CAS-No. 132465-11-3
ethyl 6-([3-[(2-chloro-4-fluorophenyl)carbamoyl]-1H-pyrazole-1-carbonyl]amino)hexanoate
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ethyl 6-chloro-3-[(3S)-3-hydroxy-7-methyloctanoyl]-2,3-dihydro-1H-indole-2-carboxylate
-
-
fenchyl caffeate
IC50 value of cytotoxicity against PC-3 cells, 24 h, is 0.089 mM
-
gallic acid
-
N'-(4-bromophenyl)benzohydrazide
28% inhibition
N'-(4-cyanophenyl)benzohydrazide
9% inhibition
N'-(4-methoxyphenyl)benzohydrazide
73% inhibition
N'-(4-methylphenyl)benzohydrazide
93% inhibition, competitive
N'-(4-nitrophenyl)benzohydrazide
17% inhibition
N'-phenylbenzohydrazide
33% inhibition
N-(2,4-dichlorophenyl)-1H-pyrazole-3-carboxamide
N-(2,5-dichlorophenyl)-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-1-(dimethylsulfamoyl)-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-1-(phenylacetyl)-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-1-methyl-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-1-[3-(trifluoromethyl)benzene-1-sulfonyl]-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
N-(2-chloro-4-fluorophenyl)-4,5-bis(trifluoromethyl)-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-4-(trifluoromethyl)-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-4-fluoro-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-4-iodo-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-4-methyl-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-4-methyl-5-(trimethylsilyl)-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-4-nitro-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-4-phenyl-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-4-[(methanesulfonyl)amino]-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-5-(difluoromethyl)-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-5-(trifluoromethyl)-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-5-iodo-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-5-methyl-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-5-nitro-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-5-[(methanesulfonyl)amino]-1H-pyrazole-3-carboxamide
-
N-(2-chlorophenyl)-1H-pyrazole-3-carboxamide
-
N-(2-chlorophenyl)-N-methyl-1H-pyrazole-3-carboxamide
-
N-(3,4-dichlorophenyl)-1H-pyrazole-3-carboxamide
-
N-(4-fluorophenyl)-1H-pyrazole-3-carboxamide
-
N-(5-chloro-1,3-thiazol-2-yl)-1H-pyrazole-3-carboxamide
-
N-(5-chloropyridin-2-yl)-1H-pyrazole-3-carboxamide
-
N-(5-fluoropyridin-2-yl)-1H-pyrazole-3-carboxamide
-
N-(7-fluoroquinolin-3-yl)-1H-pyrazole-3-carboxamide
-
N-(isoquinolin-3-yl)-1H-pyrazole-3-carboxamide
-
N-(pyridin-2-yl)-1H-pyrazole-3-carboxamide
-
N-(pyridin-3-yl)-1H-pyrazole-3-carboxamide
-
N-(pyridin-4-yl)-1H-pyrazole-3-carboxamide
-
N-(quinolin-2-yl)-1H-pyrazole-3-carboxamide
-
N-(quinolin-3-yl)-1H-pyrazole-3-carboxamide
-
N-(quinolin-6-yl)-1H-pyrazole-3-carboxamide
-
N-(tert-butyl)-3-phenyl-6-(p-tolyl)imidazo[2,1-b]thiazol-5-amine
-
N-(tert-butyl)-6-(4-chlorophenyl)-3-phenylimidazo[2,1-b]thiazol-5-amine
-
N-(tert-butyl)-6-(4-methoxyphenyl)-3-phenylimidazo[2,1-b]thiazol-5-amine
-
N-(tert-butyl)-6-(4-nitrophenyl)-3-phenylimidazo[2,1-b]thiazol-5-amine
-
N-benzyl-1H-pyrazole-3-carboxamide
-
N-cyclohexyl-6-(2-fluorophenyl)-3-phenylimidazo[2,1-b][1,3]thiazol-5-amine
-
N-cyclohexyl-6-(4-methoxyphenyl)-3-phenylimidazo[2,1-b][1,3]thiazol-5-amine
-
N-cyclohexyl-6-(4-nitrophenyl)-3-phenylimidazo[2,1-b][1,3]thiazol-5-amine
-
N-phenyl-1H-pyrazole-3-carboxamide
-
N-[4-(trifluoromethyl)phenyl]-1H-pyrazole-3-carboxamide
-
N-[4-fluoro-2-(trifluoromethyl)phenyl]-1H-pyrazole-3-carboxamide
-
N1-(2H-1,3-benzodioxol-5-yl)-N-3-(2-chloro-4-fluorophenyl)-1H-pyrazole-1,3-dicarboxamide
-
N1-butyl-N3-(2-chlorophenyl)-N3-methyl-1H-pyrazole-1,3-dicarboxamide
-
N3-(2,2-difluoro-2H-1,3-benzodioxol-4-yl)-N1-hexyl-5-methyl-1H-pyrazole-1,3-dicarboxamide
-
N3-(2-chloro-4-fluorophenyl)-N1-hexyl-4-methyl-1H-pyrazole-1,3-dicarboxamide
-
N3-(2-chloro-4-fluorophenyl)-N1-pentyl-1H-pyrazole-1,3-dicarboxamide
-
N3-(2-chlorophenyl)-N1,N1-dimethyl-1H-pyrazole-1,3-dicarboxamide
-
nordihydroguaiaretic acid
-
phenyl[(E)-phenyldiazenyl]methanone
87% inhibition
quercetin
-
stylosin
IC50 value of cytotoxicity against PC-3 cells, 24 h, is 0.101 mM
-
[(E)-(4-bromophenyl)diazenyl](phenyl)methanone
44% inhibition
[(E)-(4-methoxyphenyl)diazenyl](phenyl)methanone
19% inhibition
[(E)-(4-methylphenyl)diazenyl](phenyl)methanone
44% inhibition
[(E)-(4-nitrophenyl)diazenyl](phenyl)methanone
34% inhibition
(Z)-9-octadecenyl sulfate
-
allosteric inhibition
1-phenyl-2-([[4-(trifluoromethyl)phenyl]methyl]sulfanyl)-1H-imidazole
mixed-type inhibitor, performs as potent inhibitor in a HEK-293 cell-based assay and binds in the U-shaped channel of 15-Lox-2
-
11-thialinoleic acid
-
is a noncompetitive inhibitor of 15-lipoxygenase-1 with respect to arachidonate or linoleic acid as substrates. Presence of inhibitor does not alter the product distribution for 15-lipoxygenase-1. It does not change the regioselectivity of 15-lipoxygenase-1
2,3,4,5-tetrabromo-6-(2,4-dibromophenoxy)phenol
-
IC50: 0.0018 mM
2,3,4,5-tetrabromo-6-(3,5-dibromo-2-hydroxyphenoxy)phenol
-
IC50: 0.00079 mM
2,3,5-tribromo-6-(3,5-dibromo-2-hydroxyphenoxy)phenol
-
IC50: 0.0022 mM
2,4-dibromo-6-(2,4-dibromo-6-methoxyphenoxy)phenol
-
IC50: 0.01 mM
2,4-Dibromophenol
-
IC50: 0.034 mM
2,6-dibromo-4-[1-(3-bromo-4-hydroxyphenyl)-1-methylethyl]phenol
-
IC50: 0.005 mM
2-(4-chlorophenyl)-5-cyclohexyl-1,3,4-oxadiazole
mixed-type inhibitor, performs as potent inhibitor in a HEK-293 cell-based assay and binds in the U-shaped channel of 15-Lox-2
2-([4-[(4-fluorobenzyl)oxy]butyl]sulfanyl)-5-(naphthalen-1-yl)-1,3,4-oxadiazole
-
-
2-alkyl benzopyran-4-ones
-
weak inhibition of isozymes 15-hLO-1 and 15-hLO-2
2-alkyl-6-hydroxy-4-H-benzopyran-4-one
-
weak inhibition of isozymes 15-hLO-1 and 15-hLO-2
2-phenyl-3-[3-(pyridin-3-yl)-4,5-dihydro-1H-pyrazol-5-yl]-1H-indole
molecular docking, compound is stabilized in the catalytic pocket of enzyme by pi-cation interaction with the catalytic Fe+ and formation of one hydrogen bond with Ile 676 amino acid
-
2-[[(4-bromophenyl)methyl]sulfanyl]-1-phenyl-1H-imidazole
mixed-type inhibitor, performs as potent inhibitor in a HEK-293 cell-based assay and binds in the U-shaped channel of 15-Lox-2
-
2-[[(4-ethylphenyl)methyl]sulfanyl]-1-phenyl-1H-imidazole
mixed-type inhibitor, performs as potent inhibitor in a HEK-293 cell-based assay and binds in the U-shaped channel of 15-Lox-2
-
3'-chloro-7,8-dihydroxyisoflavone
-
weak inhibition of isozyme 15-hLO-2
3,4,6,8-tetrabromooxanthren-1-ol
-
IC50: 0.0009 mM
3,4,6-tribromo-2-(2,4-dibromophenoxy)phenol
-
IC50: 0.005 mM
3,4-dibromo-2-(5-bromo-2-hydroxyphenoxy)phenol
-
IC50: 0.011 mM
3,6,8-tribromooxanthren-1-ol
-
IC50: 0.0008 mM
3-hydroxy-H-benzopyran-4-one derivatives
-
weak inhibition of isozymes 15-hLO-1 and 15-hLO-2
3-[3-bromo-5-(2,6-dibromo-4-{2-[2-(3-bromo-4-hydroxy-phenyl)-ethylcarbamoyl]-2-[(E)-hydroxyimino]-ethyl}-phenoxy)-4-methyl-phenyl]-N-[(E)-2-(3,5-dibromo-4-hydroxy-phenyl)-vinyl]-2-[(E)-hydroxyimino]-propionamide
-
IC50: 0.059 mM
3-[[(4-methylphenyl)methyl]sulfanyl]-1-phenyl-1H-1,2,4-triazole
mixed-type inhibitor, performs as potent inhibitor in a HEK-293 cell-based assay and binds in the U-shaped channel of 15-Lox-2
-
4',6,7-trihydroxyisoflavan
-
-
4',6,7-trihydroxyisoflavanone
-
weak inhibition of isozyme 15-hLO-2
4',6,7-trihydroxyisoflavone
-
weak inhibition of isozyme 15-hLO-2
4'-chloro-7,8-dihydroxyisoflavone
-
weak inhibition of isozyme 15-hLO-2
4,4'-propane-2,2-diylbis(2,6-dibromophenol)
-
IC50: 0.004 mM
4-((5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)butyl)-4-fluorobenzoate
-
-
4-((5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)methyl)-benzyl-4-fluorobenzoate
-
-
4-(2-chlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
-
-
4-(3,4-dichlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
-
-
4-(3,4-dichlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
-
-
4-(5-(1H-indol-2-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-(2-chlorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-(2-fluorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-(2-methoxyphenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-(3-fluorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-(3-hydroxynaphthalen-2-yl)-1,3,4-oxadiazol-2-ylthio)-but-2-ynyl-4-fluorobenzoate
-
low solubility
4-(5-(4-chlorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-(4-fluorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-(furan-2-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylamino)but-2-ynyl-thiophene-2-carboxylate
-
-
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)but-2-yn-1-ol
-
-
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-1H-indole-4-carboxylate
-
-
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-benzofuran-2-carboxylate
-
-
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-thiophene-2-carboxylate
-
-
4-(5-(naphthalen-1-yl)-1,3,4-thiadiazol-2-ylthio)but-2-ynyl-thiophene-2-carboxylate
-
low solubility
4-(5-(quinolin-5-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-(thiophen-2-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-phenyl-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-allyl-2-methoxyphenyl 1-adamantanecarboxylate
-
-
4-allyl-2-methoxyphenyl 1-cyclohexanecarboxylate
-
-
4-allyl-2-methoxyphenyl 2-chlorobenzoate
-
-
4-allyl-2-methoxyphenyl 2-fluorobenzoate
-
-
4-allyl-2-methoxyphenyl 2-methylbenzoate
-
-
4-allyl-2-methoxyphenyl 2-pyridinecarboxylate
-
-
4-allyl-2-methoxyphenyl 3-chlorobenzoate
-
-
4-allyl-2-methoxyphenyl 3-fluorobenzoate
-
-
4-allyl-2-methoxyphenyl 3-methoxybenzoate
-
-
4-allyl-2-methoxyphenyl 3-methylbenzoate
-
-
4-allyl-2-methoxyphenyl 4-chlorobenzoate
-
-
4-allyl-2-methoxyphenyl 4-fluorobenzoate
-
-
4-allyl-2-methoxyphenyl 4-methoxybenzoate
-
-
4-allyl-2-methoxyphenyl 4-methylbenzoate
-
-
4-allyl-2-methoxyphenyl benzoate
-
-
4-allyl-2-methoxyphenyl isonicotinate
-
-
4-allyl-2-methoxyphenyl nicotinate
-
-
4-Bromophenol
-
IC50: 0.055 mM
4-butyl-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
-
-
4-pentyl-N-(2-[2-phenyl-5-[4-(trifluoromethyl)phenyl]-1H-imidazol-4-yl]ethyl)benzenesulfonamide
-
-
4-pentyl-N-[2-(5-phenyl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
-
-
4-pentyl-N-[2-(5-phenyl-2-pyrazin-2-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
-
-
4-pentyl-N-[2-(5-phenyl-2-pyridin-2-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
-
-
4-pentyl-N-[2-(5-phenyl-2-pyridin-3-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
-
-
4-pentyl-N-[2-(5-phenyl-2-pyridin-4-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
-
-
4-pentyl-N-[2-(5-phenyl-2-thioformyl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
-
-
4-pentyl-N-[3-(5-phenyl-2-thioformyl-1H-imidazol-4-yl)propyl]benzenesulfonamide
