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Information on EC 1.13.11.31 - arachidonate 12-lipoxygenase and Organism(s) Homo sapiens and UniProt Accession O75342

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IUBMB Comments
The product is rapidly reduced to the corresponding 12S-hydroxy compound.
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This record set is specific for:
Homo sapiens
UNIPROT: O75342
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
12-lipoxygenase, 15-lipoxygenase, 12-lox, alox5, 15-lox-1, alox15, 12-lo, 15-lo, 12/15-lipoxygenase, 12/15-lox, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12(S)-lipoxygenase
-
12-lipoxygenase
-
oxylipin-producing enzyme
-
12(S)-lipoxygenase
-
-
12-lipoxygenase
12-LO
12-LOX
12/15 lipoxygenase
12/15-lipoxygenase
12/15-LO
12/15-LOX
-
-
12/15LO
-
-
12DELTA-lipoxygenase
-
-
-
-
12R-LOX-2
-
-
12S-lipoxygenase
15-lipoxygenase
-
2-lipoxygenase
-
ALOX 12/15
-
ALOX12
Alox15
ALOX15B
-
-
C-12 lipoxygenase
-
-
-
-
DELTA 12-lipoxygenase
-
-
-
-
human platelet 12-lipoxygenase
-
leukotriene A4 synthase M
-
-
-
-
lipoxygenase 12
-
-
LOX-12
-
-
LTA4 synthase
-
-
-
-
oygenase, arachidonate 12-lip-
-
-
-
-
p12-LO
-
-
platelet 12-lipoxygenase
-
platelet-type 12(S)-lipoxygenase
-
-
platelet-type 12-human lipoxygenase
-
platelet-type 12-lipoxygenase
-
-
platelet-type 12LO
-
Platelet-type lipoxygenase 12
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
dioxygenation
-
-
-
-
dehydration
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
arachidonate:oxygen 12-oxidoreductase
The product is rapidly reduced to the corresponding 12S-hydroxy compound.
CAS REGISTRY NUMBER
COMMENTARY hide
82391-43-3
-
SUBSTRATE
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,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
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
-
-
-
?
11,14,17-eicosatrienoic acid + O2
?
show the reaction diagram
-
no activity with enzyme from platelet
-
-
?
11,14-eicosadienoic acid + O2
?
show the reaction diagram
-
no activity with enzyme from platelet
-
-
?
4,7,10,13,16,19-docosahexaenoic acid + O2
?
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
-
-
-
?
5(S)-hydroxy-6E,8Z,11Z,14Z-eicosatetraenoic acid + O2
5,12-(5S,12S)-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid + 5,12-(5S,15S)-dihydroxy-6E,8Z,11Z,13E-eicosatetraenoic acid
show the reaction diagram
-
weak activity
5S,12S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid and 5S,15S-dihydroxy-6E,8Z,11Z,13E-eicosatetraenoic acid are produced in a ratio of about 8:2
?
5,8,11,14,17-eicosapentaenoic acid + O2
12-hydroxy-5,8,10,14,17-eicosapentaenoic 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
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
-
-
-
?
8,11,14-eicosatrienoic acid + O2
12-hydroxyeicosatrienoic acid
show the reaction diagram
-
-
-
-
?
alpha-linolenic acid + O2
?
show the reaction diagram
-
no activity with enzyme from platelet
-
-
?
arachidonate + O2
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyeicosa-5,8,10,14-tetraenoate
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
-
-
-
?
arachidonic acid + O2
(12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoic acid
show the reaction diagram
-
-
the mutant enzyme G441A converts arachidonic acid to 8S-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoic acid and 12R-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoic acid in a 1.4:1 ratio
-
?
arachidonic acid + O2
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
show the reaction diagram
-
-
-
-
?
arachidonic acid + O2
?
show the reaction diagram
-
-
-
-
?
gamma-linolenic acid + O2
10-hydroxy-octadeca-6Z,8E,12Z-trienoic acid
show the reaction diagram
-
weak activity
-
-
?
leukotriene A4 + O2
lipoxin A4
show the reaction diagram
LTA4 can be converted by the action of platelet 12-lipoxygenase (12-LO) to lipoxin A4 (LXA4)
-
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
-
?
linoleic acid + O2
13(S)-hydroperoxy-9Z,11E-octadecadienoic acid
show the reaction diagram
-
no activity with enzyme from platelet
-
-
?
linoleic acid + O2
?
show the reaction diagram
-
4% of the activity with arachidonate
-
-
?