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 1-benzothiophene-2-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 1-benzothiophene-3-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 1H-imidazole-4-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2,4-difluorobenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2-fluorobenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2-fluoropyridine-3-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2-methoxybenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3,4,5-trichlorothiophene-2-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3,4,5-trifluorobenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3,4-difluorobenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-(trifluoromethyl)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-chloro-1-benzothiophene-2-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-chlorothiophene-2-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-fluorobenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(difluoromethoxy)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(methylsulfonyl)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(triazan-2-yl)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(trifluoromethoxy)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(trifluoromethyl)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-bromobenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-chloro-3-(trifluoromethyl)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-[(trifluoromethyl)sulfanyl]benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl cyclobutanecarboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl cyclopentanecarboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl cyclopropanecarboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl furan-2-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl naphthalene-2-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl thiophene-3-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]butyl 4-fluorobenzoate
-
-
4-[[5-(naphthalen-2-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-fluorobenzoate
-
-
4-{[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}but-2-yn-1-yl 4-chlorobenzoate
-
-
4-{[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}but-2-yn-1-yl 4-fluorobenzoate
-
-
4-{[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}but-2-yn-1-yl 4-methoxybenzoate
-
-
5,8,11,14-Eicosatetraynoic acid
6,11-dihydro[1]benzothiopyrano[4,3-b]indole
-
PD146176
6,7-dihydroxy-2-t-butylbenzopyran-4-one
-
weak inhibition of isozyme 15-hLO-2
6,7-dihydroxy-3',4'-methylenedioxyisoflavan
-
-
6,7-dihydroxy-3'-methylisoflavan
-
-
6,7-dihydroxy-3'-methylisoflavanone
-
weak inhibition of isozyme 15-hLO-2
6,7-dihydroxy-4'-methoxyisoflavan
-
-
6,7-dihydroxy-4'-methoxyisoflavanone
-
weak inhibition of isozyme 15-hLO-2
6,7-dihydroxyisoflavones
-
weak inhibition of isozymes 15-hLO-1 and 15-hLO-2
6-hydroxy-2-pentyl-4H-benzopyran-4-one
-
weak inhibition of isozyme 15-hLO-2
6-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]-1-phenylhexan-1-one
-
low solubility
7,8-dihydroxy-3',4'-dimethoxyisoflavan
-
-
7,8-dihydroxy-3'-methylisoflavone
-
weak inhibition of isozyme 15-hLO-2
7,8-dihydroxy-3'-trifluoromethylisoflavone
-
weak inhibition of isozyme 15-hLO-2
7,8-dihydroxy-4'-methoxyisoflavan
-
-
7,8-dihydroxy-4'-methylisoflavan
-
-
7,8-dihydroxy-4'-methylisoflavone
-
weak inhibition of isozyme 15-hLO-2
7,8-dihydroxyisoflavone
-
weak inhibition of isozyme 15-hLO-2
7-hydroxy-H-benzopyran-4-one derivatives
-
weak inhibition of isozymes 15-hLO-1 and 15-hLO-2
alpha-mangostin
-
NSC30552, a natural product, caspase-3 pathway inhibitor, performs selective inhibition of 12-LO
anthraquinone
-
-
apigenin
-
IC50: 0.0034 mM without Triton X-100, IC50: 0.0003 mM in the presence of 0.01% Triton X-100
arachidonic acid
-
autoinactivates 15-hLO-1 to a much greater extent than linoleic acid at high substrate concentrations. No autoinactivation at low substrate concentrations
baicalein
bestatin 7
-
IC50: 0.027 mM
caffeic acid
cinnamyl 3,4-dihydroxy-cyanocinnamate
-
CDC
conjugated linoleic acids
-
conjugated linoleic acids may function as inhibitors of 15-LO-1 activity in macrophages/in vivo, overview
-
dysidenin
-
-
eicosatetraynoic acid
-
-
esculetin
-
-
GATA-6
-
inhibits non-steroidal anti-inflammatory drugs-induced transcription of 15-LOX-1 in colorectal cancer cells
-
glucocorticoid
-
inhibits induction in monocytes
-
interferon-gamma
-
inhibits induction in monocytes
-
linoleic acid
michellamine B
-
NSC661755, potent but non-selective inhibitor, a natural anti-viral agent
N'-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
-
-
N'-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3S)-1-phenoxypyrrolidin-3-yl]sulfamide
-
-
N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
-
-
N-(4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol)-2-ylthio)but-2-ynyl-thiophene-2-carboxamide
-
-
N-ethyl-N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-N-[(3R)-1-(1-methyl-1-phenylethyl)pyrrolidin-3-yl]sulfamide
-
-
N-ethyl-N-[(3R)-1-[1-(4-fluorophenyl)ethyl]pyrrolidin-3-yl]-N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]sulfamide
-
-
N-[(3R)-1-(3,4-dichlorobenzyl)pyrrolidin-3-yl]-N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-N-methylsulfamide
-
-
N-[2-(2,5-diphenyl-1H-imidazol-4-yl)ethyl]-4-methylbenzenesulfonamide
-
-
N-[2-(2,5-diphenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-(2-cyclopropyl-5-phenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-(2-methyl-5-phenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-(2-tert-butyl-5-phenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-[2-(2-methyl-1,3-thiazol-4-yl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-[2-(3-nitrophenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-[2-(4-chlorophenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-[2-(4-methoxyphenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-[2-(4-methylphenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-[5-(3-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-[5-(4-fluorophenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-phenylpiperazine-1-sulfonamide
-
-
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N'-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
-
-
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N'-[(3S)-1-phenoxypyrrolidin-3-yl]sulfamide
-
-
N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-4-pentylpiperazine-1-sulfonamide
-
-
N-[3-(2,5-diphenyl-1H-imidazol-4-yl)propyl]-4-pentylbenzenesulfonamide
-
-
neodysidenin
-
natural product from marine sponge Dysidea herbacea from Papua New Guinea, extraction and purification, overview, steady-state inhibition kinetics, competitive mode of inhibition, selective for 12-LO
nor-dihydro-guaiaretic acid
-
-
nordihydroguaiaretic acid
NSC172033
-
a synthetic compound from the NCI library
NSC292213
-
a synthetic compound from the NCI library
NSC617570
-
a synthetic compound from the NCI library
PD146176
-
-
quercetin
-
-
siRNA
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12(S)-hydroperoxyeicosatetraenoic acid
-
reduces the kinetic lag phase
13(S)-hydroperoxyoctadecadienoic acid
-
activates 15-hLO-1 and removes the kinetic lag phase
13-(S)-hydroxyoctadecadienoic acid
-
allosteric effector, which changes the conformation of 15-hLO-2 such that substrate affinity toward linoleic acid is significantly increased
13-hydroperoxy-octadecadienoic acid
-
-
15(S)-hydroperoxyeicosatetraenoic acid
-
activates 15-hLO-1 and removes the kinetic lag phase
Acetylsalicylic acid
-
ASA, 40% activation of 15(S)-HETE production at 0.02 mM in ASA-sensitive asthmatic patients
mannitol
-
osmotic activation of nasal tissue with mannitol activates 15-LO-1 leading to increased amounts of 15(S)-hydroxyeicosatetranoic acid in nasal lavage, and the levels of 15(S)-hydroxyeicosatetranoic acid are associated with nasal symptoms
phosphatidylcholine
-
stimulates
phosphatidylinositol-3,4-bisphosphate
-
0.02 mM, 3fold activity increase, in the presence of Ca2+
phosphatidylinositol-4,5-bisphosphate
-
0.02 mM, 3fold activity increase, in the presence of Ca2+
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0067
4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid
pH 7.5, 25°C
-
0.0078
5S-hydroperoxy-6E,8Z,10E,14Z-eicosatetraenoic acid
pH 7.5, temperature not specified in the publication
-
0.0049
5S-hydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
pH 7.5, temperature not specified in the publication
-
0.0027 - 0.005
arachidonate
0.0009
4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid
pH 7.5, 25°C
-
0.0017 - 0.057
5S-hydroperoxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
0.0017 - 0.029
5S-hydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
0.00095 - 0.005
arachidonate
0.0025 - 1.1
arachidonic acid
0.003 - 0.0772
linoleic acid
0.01
lipoic acid
-
splice variant 15-LOb1
0.0096 - 4.2
O2
additional information
additional information
-
steady-state kinetics of isozymes 15-hLO-1 and 15-hLO-2 with arachidonate and linoleic acid in presence or absence of 0.2% sodium cholate, or of oxygenated fatty acids, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.4
4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid
pH 7.5, 25°C
-
4.6
5S,15S-dihydroperoxyeicosatetraenoic acid
pH 7.5, temperature not specified in the publication
-
1.8
5S-hydroperoxy-6E,8Z,10E,14Z-eicosatetraenoic acid
pH 7.5, temperature not specified in the publication
-
1.1
5S-hydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
pH 7.5, temperature not specified in the publication
-
5.3 - 10
arachidonate
13
4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid
pH 7.5, 25°C
-
0.088 - 2
5S-hydroperoxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
2.1 - 9.7
5S-hydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
0.96 - 18
arachidonate
0.57 - 9.93
arachidonic acid
4 - 17.8
linoleic acid
5.1 - 7.6
O2
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
360
4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid
pH 7.5, 25°C
-
0.00021
5S,15S-dihydroperoxyeicosatetraenoic acid
pH 7.5, temperature not specified in the publication
-
230
5S-hydroperoxy-6E,8Z,10E,14Z-eicosatetraenoic acid
pH 7.5, temperature not specified in the publication
-
230
5S-hydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
pH 7.5, temperature not specified in the publication
-
2000 - 2100
arachidonate
14000
4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid
pH 7.5, 25°C
-
35 - 51
5S-hydroperoxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
72 - 5800
5S-hydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
190 - 19000
arachidonate
0.00005 - 0.00075
arachidonic acid
240 - 790
O2
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00398
4-[(E)-benzoyldiazenyl]benzonitrile
pH and temperature not specified in the publication
0.00081
N'-(4-methylphenyl)benzohydrazide
pH and temperature not specified in the publication
0.1
2-([4-[(4-fluorobenzyl)oxy]butyl]sulfanyl)-5-(naphthalen-1-yl)-1,3,4-oxadiazole
-
Ki above 0.1 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.0006
4-((5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)butyl)-4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.07
4-((5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)methyl)-benzyl-4-fluorobenzoate
-
apparent value, Ki above 0.07 mM, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000023
4-(5-(1H-indol-2-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000057
4-(5-(2-chlorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000043
4-(5-(2-fluorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000081
4-(5-(2-methoxyphenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-(5-(3-fluorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, Ki above 0.00001 mM, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-(5-(4-chlorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, Ki above 0.00001 mM, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-(5-(4-fluorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, Ki above 0.00001 mM, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.001
4-(5-(furan-2-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.0013
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylamino)but-2-ynyl-thiophene-2-carboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.0035
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)but-2-yn-1-ol
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000076
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-1H-indole-4-carboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000015
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-benzofuran-2-carboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000019
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-thiophene-2-carboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00014
4-(5-(quinolin-5-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000082
4-(5-(thiophen-2-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000026
4-(5-phenyl-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 1-benzothiophene-2-carboxylate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 1-benzothiophene-3-carboxylate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.0014
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 1H-imidazole-4-carboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2,4-difluorobenzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2-fluorobenzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2-fluoropyridine-3-carboxylate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00047
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2-methoxybenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3,4,5-trichlorothiophene-2-carboxylate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000016
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3,4,5-trifluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3,4-difluorobenzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000027
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-(trifluoromethyl)benzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000031
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-chloro-1-benzothiophene-2-carboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-chlorothiophene-2-carboxylate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-fluorobenzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(difluoromethoxy)benzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000033
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(methylsulfonyl)benzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000015
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(triazan-2-yl)benzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(trifluoromethoxy)benzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(trifluoromethyl)benzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-bromobenzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.0001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-chloro-3-(trifluoromethyl)benzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-[(trifluoromethyl)sulfanyl]benzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl benzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000085
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl cyclobutanecarboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl cyclopentanecarboxylate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00027
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl cyclopropanecarboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00017
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl furan-2-carboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000022
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl naphthalene-2-carboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl thiophene-3-carboxylate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000026
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]butyl 4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-2-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-fluorobenzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-{[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}but-2-yn-1-yl 4-chlorobenzoate
-
apparent value, Ki above 0.00001 mM, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-{[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}but-2-yn-1-yl 4-fluorobenzoate
-
apparent value, Ki above 0.00001 mM, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-{[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}but-2-yn-1-yl 4-methoxybenzoate
-
apparent value, Ki above 0.00001 mM, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.002
apigenin
-
-
0.00018 - 0.0011
baicalein
0.008
dysidenin
-
above, pH 7.5, recombinant isozyme 15-hLO-1
0.005 - 0.017
linoleic acid
0.002
N-(4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol)-2-ylthio)but-2-ynyl-thiophene-2-carboxamide
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.5
neodysidenin
-
above, pH 7.5, recombinant isozyme 15-hLO-1
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000032
4,5-dichloro-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0171
4-methyl-2-(4-methylpiperazinyl)pyrimido[4,5-b]benzothiazine
Homo sapiens
pH 7.0, 25°C
-
0.00978
4-[(E)-benzoyldiazenyl]benzonitrile
Homo sapiens
pH and temperature not specified in the publication
0.0002
5-(methylamino)-2-(naphthalen-1-yl)-4,5-dihydro-1,3-oxazole-4-carbonitrile
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.00055
5-chloro-N-(2,4-dichlorophenyl)-1H-pyrazole-3-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.000197
6,6a,11,11a-tetrahydro[1]benzothiopyrano[4,3-b]indole
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.0261
adamantyl caffeate
Homo sapiens
pH 7.0, 25°C
-
0.399
bornyl vanillate
Homo sapiens
pH 7.0, 25°C
-
0.00009
ethyl 6-chloro-3-[(3S)-3-hydroxy-7-methyloctanoyl]-2,3-dihydro-1H-indole-2-carboxylate
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.011
fenchyl caffeate
Homo sapiens
pH 7.0, 25°C
-
0.00535
N'-(4-methylphenyl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000099
N-(2,4-dichlorophenyl)-1H-pyrazole-3-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0001
N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000025
NDGA
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00697
phenyl[(E)-phenyldiazenyl]methanone
Homo sapiens
pH and temperature not specified in the publication
0.0668
stylosin
Homo sapiens
pH 7.0, 25°C
-
0.00034
1-phenyl-2-([[4-(trifluoromethyl)phenyl]methyl]sulfanyl)-1H-imidazole
Homo sapiens
pH 7.5, 23°C
-
0.0018
2,3,4,5-tetrabromo-6-(2,4-dibromophenoxy)phenol
Homo sapiens
-
IC50: 0.0018 mM
0.00079
2,3,4,5-tetrabromo-6-(3,5-dibromo-2-hydroxyphenoxy)phenol
Homo sapiens
-
IC50: 0.00079 mM
0.0022
2,3,5-tribromo-6-(3,5-dibromo-2-hydroxyphenoxy)phenol
Homo sapiens
-
IC50: 0.0022 mM
0.01
2,4-dibromo-6-(2,4-dibromo-6-methoxyphenoxy)phenol
Homo sapiens
-
IC50: 0.01 mM
0.034
2,4-Dibromophenol
Homo sapiens
-
IC50: 0.034 mM
0.005
2,6-dibromo-4-[1-(3-bromo-4-hydroxyphenyl)-1-methylethyl]phenol
Homo sapiens
-
IC50: 0.005 mM
0.0026
2-(4-chlorophenyl)-5-cyclohexyl-1,3,4-oxadiazole
Homo sapiens
pH 7.5, 23°C
0.00053
2-[[(4-bromophenyl)methyl]sulfanyl]-1-phenyl-1H-imidazole
Homo sapiens
pH 7.5, 23°C
-
0.00087
2-[[(4-ethylphenyl)methyl]sulfanyl]-1-phenyl-1H-imidazole
Homo sapiens
pH 7.5, 23°C
-
0.0062
3'-chloro-7,8-dihydroxyisoflavone
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.0009
3,4,6,8-tetrabromooxanthren-1-ol
Homo sapiens
-
IC50: 0.0009 mM
0.005
3,4,6-tribromo-2-(2,4-dibromophenoxy)phenol
Homo sapiens
-
IC50: 0.005 mM
0.011
3,4-dibromo-2-(5-bromo-2-hydroxyphenoxy)phenol
Homo sapiens
-
IC50: 0.011 mM
0.0008
3,6,8-tribromooxanthren-1-ol
Homo sapiens
-
IC50: 0.0008 mM
0.059
3-[3-bromo-5-(2,6-dibromo-4-{2-[2-(3-bromo-4-hydroxy-phenyl)-ethylcarbamoyl]-2-[(E)-hydroxyimino]-ethyl}-phenoxy)-4-methyl-phenyl]-N-[(E)-2-(3,5-dibromo-4-hydroxy-phenyl)-vinyl]-2-[(E)-hydroxyimino]-propionamide
Homo sapiens
-
IC50: 0.059 mM
0.0031
3-[[(4-methylphenyl)methyl]sulfanyl]-1-phenyl-1H-1,2,4-triazole
Homo sapiens
pH 7.5, 23°C
-
0.00051 - 0.071
4',6,7-trihydroxyisoflavan
0.0038 - 0.1
4',6,7-trihydroxyisoflavanone
0.049
4',6,7-trihydroxyisoflavone
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.009
4'-chloro-7,8-dihydroxyisoflavone
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.004
4,4'-propane-2,2-diylbis(2,6-dibromophenol)
Homo sapiens
-
IC50: 0.004 mM
0.045 - 0.132
4-(2-chlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
0.055 - 0.378
4-(3,4-dichlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
0.036 - 0.133
4-(3,4-dichlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
0.055
4-Bromophenol
Homo sapiens
-
IC50: 0.055 mM
0.014 - 0.05
4-butyl-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
0.000072 - 0.000372
4-pentyl-N-(2-[2-phenyl-5-[4-(trifluoromethyl)phenyl]-1H-imidazol-4-yl]ethyl)benzenesulfonamide
0.01
4-pentyl-N-[2-(5-phenyl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
Homo sapiens
-
above, versus substrate linoleic acid
0.00281
4-pentyl-N-[2-(5-phenyl-2-pyrazin-2-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.00097 - 5.321
4-pentyl-N-[2-(5-phenyl-2-pyridin-2-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
0.00056
4-pentyl-N-[2-(5-phenyl-2-pyridin-3-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.000087 - 3.211
4-pentyl-N-[2-(5-phenyl-2-pyridin-4-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
0.000006 - 0.000013
4-pentyl-N-[2-(5-phenyl-2-thioformyl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
0.000053 - 0.000396
4-pentyl-N-[3-(5-phenyl-2-thioformyl-1H-imidazol-4-yl)propyl]benzenesulfonamide
0.018
6,7-dihydroxy-2-t-butylbenzopyran-4-one
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.00035 - 0.016
6,7-dihydroxy-3',4'-methylenedioxyisoflavan
0.00021 - 0.0083
6,7-dihydroxy-3'-methylisoflavan
0.00021 - 0.014
6,7-dihydroxy-3'-methylisoflavanone
0.00015 - 0.1
6,7-dihydroxy-4'-methoxyisoflavan
0.0016 - 0.019
6,7-dihydroxy-4'-methoxyisoflavanone
0.038
6-hydroxy-2-pentyl-4H-benzopyran-4-one
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.1
7,8-dihydroxy-3',4'-dimethoxyisoflavan
0.011
7,8-dihydroxy-3'-methylisoflavone
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.0083
7,8-dihydroxy-3'-trifluoromethylisoflavone
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.0037 - 0.1
7,8-dihydroxy-4'-methoxyisoflavan
0.0057 - 0.1
7,8-dihydroxy-4'-methylisoflavan
0.0078
7,8-dihydroxy-4'-methylisoflavone
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.013
7,8-dihydroxyisoflavone
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.0031 - 0.05
alpha-mangostin
0.0003 - 100
apigenin
Homo sapiens
-
IC50: 0.0034 mM without Triton X-100, IC50: 0.0003 mM in the presence of 0.01% Triton X-100
0.038 - 100
baicalein
Homo sapiens
-
potent inhibitor, IC50: 0.0016 mM without Triton X-100, IC50: 0.038 mM in the presence of 0.01% Triton X-100
0.027
bestatin 7
Homo sapiens
-
IC50: 0.027 mM
0.0076 - 0.05
michellamine B
0.031 - 0.186
N'-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
0.08 - 0.822
N'-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3S)-1-phenoxypyrrolidin-3-yl]sulfamide
0.038 - 0.375
N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
0.01 - 0.132
N-ethyl-N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-N-[(3R)-1-(1-methyl-1-phenylethyl)pyrrolidin-3-yl]sulfamide
0.003 - 0.75
N-ethyl-N-[(3R)-1-[1-(4-fluorophenyl)ethyl]pyrrolidin-3-yl]-N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]sulfamide
0.011 - 0.083
N-[(3R)-1-(3,4-dichlorobenzyl)pyrrolidin-3-yl]-N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-N-methylsulfamide
0.000364 - 0.0028
N-[2-(2,5-diphenyl-1H-imidazol-4-yl)ethyl]-4-methylbenzenesulfonamide
0.000033 - 0.000162
N-[2-(2,5-diphenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
0.01
N-[2-(2-cyclopropyl-5-phenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
0.01
N-[2-(2-methyl-5-phenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
above, versus substrate linoleic acid
0.00192 - 0.01
N-[2-(2-tert-butyl-5-phenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
0.00072
N-[2-[2-(2-methyl-1,3-thiazol-4-yl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.000099 - 0.0011
N-[2-[2-(3-nitrophenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
0.000021 - 0.0011
N-[2-[2-(4-chlorophenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
0.01
N-[2-[2-(4-methoxyphenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
above, versus substrate linoleic acid
0.003
N-[2-[2-(4-methylphenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.000082 - 0.000531
N-[2-[5-(3-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
0.000059 - 0.000261
N-[2-[5-(4-fluorophenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
0.000014 - 0.00005
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
0.212 - 3.45
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-phenylpiperazine-1-sulfonamide
0.083 - 0.719
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N'-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
0.272 - 2.41
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N'-[(3S)-1-phenoxypyrrolidin-3-yl]sulfamide
0.091 - 0.646
N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-4-pentylpiperazine-1-sulfonamide
0.00014 - 0.000914
N-[3-(2,5-diphenyl-1H-imidazol-4-yl)propyl]-4-pentylbenzenesulfonamide
0.5
neodysidenin
Homo sapiens
-
above, pH 7.5, recombinant isozyme 15-hLO-1
0.00011
nordihydroguaiaretic acid
Homo sapiens
-
IC50: 0.00011 mM
0.0094 - 0.05
NSC172033
0.025 - 0.05
NSC292213
0.05 - 0.5
NSC617570
0.1
additional information
Homo sapiens
-
IC50 above 0.1 mM: compound 1a, compound 1b, compound 1d, compound 1e, compound 1g
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.125
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7 - 7.3
-
-
6.8 - 7.2
-
-
7 - 8.5
-
-
8 - 9
-
pH-optimum of 15-LOX-2 for arachidonic acid oxygenation
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.5
-
pH 6 about 50% of maximal activity, pH 9.5 about 60% of maximal activity
7 - 8
-
approximately level between pH 7 and 8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
visceral adipose tissue
Manually annotated by BRENDA team
-
epidermoid carcinoma of the submandibular gland
Manually annotated by BRENDA team
-
expression, but no activity of 15-LOX in leukemic blasts induced by a Ca2+ ionophore, from acute myeloid leukemic and acute lymphoid leukemic patients, overview, quantitative expression analysis
Manually annotated by BRENDA team
-
medium expression
Manually annotated by BRENDA team
-
breast carcinoma BT-20 cells
Manually annotated by BRENDA team
-
express both 15-LOX-1 and -2
Manually annotated by BRENDA team
-
15-LOX-1 but not 15-LOX-2
Manually annotated by BRENDA team
-
hypopharyngeal carcinoma
Manually annotated by BRENDA team
-
epidermal carcinoma of the mouth
Manually annotated by BRENDA team
-
carcinoma of the retromolar trigone region
Manually annotated by BRENDA team
-
higher expression of 15-LO-1 compared with ostheoarthritis synovial tissue
Manually annotated by BRENDA team
-
15-LOX-1 and 15-LOX-2
Manually annotated by BRENDA team
-
CD14+
Manually annotated by BRENDA team
-
squamous cell carcinoma of retromolar trigone
Manually annotated by BRENDA team
-
laryngeal carcinoma
Manually annotated by BRENDA team
-
squamous cell carcinoma of floor mouth
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
15-LOX-1, in the stroma of fibroblasts
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
disruption of normal 12- and 15-LO function by the inflammatory obese condition promotes adipocyte dysfunction and overall metabolic disease including insulin resistance and diabetes
physiological function
malfunction
-
when 15-LOX-1 activity is knocked down by siRNA, the induction of MIP-1alpha, RANTES, and IP-10 is significantly attenuated
metabolism
-
shifting linoleic acid metabolism from 15-LOX-1 to COX-2 is procarcinogenic
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LOX15_HUMAN
662
0
74804
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
-
x * 70000, SDS-PAGE
72000
-
x * 72000, SDS-PAGE
74000
-
x * 74000, SDS-PAGE
74727
-
x * 74727, electrospray mass spectrometry
75000
-
SDS-PAGE
76000
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 75000
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I417A
naturally occuring mutation, the mutant produces 94% 12-hydroperoxyicosatetraenoate and 6% 15-hydroperoxyicosatetraenoate, in contrast to the wild-type, that produces 15% 12-hydroperoxyicosatetraenoate and 85% 15-hydroperoxyicosatetraenoate
M419T
naturally occuring mutation, the mutant produces more 12-hydroperoxyicosatetraenoate compared to 15-hydroperoxyicosatetraenoate, incontrast to the wild-type, inversed substrate specificity
T560M
naturally occurring enzyme mutant, the mutant shows 20fold reduced catalytic activity, genotyping using 12974 samples, the haplotypes show increased risk of coronary artery disease compared to non-carriers, overview
T594V
naturally occuring mutation, the mutant produces more 12-hydroperoxyicosatetraenoate compared to 15-hydroperoxyicosatetraenoate, incontrast to the wild-type, inversed substrate specificity
A416T
-
inactive mutant protein
A416V
-
inactive mutant protein
A417G
-
the mutant enzyme converts arachidonic acid to (11R)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid and (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid in a 1.5:1 ratio. The wild.type enzyme converts arachidonic acid exlusively (15S)-Hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid. Turnover number for arachidonic acid is 4.6fold lower than that of the wild-type enzyme, no significant change in Km-value
D602Y
-
15-LOX-2 mutant shows a similar pH-profile as the wild-type enzyme
D602Y/V603H
-
a strong shift of the pH profile of 15-LOX-2 mutant towards more acidic values
H361L
-
is devoid of enzymatic activity, can induce phosphorylation of p53 as the wild-type
L397M
-
ratio of 15-lipoxygenation to 12-lipoxygenation is 9:1 for the wild-type enzyme and the mutant enzymes V104I, L397M and Q431R
L397M/M418V
-
the ratio of 15-lipoxygenation to 12-lipoxygenation is 1:1 for the mutant enzymes V104/L397M/M418V/Q431R, L397M/M418V/Q431R, L397M/M418V and M418V, compared to 9:1 for the wild-type enzyme
L397M/M418V/Q431R
-
the ratio of 15-lipoxygenation to 12-lipoxygenation is 1:1 for the mutant enzymes V104/L397M/M418V/Q431R, L397M/M418V/Q431R, L397M/M418V and M418V, compared to 9:1 for the wild-type enzyme
M418V
-
the ratio of 15-lipoxygenation to 12-lipoxygenation is 1:1 for the mutant enzymes V104/L397M/M418V/Q431R, L397M/M418V/Q431R, L397M/M418V and M418V, compared to 9:1 for the wild-type enzyme
N287D
-
relative catalytic activity: 1.1% compared to wild-type 100%
N287L
-
relative catalytic activity: 0.5% compared to wild-type 100%
N287Q
-
relative catalytic activity: 3.9% compared to wild-type 100%
Q294L
-
relative catalytic activity: 0.6% compared to wild-type 100%
Q431R
-
ratio of 15-lipoxygenation to 12-lipoxygenation is 9:1 for the wild-type enzyme and the mutant enzymes V104I, L397M and Q431R
T560A
-
mutant shows strongly impaired catalytic activity, relative catalytic activity: 16.6% compared to wild-type 100%
T560M
-
mutant shows strongly impaired catalytic activity, relative catalytic activity: 3.8% compared to wild-type 100%
T560S
-
enzyme retains activity, relative catalytic activity: 70.7% compared to wild-type 100%
V104/L397M/M418V/Q431R
-
the ratio of 15-lipoxygenation to 12-lipoxygenation is 1:1 for the mutant enzymes V104/L397M/M418V/Q431R, L397M/M418V/Q431R, L397M/M418V and M418V, compared to 9:1 for the wild-type enzyme
V104I
-
ratio of 15-lipoxygenation to 12-lipoxygenation is 9:1 for the wild-type enzyme and the mutant enzymes V104I, L397M and Q431R
V603H
-
a strong shift of the pH profile of 15-LOX-2 mutant towards more acidic values. 15-H(p)ETE is the major oxygenation product at pH 8
additional information
-
endothelial 15-lipoxygenase-1 overexpression in Oryctolagus cuniculus aortic endothelial cells increases acetylcholine-induced hypotension and vasorelaxation, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
frozen at -70°C and thawed with recovery of activity
-
repeated freeze thawing especially in the absence of gylcerol results in 60% reduction of specific activity
-
severe autoinactivation is observed at high substrate concentrations if the substrate is not HPLC-purified and stored at -80°C
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 5% glycerol, stable for more than 6 months
-
-80°C, 10% glycerol
-
-80°C, 10-20% glycerol
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by one step Ni2+ affinity chromatography, more than 90% pure
-
on Ni column
-
partial
-
recombinant His-tagged enzyme from Escherichia coli coli by nickel affinity and anion exchange chromatography
-
recombinant His-tagged isozyme 15-hLO-1 by nickel affinity chromatography, recombinant untagged isozyme 15-hLO-2 by ion exchange chromatography
-
recombinant His6-tagged isozyme 15-LOX-2 from Escherichia coli strain Rossetta 2 (DE3) by cobalt affinity chromatography, ultrafiltration, and gel filtration
recombinant isozyme 15-hLO-2 from Spodoptera frugiperda Sf9 cells by anion exchange chromatography, recombinant His-tagged isozyme 15-hLO-1
-
Resource-Q 5 column chromatography
-
to greater than 90% purity
-
two enzyme forms
-
using Ni-NTA chromatography
-
without a His6-tag, more than 90% pure
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ALOX15, DNA and amino acid sequence determination and analysis of wild-type and mutant T560M, promoter sequence analysis, genotyping, overview, expression of wild-type and mutant enzymes in Escherichia coli and HEK-297 cells, the mutant shows a low expression level in both systems compared to the wild-type enzyme
gene ALOX15, located on the short arm of chromosome 17
recombinant expression of 15-LOX-1 in Spodoptera frugiperda SF9 cells
sequence comparisons and phylogenetic analysis
15-LO-1 expressed in Sf 9 cells
-
15-LOX-1 cDNA fragment without 3'-UTR inserted into pLP-IRESneo, overexpression of 15-LOX-1 in A549 cells
-
15-LOX2 has at least six alternatively spliced isoforms
expressed as a fusion protein with GFP (pEGFP-15LOX-2) in DU145 and PC-3 cells
-
expressed in CV-1 cells
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expressed in Mus musculus C57BL/6
-
expressed in Mus musculus C57BL/6 prostate
-
expressed in rabbit aorta endothelium
-
expressed in Sf9 cells
-
expressed with hexa-His tags
-
expression in a human osteosarcoma cell line, expression of a CheY-15-lipoxygenase fusion protein in Escherichia coli
-
expression in CHO and in neuro-2 A neuroblastoma cells both stably expressing human APP carrying the K670N/M671L Swedish mutation, expression analysis
-
expression in Escherichia coli
expression of His-tagged isozyme 15-hLO-1, expression of isozyme 15-hLO-2 in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
-
expression of isozyme 15-hLO-1 as His-tagged enzyme, and of untagged isozyme 15-hLO-2
-
expression of isozyme 15-hLO-2 in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system, expression of N-terminally His6-tagged 15-hLO-1
-
expression to high levels, approximately 20% of cellular protein, in a baculovirus/insect cell expression system
-
HCT-116 and LoVo cells transfected with 15-LOX-1 vector
-
isoenzyme 15S-LOb and a splice variant of 15-LOb, baculovirus/insect cell expression system
-
LOX isoforms ligated into the pQE-9 plasmid and expressed as N-terminal His-tag fusion protein in Escherichia coli (XL-1 Blue)
-
overexpressed as N-terminally, His6-tagged protein
-
overexpression of 15-LOX-2 in human macrophages by adenovirus-mediated gene delivery
-
overexpression of His-tagged enzyme in Escherichia coli
-
overexpression of isozyme 15-LO-1 in Oryctolagus cuniculus via adenovirus transfection method, the expression is restricted to aortic endothelial cells, overview
-
Pca cell clones stably expressing 15-LOX2 or splice variant 15-LOX2sc-b are estabilished. The 15-LOX2 clones express 15-LOX2 in the nuclei and possess robust enzymatic activity, whereas 15-LOX2sc-b clones show neither nuclear protein localization nor arachidonic acid-metabolizing activity
-
pcDNA3.1(1) vector carrying native or mutant 15-LOX-1 expressed in HCT-116 cells
-
radiation-inducible 15-LOX-2 expression vector in which the full-length 15-LOX-2 cDNA is inserted downstream the recombinant Egr-1 promoter (pEgr-LOX2-GFP) and transfected in head-and-neck cancer cells
-
RAW 267.4 murine macrophages stably transfected to overexpress 15-LO-1
-
recombinant expression of His6-tagged isozyme 15-LOX-2 in Escherichia coli strain Rossetta 2 (DE3), coexpression with Escherichia coli YjgD protein
transgenic mice overexpressing 15-LO-1
-
without a His6-tag
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
12/15-LO is upregulated in white adipose tissue in the obese state. The potent vasoconstricting and pro-inflammatory hormone angiotensin II (Ang II) led to increases in leukocyte-type 12-LO mRNA and protein levels, as well as increased enzyme activity
15LO1 is highly expressed in fresh epithelial cells from severe asthmatic patients
-
demethylation of DNA in some cell lines increases 15-LOX-1 expression. Increased levels of 15-LOX-1 are associated with downregulation of GATA-6 in Caco-2 colon cancer cells treated with sodium butyrate to induce cell differentiation and apoptosis. Activation of the cGMP-PKG system can induce the cellular expression of 15-LOX-1 in SW-480 colon cancer cells. 5-aza-2-deoxycytidine increases 15-LOX-1 expression. Interleukin-4 upregulates the 15-LOX-1 gene in HTB-38 and Caco-2 human colorectal cancer cell lines. Interleukin-13 upregulates the 15-LOX-1 gene in HTB-38 and Caco-2 human colorectal cancer cell lines
-
hypoxia increases ALOX15 in human muscle cells
-
increased expression and activity of 15-LO-1 in the respiratory tissue from asthma patients. Patients with chronic obstructive pulmonary disease also display an increased expression of 15-LO-1 in bronchial biopsies. Interleukin-4 and interleukin-13 are inducers
-
induction by interleukin-4 and interleukin-13
-
interleukin-13 induces 15LO1 expression and production of intracellular 15-hydroxyeicosatetraenoic acid conjugated to phosphotidylethanolamine in vitro. 15-hydroxyeicosatetraenoic acid enhances interleukin-13 induced MUC5AC expression in vitro
-
interleukin-4 increases the expression of 15-LOX-1 and of downstream targets of p53
-
ischemia of the heart leads to increased expression of ALOX15
-
level of 15-LOX expression is dose-dependently induced by UVA and UVB-irradiation. Psoralen plus ultraviolet A, UVA-photochemotherapy significantly increases 15-LOX expression
-
normal human airway epithelial cells treated with interleukin-4 express higher levels of 15-LOX-1 than transfected A549 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
drug development
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ford-Hutchinson, A.W.
Arachidonate 15-lipoxygenase; characteristics and potential biological significance
Eicosanoids
4
65-74
1991
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Izumi, T.; Radmark, O.; Joernvall, H.; Samuelsson, B.
Purification of two forms of arachidonate 15-lipoxygenase from human leukocytes
Eur. J. Biochem.
202
1231-1238
1991
Homo sapiens
Manually annotated by BRENDA team
Nichols, R.C.; Vanderhoek, J.Y.
Calcium regulation of the human PMN cytosolic 15-lipoxygenase
Biochim. Biophys. Acta
1085
77-81
1991
Homo sapiens
Manually annotated by BRENDA team
Izumi, T.; Radmark, O.; Samuelsson, B.
Purification of 15-lipoxygenase from human keukocytes, evidence for the presebce of isozymes
Adv. Prostaglandin Thromboxane Leukot. Res.
21
101-104
1990
Homo sapiens
-
Manually annotated by BRENDA team
Sigal, E.; Grunberger, D.; Highland, E.; Gross, C.; Dixon, R.A.F.; Craik, C.S.
Expression of cloned human reticulocyte 15-lipoxygenase and immunological evidence that 15-lipoxygenases of different cell types are related
J. Biol. Chem.
265
5113-5120
1990
Homo sapiens
Manually annotated by BRENDA team
Sigal, E.; Grunberger, D.; Cashman, J.R.; Craik, C.S.; Caughey, G.H.; Nadel, J.A.
Arachidonate 15-lipoxygenase from human eosinophil-enriched leukocytes: partial purification and properties
Biochem. Biophys. Res. Commun.
150
376-383
1988
Homo sapiens
Manually annotated by BRENDA team
Sigal, E.; Craik, C.S.; Dixon, R.A.F.; Nadel, J.A.
Cloning and expression of human arachidonate 15-lipoxygenase
Trans. Assoc. Am. Physicians
102
176-184
1989
Homo sapiens
Manually annotated by BRENDA team
Sigal, E.; Grunberger, D.; Craik, C.S.; Caughey, G.H.; Nadel, J.A.
Arachidonate 15-lipoxygenase (omega-6 lipoxygenase) from human leukocytes. Purification and structural homology to other mammalian lipoxygenases
J. Biol. Chem.
263
5328-5332
1988
Homo sapiens
Manually annotated by BRENDA team
Burrall, B.A.; Cheung, M.; Chiu, A.; Goetzel, E.J.
Enzymatic properties of the 15-lipoxygenase of human cultured keratinocytes
J. Invest. Dermatol.
91
294-297
1988
Homo sapiens
Manually annotated by BRENDA team
Soberman, R.J.; Harper, T.W.; Betteridge, D.; Lewis, R.A.; Austen, K.F.
Characterization and separation of the arachidonic acid 5-lipoxygenase and linoleic acid omega-6 lipoxygenase (arachidonic acid 15-lipoxygenase) of human polymorphonuclear leukocytes
J. Biol. Chem.
260
4508-4515
1985
Homo sapiens
Manually annotated by BRENDA team
Jung, G.; Yang, D.C.; Nakao, A.
Oxygenation of phosphatidylcholine by human polymorphonuclear leukocyte 15-lipoxygenase
Biochem. Biophys. Res. Commun.
130
559-566
1985
Homo sapiens
Manually annotated by BRENDA team
Sloane, D.L.; leung, R.; Craik, C.S.; Sigal, E.
A primary determinant for lipoxygenase positional specificity
Nature
354
149-1152
1991
Homo sapiens
Manually annotated by BRENDA team
Kuehn, H.; Heydeck, D.; Brinckman, R.; Trebus, F.
Regulation of cellular 15-lipoxygenase activity on pretranslational, translational, and posttranslational levels
Lipids
34
S273-S279
1999
Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus
-
Manually annotated by BRENDA team
Reddy, N.; Everhart, A.; Eling, T.; Glasgow, W.
Characterization of a 15-lipoxygenase in human breast carcinoma BT-20 cells: stimulation of 13-HODE formation by TGFa/EGF
Biochem. Biophys. Res. Commun.
231
111-116
1997
Homo sapiens
Manually annotated by BRENDA team
Kuehn, H.; Barnett, J.; Grunberger, D.; Baecker, P.; Chow, J.; Nguyen, B.; Bursztyn-Pettegrew, H.; Chan, H.; Sigal, E.
Overexpression, purification and characterization of human recombinant 15-lipoxygenase
Biochim. Biophys. Acta
1169
80-89
1993
Homo sapiens
Manually annotated by BRENDA team
Liminga, M.; Hornsten, L.; Sprecher, H.W.; Oliw, E.H.
Arachidonate 15-lipoxygenase in human corneal epithelium and 12- and 15-lipoxygenases in bovine corneal epithelium: comparison with other bovine 12-lipoxygenases
Biochim. Biophys. Acta
1210
288-296
1994
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Tang, S.; Bhatia, B.; Maldonado, C.J.; Yang, P.; Newman, R.A.; Liu, J.; Chandra, D.; Traag, J.; Klein, R.D.; Fischer, S.M.; Chopra, D.; Shen, J.; Zhau, H.E.; Chung, L.W.K.; Tang, D.G.
Evidence that arachidonate 15-lipoxygenase 2 is a negative cell cycle regulator in normal prostate epithelial cells
J. Biol. Chem.
277
16189-16201
2002
Homo sapiens (O15296), Homo sapiens
Manually annotated by BRENDA team
Kilty, I.; Logan, A.; Vickers, P.J.
Differential characteristics of human 15-lipoxygenase isozymes and a novel splice variant of 15S-lipoxygenase
Eur. J. Biochem.
266
83-93
1999
Homo sapiens
Manually annotated by BRENDA team
Mogul, R.; Johansen, E.; Holman, T.R.
Oleyl sulfate reveals allosteric inhibition of soybean lipoxygenase-1 and human 15-lipoxygenase
Biochemistry
39
4801-4807
2000
Homo sapiens
Manually annotated by BRENDA team
Schewe, T.
15-Lipoxygenase-1: A prooxidant enzyme
Biol. Chem.
383
365-374
2002
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
MacMillan, D.K.; Hill, E.; Sala, A.; Sigal, E.; Shuman, T.; Henson, P.M.; Murphy, R.C.
Eosinophil 15-lipoxygenase is a leukotriene A4 synthase
J. Biol. Chem.
269
26663-26668
1994
Homo sapiens
Manually annotated by BRENDA team
Segraves, E.N.; Holman, T.R.
Kinetic investigations of the rate-limiting step in human 12- and 15-lipoxygenase
Biochemistry
42
5236-5243
2003
Homo sapiens
Manually annotated by BRENDA team
Chang, M.S.; Schneider, C.; Roberts, R.L.; Shappell, S.B.; Haselton, F.R.; Boeglin, W.E.; Brash, A.R.
Detection and subcellular localization of two 15S-lipoxygenases in human cornea
Invest. Ophthalmol. Vis. Sci.
46
849-856
2005
Homo sapiens
Manually annotated by BRENDA team
Bhatia, B.; Maldonado, C.J.; Tang, S.; Chandra, D.; Klein, R.D.; Chopra, D.; Shappell, S.B.; Yang, P.; Newman, R.A.; Tang, D.G.
Subcellular localization and tumor-suppressive functions of 15-lipoxygenase 2 (15-LOX2) and its splice variants
J. Biol. Chem.
278
25091-25100
2003
Homo sapiens
Manually annotated by BRENDA team
Segraves, E.N.; Shah, R.R.; Segraves, N.L.; Johnson, T.A.; Whitman, S.; Sui, J.K.; Kenyon, V.A.; Cichewicz, R.H.; Crews, P.; Holman, T.R.
Probing the activity differences of simple and complex brominated aryl compounds against 15-soybean, 15-human, and 12-human lipoxygenase
J. Med. Chem.
47
4060-4065
2004
Glycine max, Homo sapiens
Manually annotated by BRENDA team
Coffa, G.; Brash, A.R.
A single active site residue directs oxygenation stereospecificity in lipoxygenases: Stereocontrol is linked to the position of oxygenation
Proc. Natl. Acad. Sci. USA
101
15579-15584
2004
Homo sapiens
Manually annotated by BRENDA team
Aggarwal, N.T.; Holmes, B.B.; Cui, L.; Viita, H.; Yla-Herttuala, S.; Campbell, W.B.
Adenoviral expression of 15-lipoxygenase-1 in rabbit aortic endothelium: role in arachidonic acid-induced relaxation
Am. J. Physiol. Heart Circ. Physiol.
292
H1033-H1041
2007
Homo sapiens
Manually annotated by BRENDA team
Andersson, E.; Schain, F.; Svedling, M.; Claesson, H.; Forsell, P.K.
Interaction of human 15-lipoxygenase-1 with phosphatidylinositol bisphosphates results in increased enzyme activity
Biochim. Biophys. Acta
1761
1498-1505
2006
Homo sapiens
Manually annotated by BRENDA team
Deschamps, J.D.; Kenyon, V.A.; Holman, T.R.
Baicalein is a potent in vitro inhibitor against both reticulocyte 15-human and platelet 12-human lipoxygenases
Bioorg. Med. Chem.
14
4295-4301
2006
Homo sapiens
Manually annotated by BRENDA team
Shureiqi, I.; Wu, Y.; Chen, D.; Yang, X.L.; Guan, B.; Morris, J.S.; Yang, P.; Newman, R.A.; Broaddus, R.; Hamilton, S.R.; Lynch, P.; Levin, B.; Fischer, S.M.; Lippman, S.M.
The critical role of 15-lipoxygenase-1 in colorectal epithelial cell terminal differentiation and tumorigenesis
Cancer Res.
65
11486-11492
2005
Homo sapiens
Manually annotated by BRENDA team
Deguchi, A.; Xing, S.W.; Shureiqi, I.; Yang, P.; Newman, R.A.; Lippman, S.M.; Feinmark, S.J.; Oehlen, B.; Weinstein, I.B.
Activation of protein kinase G up-regulates expression of 15-lipoxygenase-1 in human colon cancer cells
Cancer Res.
65
8442-8447
2005
Homo sapiens
Manually annotated by BRENDA team
Flores, A.M.; Li, L.; McHugh, N.G.; Aneskievich, B.J.
Enzyme association with PPARgamma: evidence of a new role for 15-lipoxygenase type 2
Chem. Biol. Interact.
151
121-132
2005
Homo sapiens
Manually annotated by BRENDA team
Kelavkar, U.; Lin, Y.; Landsittel, D.; Chandran, U.; Dhir, R.
The yin and yang of 15-lipoxygenase-1 and delta-desaturases: Dietary omega-6 linoleic acid metabolic pathway in prostate
J. Carcinog.
5
9-9
2006
Homo sapiens
Manually annotated by BRENDA team
Bhattacharjee, A.; Xu, B.; Frank, D.A.; Feldman, G.M.; Cathcart, M.K.
Monocyte 15-lipoxygenase expression is regulated by a novel cytosolic signaling complex with protein kinase C delta and tyrosine-phosphorylated Stat3
J. Immunol.
177
3771-3781
2006
Homo sapiens
Manually annotated by BRENDA team
Kim, J.S.; Baek, S.J.; Bottone, F.G.; Sali, T.; Eling, T.E.
Overexpression of 15-lipoxygenase-1 induces growth arrest through phosphorylation of p53 in human colorectal cancer cells
Mol. Cancer Res.
3
511-517
2005
Homo sapiens
Manually annotated by BRENDA team
Kong, J.; Sumaroka, M.; Eastmond, D.L.; Liebhaber, S.A.
Shared stabilization functions of pyrimidine-rich determinants in the erythroid 15-lipoxygenase and alpha-globin mRNAs
Mol. Cell. Biol.
26
5603-5614
2006
Homo sapiens
Manually annotated by BRENDA team
Kelavkar, U.P.; Parwani, A.V.; Shappell, S.B.; Martin, W.D.
Conditional expression of human 15-lipoxygenase-1 in mouse prostate induces prostatic intraepithelial neoplasia: the FLiMP mouse model
Neoplasia
8
510-522
2006
Homo sapiens
Manually annotated by BRENDA team
Subbarayan, V.; Krieg, P.; Hsi, L.C.; Kim, J.; Yang, P.; Sabichi, A.L.; Llansa, N.; Mendoza, G.; Logothetis, C.J.; Newman, R.A.; Lippman, S.M.; Menter, D.G.
15-Lipoxygenase-2 gene regulation by its product 15-(S)-hydroxyeicosatetraenoic acid through a negative feedback mechanism that involves peroxisome proliferator-activated receptor gamma
Oncogene
25
6015-6025
2006
Homo sapiens
Manually annotated by BRENDA team
Kim, K.S.; Chun, H.S.; Yoon, J.H.; Lee, J.G.; Lee, J.H.; Yoo, J.B.
Expression of 15-lipoxygenase-1 in human nasal epithelium: its implication in mucociliary differentiation
Prostaglandins Leukot. Essent. Fatty Acids
73
77-83
2005
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Jiang, W.G.; Watkins, G.; Douglas-Jones, A.; Mansel, R.E.
Reduction of isoforms of 15-lipoxygenase (15-LOX)-1 and 15-LOX-2 in human breast cancer
Prostaglandins Leukot. Essent. Fatty Acids
74
235-245
2006
Homo sapiens
Manually annotated by BRENDA team
Sen, M.; McHugh, K.; Hutzley, J.; Philips, B.J.; Dhir, R.; Parwani, A.V.; Kelavkar, U.P.
Orthotopic expression of human 15-lipoxygenase (LO)-1 in the dorsolateral prostate of normal wild-type C57BL/6 mouse causes PIN-like lesions
Prostaglandins Other Lipid Mediat.
81
1-13
2006
Homo sapiens
Manually annotated by BRENDA team
Fischer, K.A.; Van Leyen, K.; Lovercamp, K.W.; Manandhar, G.; Sutovsky, M.; Feng, D.; Safranski, T.; Sutovsky, P.
15-Lipoxygenase is a component of the mammalian sperm cytoplasmic droplet
Reproduction
130
213-222
2005
Babyrousa babyrussa, Equus caballus, Homo sapiens, Mus musculus, Sus scrofa
Manually annotated by BRENDA team
Wang, D.; Chen, S.; Feng, Y.; Yang, Q.; Campbell, B.H.; Tang, X.; Campbell, W.B.
Reduced expression of 15-lipoxygenase 2 in human head and neck carcinomas
Tumour Biol.
27
261-273
2006
Homo sapiens
Manually annotated by BRENDA team
Assimes, T.L.; Knowles, J.W.; Priest, J.R.; Basu, A.; Borchert, A.; Volcik, K.A.; Grove, M.L.; Tabor, H.K.; Southwick, A.; Tabibiazar, R.; Sidney, S.; Boerwinkle, E.; Go, A.S.; Iribarren, C.; Hlatky, M.A.; Fortmann, S.P.; Myers, R.M.; Kuhn, H.; Risch, N.; Quertermous, T.
A near null variant of 12/15-LOX encoded by a novel SNP in ALOX15 and the risk of coronary artery disease
Atherosclerosis
198
136-144
2008
Homo sapiens (P16050)
Manually annotated by BRENDA team
Jacquot, C.; Wecksler, A.T.; McGinley, C.M.; Segraves, E.N.; Holman, T.R.; van der Donk, W.A.
Isotope sensitive branching and kinetic isotope effects in the reaction of deuterated arachidonic acids with human 12- and 15-lipoxygenases
Biochemistry
47
7295-7303
2008
Homo sapiens
Manually annotated by BRENDA team
Wecksler, A.T.; Kenyon, V.; Deschamps, J.D.; Holman, T.R.
Substrate specificity changes for human reticulocyte and epithelial 15-lipoxygenases reveal allosteric product regulation
Biochemistry
47
7364-7375
2008
Homo sapiens
Manually annotated by BRENDA team
Gulliksson, M.; Brunnstroem, A.; Johannesson, M.; Backman, L.; Nilsson, G.; Harvima, I.; Dahlen, B.; Kumlin, M.; Claesson, H.
Expression of 15-lipoxygenase type-1 in human mast cells
Biochim. Biophys. Acta
1771
1156-1165
2007
Homo sapiens
Manually annotated by BRENDA team
Deschamps, J.D.; Gautschi, J.T.; Whitman, S.; Johnson, T.A.; Gassner, N.C.; Crews, P.; Holman, T.R.
Discovery of platelet-type 12-human lipoxygenase selective inhibitors by high-throughput screening of structurally diverse libraries
Bioorg. Med. Chem.
15
6900-6908
2007
Homo sapiens
Manually annotated by BRENDA team
Vasquez-Martinez, Y.; Ohri, R.V.; Kenyon, V.; Holman, T.R.; Sepulveda-Boza, S.
Structure-activity relationship studies of flavonoids as potent inhibitors of human platelet 12-hLO, reticulocyte 15-hLO-1, and prostate epithelial 15-hLO-2
Bioorg. Med. Chem.
15
7408-7425
2007
Homo sapiens
Manually annotated by BRENDA team
Sadeghian, H.; Seyedi, S.M.; Saberi, M.R.; Arghiani, Z.; Riazi, M.
Design and synthesis of eugenol derivatives, as potent 15-lipoxygenase inhibitors
Bioorg. Med. Chem.
16
890-901
2008
Glycine max, Homo sapiens
Manually annotated by BRENDA team
Weinstein, D.S.; Liu, W.; Ngu, K.; Langevine, C.; Combs, D.W.; Zhuang, S.; Chen, C.; Madsen, C.S.; Harper, T.W.; Robl, J.A.
Discovery of selective imidazole-based inhibitors of mammalian 15-lipoxygenase: highly potent against human enzyme within a cellular environment
Bioorg. Med. Chem. Lett.
17
5115-5120
2007
Homo sapiens
Manually annotated by BRENDA team
Jedrzejczak-Czechowicz, M.; Lewandowska-Polak, A.; Bienkiewicz, B.; Kowalski, M.L.
Involvement of 15-lipoxygenase and prostaglandin EP receptors in aspirin-triggered 15-hydroxyeicosatetraenoic acid generation in aspirin-sensitive asthmatics
Clin. Exp. Allergy
38
1108-1116
2008
Homo sapiens
Manually annotated by BRENDA team
Aggarwal, N.T.; Chawengsub, Y.; Gauthier, K.M.; Viita, H.; Yla-Herttuala, S.; Campbell, W.B.
Endothelial 15-lipoxygenase-1 overexpression increases acetylcholine-induced hypotension and vasorelaxation in rabbits
Hypertension
51
246-251
2008
Homo sapiens
Manually annotated by BRENDA team
Stachowska, E.; Dziedziejko, V.; Safranow, K.; Jakubowska, K.; Olszewska, M.; Machalinski, B.; Chlubek, D.
Effect of conjugated linoleic acids on the activity and mRNA expression of 5- and 15-lipoxygenases in human macrophages
J. Agric. Food Chem.
55
5335-5342
2007
Homo sapiens
Manually annotated by BRENDA team
Pirillo, A.; Uboldi, P.; Bolego, C.; Kuhn, H.; Catapano, A.L.
The 15-lipoxygenase-modified high density lipoproteins 3 fail to inhibit the TNF-alpha-induced inflammatory response in human endothelial cells
J. Immunol.
181
2821-2830
2008
Homo sapiens
Manually annotated by BRENDA team
Succol, F.; Pratico, D.
A role for 12/15 lipoxygenase in the amyloid beta precursor protein metabolism
J. Neurochem.
103
380-387
2007
Homo sapiens
Manually annotated by BRENDA team
Vincent, C.; Fiancette, R.; Donnard, M.; Bordessoule, D.; Turlure, P.; Trimoreau, F.; Denizot, Y.
5-LOX, 12-LOX and 15-LOX in immature forms of human leukemic blasts
Leuk. Res.
32
1756-1762
2008
Homo sapiens
Manually annotated by BRENDA team
Feltenmark, S.; Gautam, N.; Brunnstroem, A.; Griffiths, W.; Backman, L.; Edenius, C.; Lindbom, L.; Bjoerkholm, M.; Claesson, H.E.
Eoxins are proinflammatory arachidonic acid metabolites produced via the 15-lipoxygenase-1 pathway in human Feltenmark, S.; Gautam, N.; Brunnstroem, A.; Griffiths, W.; Backman, L.; Edenius, C.; Lindbom, L.; Bjoerkholm, M.; Claesson, H.E.: Eoxins are proinflammatory arachidonic acid metabolites produced via the 15-lipoxygenase-1 pathway in human eosinophils and mast cells
Proc. Natl. Acad. Sci. USA
105
680-685
2008
Homo sapiens
Manually annotated by BRENDA team
Tang, D.G.; Bhatia, B.; Tang, S.; Schneider-Broussard, R.
15-Lipoxygenase 2 (15-LOX2) is a functional tumor suppressor that regulates human prostate epithelial cell differentiation, senescence, and growth (size)
Prostaglandins Other Lipid Mediat.
82
135-146
2007
Homo sapiens (O15296), Homo sapiens
Manually annotated by BRENDA team
Liu, C.; Xu, D.; Liu, L.; Schain, F.; Brunnstroem, A.; Bjoerkholm, M.; Claesson, H.E.; Sjoeberg, J.
15-Lipoxygenase-1 induces expression and release of chemokines in cultured human lung epithelial cells
Am. J. Physiol. Lung Cell Mol. Physiol.
297
L196-L203
2009
Homo sapiens
Manually annotated by BRENDA team
Zhao, J.; Maskrey, B.; Balzar, S.; Chibana, K.; Mustovich, A.; Hu, H.; Trudeau, J.B.; ODonnell, V.; Wenzel, S.E.
Interleukin-13-induced MUC5AC is regulated by 15-lipoxygenase 1 pathway in human bronchial epithelial cells
Am. J. Respir. Crit. Care Med.
179
782-790
2009
Homo sapiens
Manually annotated by BRENDA team
Weibel, G.L.; Joshi, M.R.; Alexander, E.T.; Zhu, P.; Blair, I.A.; Rothblat, G.H.
Overexpression of human 15(S)-lipoxygenase-1 in RAW macrophages leads to increased cholesterol mobilization and reverse cholesterol transport
Arterioscler. Thromb. Vasc. Biol.
29
837-842
2009
Homo sapiens
Manually annotated by BRENDA team
Chabane, N.; Zayed, N.; Benderdour, M.; Martel-Pelletier, J.; Pelletier, J.; Duval, N.; Fahmi, H.
Human articular chondrocytes express 15-lipoxygenase-1 and -2: Potential role in osteoarthritis
Arthritis Res. Ther.
11
R44
2009
Homo sapiens
Manually annotated by BRENDA team
Gheorghe, K.R.; Korotkova, M.; Catrina, A.I.; Backman, L.; af Klint, E.; Claesson, H.E.; Radmark, O.; Jakobsson, P.J.
Expression of 5-lipoxygenase and 15-lipoxygenase in rheumatoid arthritis synovium and effects of intraarticular glucocorticoids
Arthritis Res. Ther.
11
R83
2009
Homo sapiens
Manually annotated by BRENDA team
Danielsson, K.; Rydberg, E.; Ingelsten, M.; Akyuerek, L.; Jirholt, P.; Ullstroem, C.; Forsberg, G.; Boren, J.; Wiklund, O.; Hulten, L.
15-Lipoxygenase-2 expression in human macrophages induces chemokine secretion and T cell migration
Atherosclerosis
199
34-40
2008
Homo sapiens
Manually annotated by BRENDA team
Wecksler, A.T.; Jacquot, C.; van der Donk, W.A.; Holman, T.R.
Mechanistic investigations of human reticulocyte 15- and platelet 12-lipoxygenases with arachidonic acid
Biochemistry
48
6259-6267
2009
Homo sapiens
Manually annotated by BRENDA team
Wecksler, A.T.; Kenyon, V.; Garcia, N.K.; Deschamps, J.D.; van der Donk, W.A.; Holman, T.R.
Kinetic and structural investigations of the allosteric site in human epithelial 15-lipoxygenase-2
Biochemistry
48
8721-8730
2009
Homo sapiens
Manually annotated by BRENDA team
Walther, M.; Roffeis, J.; Jansen, C.; Anton, M.; Ivanov, I.; Kuhn, H.
Structural basis for pH-dependent alterations of reaction specificity of vertebrate lipoxygenase isoforms
Biochim. Biophys. Acta
1791
827-835
2009
Oryctolagus cuniculus, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Yang, Q.; Feng, Y.; Schultz, C.J.; Li, X.A.; Wu, H.; Wang, D.
Synergistic effect of 15-lipoxygenase 2 and radiation in killing head-and-neck cancer
Cancer Gene Ther.
15
323-330
2008
Homo sapiens
Manually annotated by BRENDA team
Mochizuki, N.; Kwon, Y.
15-Lipoxygenase-1 in the vasculature: Expanding roles in angiogenesis
Circ. Res.
102
143-145
2008
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Claesson, H.E.; Griffiths, W.J.; Brunnstroem, A.; Schain, F.; Andersson, E.; Feltenmark, S.; Johnson, H.A.; Porwit, A.; Sjoeberg, J.; Bjoerkholm, M.
Hodgkin Reed-Sternberg cells express 15-lipoxygenase-1 and are putative producers of eoxins in vivo: novel insight into the inflammatory features of classical Hodgkin lymphoma
FEBS J.
275
4222-4234
2008
Homo sapiens
Manually annotated by BRENDA team
Yoo, H.; Jeon, B.; Jeon, M.S.; Lee, H.; Kim, T.Y.
Reciprocal regulation of 12- and 15-lipoxygenases by UV-irradiation in human keratinocytes
FEBS Lett.
582
3249-3253
2008
Homo sapiens
Manually annotated by BRENDA team
Zhu, H.; Glasgow, W.; George, M.D.; Chrysovergis, K.; Olden, K.; Roberts, J.D.; Eling, T.
15-lipoxygenase-1 activates tumor suppressor p53 independent of enzymatic activity
Int. J. Cancer
123
2741-2749
2008
Homo sapiens
Manually annotated by BRENDA team
Tang, Y.; Wang, M.T.; Chen, Y.; Yang, D.; Che, M.; Honn, K.V.; Akers, G.D.; Johnson, S.R.; Nie, D.
Downregulation of vascular endothelial growth factor and induction of tumor dormancy by 15-lipoxygenase-2 in prostate cancer
Int. J. Cancer
124
1545-1551
2009
Homo sapiens
Manually annotated by BRENDA team
Jacquot, C.; McGinley, C.M.; Plata, E.; Holman, T.R.; van der Donk, W.A.
Synthesis of 11-thialinoleic acid and 14-thialinoleic acid, inhibitors of soybean and human lipoxygenases
Org. Biomol. Chem.
6
4242-4252
2008
Homo sapiens
Manually annotated by BRENDA team
Claesson, H.E.
On the biosynthesis and biological role of eoxins and 15-lipoxygenase-1 in airway inflammation and Hodgkin lymphoma
Prostaglandins Other Lipid Mediat.
89
120-125
2009
Homo sapiens, Mus musculus, Oryctolagus cuniculus, Sus scrofa
Manually annotated by BRENDA team
Bhattacharya, S.; Mathew, G.; Jayne, D.G.; Pelengaris, S.; Khan, M.
15-lipoxygenase-1 in colorectal cancer: a review
Tumour Biol.
30
185-199
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Rai, G.; Kenyon, V.; Jadhav, A.; Schultz, L.; Armstrong, M.; Jameson, J.B.; Hoobler, E.; Leister, W.; Simeonov, A.; Holman, T.R.; Maloney, D.J.
Discovery of potent and selective inhibitors of human reticulocyte 15-lipoxygenase-1
J. Med. Chem.
53
7392-7404
2010
Homo sapiens
Manually annotated by BRENDA team
Magnusson, L.U.; Lundqvist, A.; Asp, J.; Synnergren, J.; Johansson, C.T.; Palmqvist, L.; Jeppsson, A.; Hulten, L.M.
High expression of arachidonate 15-lipoxygenase and proinflammatory markers in human ischemic heart tissue
Biochem. Biophys. Res. Commun.
424
327-330
2012
Homo sapiens
Manually annotated by BRENDA team
Schurmann, K.; Anton, M.; Ivanov, I.; Richter, C.; Kuhn, H.; Walther, M.
Molecular basis for the reduced catalytic activity of the naturally occurring T560M mutant of human 12/15-lipoxygenase that has been implicated in coronary artery disease
J. Biol. Chem.
286
23920-23927
2011
Homo sapiens
Manually annotated by BRENDA team
Zhao, J.; ODonnell, V.B.; Balzar, S.; St Croix, C.M.; Trudeau, J.B.; Wenzel, S.E.
15-Lipoxygenase 1 interacts with phosphatidylethanolamine-binding protein to regulate MAPK signaling in human airway epithelial cells
Proc. Natl. Acad. Sci. USA
108
14246-14251
2011
Homo sapiens
Manually annotated by BRENDA team
Droege, K.D.; Keithly, M.E.; Sanders, C.R.; Armstrong, R.N.; Thompson, M.K.
Structural dynamics of 15-lipoxygenase-2 via hydrogen-deuterium exchange
Biochemistry
56
5065-5074
2017
Homo sapiens (O15296)
Manually annotated by BRENDA team
Ackermann, J.A.; Hofheinz, K.; Zaiss, M.M.; Kroenke, G.
The double-edged role of 12/15-lipoxygenase during inflammation and immunity
Biochim. Biophys. Acta
1862
371-381
2017
Homo sapiens (P16050), Mus musculus (P39654)
Manually annotated by BRENDA team
Pelcman, B.; Sanin, A.; Nilsson, P.; Schaal, W.; Olofsson, K.; Krog-Jensen, C.; Forsell, P.; Hallberg, A.; Larhed, M.; Boesen, T.; Kromann, H.; Claesson, H.E.
N-Substituted pyrazole-3-carboxamides as inhibitors of human 15-lipoxygenase
Bioorg. Med. Chem. Lett.
25
3017-3023
2015
Homo sapiens (P16050)
Manually annotated by BRENDA team
Pelcman, B.; Sanin, A.; Nilsson, P.; No, K.; Schaal, W.; Oehrman, S.; Krog-Jensen, C.; Forsell, P.; Hallberg, A.; Larhed, M.; Boesen, T.; Kromann, H.; Vogensen, S.B.; Groth, T.; Claesson, H.E.
3-Substituted pyrazoles and 4-substituted triazoles as inhibitors of human 15-lipoxygenase-1
Bioorg. Med. Chem. Lett.
25
3024-3029
2015
Homo sapiens (P16050)
Manually annotated by BRENDA team
Tirapegui, C.; Acevedo-Fuentes, W.; Dahech, P.; Torrent, C.; Barrias, P.; Rojas-Poblete, M.; Mascayano, C.
Easy and rapid preparation of benzoylhydrazides and their diazene derivatives as inhibitors of 15-lipoxygenase
Bioorg. Med. Chem. Lett.
27
1649-1653
2017
Homo sapiens (P16050)
Manually annotated by BRENDA team
Tehrani, M.B.; Emami, S.; Asadi, M.; Saeedi, M.; Mirzahekmati, M.; Ebrahimi, S.M.; Mahdavi, M.; Nadri, H.; Moradi, A.; Moghadam, F.H.; Farzipour, S.; Vosooghi, M.; Foroumadi, A.; Shafiee, A.
Imidazo[2,1-b]thiazole derivatives as new inhibitors of 15-lipoxygenase
Eur. J. Med. Chem.
87
759-764
2014
Homo sapiens (P16050)
Manually annotated by BRENDA team
Ivanov, I.; Kuhn, H.; Heydeck, D.
Structural and functional biology of arachidonic acid 15-lipoxygenase-1 (ALOX15)
Gene
573
1-32
2015
Oryctolagus cuniculus (P12530), Oryctolagus cuniculus, Homo sapiens (P16050), Homo sapiens, Mus musculus (P39654), Mus musculus, Rattus norvegicus (Q02759)
Manually annotated by BRENDA team
Adel, S.; Karst, F.; Gonzalez-Lafont, A.; Pekarova, M.; Saura, P.; Masgrau, L.; Lluch, J.M.; Stehling, S.; Horn, T.; Kuhn, H.; Heydeck, D.
Evolutionary alteration of ALOX15 specificity optimizes the biosynthesis of antiinflammatory and proresolving lipoxins
Proc. Natl. Acad. Sci. USA
113
E4266-E4275
2016
Homo sapiens (P16050), Homo sapiens neanderthalensis, Homo sapiens subsp. 'Denisova', Macaca mulatta (F7EPQ4), Nomascus leucogenys (G1S6D2), Oryctolagus cuniculus (P12530), Pan paniscus, Pan troglodytes (H2QBX9), Papio anubis (A0A096P2G1), Pongo abelii (Q5RBE8), Pongo pygmaeus (Q5RBE8)
Manually annotated by BRENDA team
Cole, B.; Lieb, D.; Dobrian, A.; Nadler, J.
12- and 15-lipoxygenases in adipose tissue inflammation
Prostaglandins Other Lipid Mediat.
104-105
84-92
2013
Homo sapiens (P16050)
-
Manually annotated by BRENDA team
Green, A.R.; Freedman, C.; Tena, J.; Tourdot, B.E.; Liu, B.; Holinstat, M.; Holman, T.R.
5 S,15 S-Dihydroperoxyeicosatetraenoic Acid (5,15-diHpETE) as a lipoxin intermediate Reactivity and kinetics with human leukocyte 5-lipoxygenase, platelet 12-lipoxygenase, and reticulocyte 15-lipoxygenase-1
Biochemistry
57
6726-6734
2018
Homo sapiens (P16050), Homo sapiens
Manually annotated by BRENDA team
Freedman, C.; Tran, A.; Tourdot, B.E.; Kalyanaraman, C.; Perry, S.; Holinstat, M.; Jacobson, M.P.; Holman, T.R.
Biosynthesis of the maresin intermediate, 13S,14S-epoxy-DHA, by human 15-lipoxygenase and 12-lipoxygenase and its regulation through negative allosteric modulators
Biochemistry
59
1832-1844
2020
Homo sapiens (P16050), Homo sapiens (P18054), Homo sapiens
Manually annotated by BRENDA team
Perry, S.C.; Horn, T.; Tourdot, B.E.; Yamaguchi, A.; Kalyanaraman, C.; Conrad, W.S.; Akinkugbe, O.; Holinstat, M.; Jacobson, M.P.; Holman, T.R.
Role of human 15-lipoxygenase-2 in the biosynthesis of the lipoxin intermediate, 5S,15S-diHpETE, implicated with the altered positional specificity of human 15-lipoxygenase-1
Biochemistry
59
4118-4130
2020
Homo sapiens (O15296), Homo sapiens (P16050), Homo sapiens (P18054), Homo sapiens
Manually annotated by BRENDA team
Tsai, W.C.; Gilbert, N.C.; Ohler, A.; Armstrong, M.; Perry, S.; Kalyanaraman, C.; Yasgar, A.; Rai, G.; Simeonov, A.; Jadhav, A.; Standley, M.; Lee, H.W.; Crews, P.; Iavarone, A.T.; Jacobson, M.P.; Neau, D.B.; Offenbacher, A.R.; Newcomer, M.; Holman, T.R.
Kinetic and structural investigations of novel inhibitors of human epithelial 15-lipoxygenase-2
Bioorg. Med. Chem.
46
116349
2021
Homo sapiens (O15296), Homo sapiens
Manually annotated by BRENDA team
ElBordiny, H.S.; El-Miligy, M.M.; Kassab, S.E.; Daabees, H.; Mohamed Ali, W.A.; Abdelhamid Mohamed El-Hawash, S.
Design, synthesis, biological evaluation and docking studies of new 3-(4,5-dihydro-1H-pyrazol/isoxazol-5-yl)-2-phenyl-1H-indole derivatives as potent antioxidants and 15-lipoxygenase inhibitors
Eur. J. Med. Chem.
145
594-605
2018
Homo sapiens (O15296)
Manually annotated by BRENDA team
Nagasaki, T.; Schuyler, A.J.; Zhao, J.; Samovich, S.N.; Yamada, K.; Deng, Y.; Ginebaugh, S.P.; Christenson, S.A.; Woodruff, P.G.; Fahy, J.V.; Trudeau, J.B.; Stoyanovsky, D.; Ray, A.; Tyurina, Y.Y.; Kagan, V.E.; Wenzel, S.E.
15LO1 dictates glutathione redox changes in asthmatic airway epithelium to worsen type 2 inflammation
J. Clin. Invest.
132
e151685
2022
Homo sapiens (P16050)
Manually annotated by BRENDA team
Coppey, L.; Obrosov, A.; Shevalye, H.; Davidson, E.; Paradee, W.; Yorek, M.A.
Characterization of mice ubiquitously overexpressing human 15-lipoxygenase-1 effect of diabetes on peripheral neuropathy and treatment with menhaden oil
J. Diabetes Res.
2021
5564477
2021
Homo sapiens (P16050)
Manually annotated by BRENDA team
Goftari, S.N.; Sadeghian, H.; Bahrami, A.R.; Maleki, F.; Matin, M.M.
Stylosin and some of its synthetic derivatives induce apoptosis in prostate cancer cells as 15-lipoxygenase enzyme inhibitors
Naunyn Schmiedebergs Arch. Pharmacol.
392
1491-1502
2019
Homo sapiens (P16050), Homo sapiens
Manually annotated by BRENDA team
Archambault, A.S.; Turcotte, C.; Martin, C.; Provost, V.; Larose, M.C.; Laprise, C.; Chakir, J.; Bissonnette, E.; Laviolette, M.; Bosse, Y.; Flamand, N.
Comparison of eight 15-lipoxygenase (LO) inhibitors on the biosynthesis of 15-LO metabolites by human neutrophils and eosinophils
PLoS ONE
13
e0202424
2018
Homo sapiens (O15296), Homo sapiens (P16050), Homo sapiens
Manually annotated by BRENDA team