15(S)-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoic acid + O2
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,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
show the reaction diagram
-
-
-
?
arachidonate + O2
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyeicosa-5,8,10,14-tetraenoate
show the reaction diagram
arachidonate + O2
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
show the reaction diagram
leukotriene A4 + O2
lipoxin A4
show the reaction diagram
LTA4 can be converted by the action of platelet 12-lipoxygenase (12-LO) to lipoxin A4 (LXA4)
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe3+
-
non-heme iron-containing enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ML355
a selective 12-LOX inhibitor, blocks both FcgammaRIIa-induced platelet aggregation and (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate production
11-thialinoleic acid
-
is a competitive inhibitor of 12-lipoxygenase with arachidonate as substrate. Presence of inhibitor does not alter the product distribution for 12-lipoxygenase. It does not change the regioselectivity of 12-lipoxygenase
2,3,4,5-tetrabromo-6-(2,4-dibromophenoxy)phenol
-
IC50: 0.0007 mM
2,3,4,5-tetrabromo-6-(4,5-dibromo-2-hydroxyphenoxy)phenol
-
IC50: 0.0041 mM
2,3,5-tribromo-6-(4,5-dibromo-2-hydroxyphenoxy)phenol
-
IC50: 0.00041 mM
2,4-dibromo-6-(2,4-dibromo-6-methoxyphenoxy)phenol
-
IC50: 0.012 mM
2,6-dibromo-4-[1-(3-bromo-4-hydroxyphenyl)-1-methylethyl]phenol
-
IC50: 0.007 mM
2-alkyl benzopyran-4-ones
-
weak inhibition
2-alkyl-6-hydroxy-4-H-benzopyran-4-one
-
weak inhibition
3'-chloro-7,8-dihydroxyisoflavone
-
-
3,15-dihydroxy-8,11,13-eicosatrienoic acid
-
IC50: 0.0075 mM
3,4,6,8-tetrabromooxanthren-1-ol
-
IC50: 0.05 mM
3,4,6-tribromo-2-(2,4-dibromophenoxy)phenol
-
IC50: 0.006 mM
3,4-dibromo-2-(5-bromo-2-hydroxyphenoxy)phenol
-
IC50: 0.047 mM
3,6,8-tribromooxanthren-1-ol
-
IC50: 0.03 mM
3-O-acetyl-11-keto-boswellic acid
-
0.03 mM
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: 0.0004 mM
4',6,7-trihydroxyisoflavan
-
-
4',6,7-trihydroxyisoflavanone
-
-
4',6,7-trihydroxyisoflavone
-
-
4'-chloro-7,8-dihydroxyisoflavone
-
-
4,15-dihydroxy-5,8,11,13-eicosatetraenoic acid
-
IC50: 0.0081 mM
4,4'-propane-2,2-diylbis(2,6-dibromophenol)
-
IC50: 0.01 mM
4,5-dichloro-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
-
4-methyl-2-(4-methylpiperazinyl)pyrimido[4,5-b]benzothiazine
-
-
4-[5-(1H-indol-3-yl)-3-trifluoromethyl-4,5-dihydropyrazol-1-yl]-benzenesulfonamide
-
0.01 mM inhibits LOX-12 by 5%
4-[5-(7-chloro-1H-indol-3-yl)-3-trifluoromethyl-4,5-dihydropyrazol-1-yl]-benzenesulfonamide
-
0.01 mM inhibits LOX-12 by 3%
5,15-dihydroxy-5,8,11,13,17-eicosapentaenoic acid
-
IC50: 0.0008 mM
5-(methylamino)-2-(naphthalen-1-yl)-4,5-dihydro-1,3-oxazole-4-carbonitrile
-
-
5-chloro-N-(2,4-dichlorophenyl)-1H-pyrazole-3-carboxamide
-
-
6,17-dihydroxy-4,7,10,13,15,19-eicosahexaenoic acid
-
IC50: 0.0004 mM
6,6a,11,11a-tetrahydro[1]benzothiopyrano[4,3-b]indole
-
-
6,7-dihydroxy-3',4'-methylenedioxyisoflavan
-
-
6,7-dihydroxy-3',4'-methylenedioxyisoflavone
-
-
6,7-dihydroxy-3'-methylisoflavan
-
-
6,7-dihydroxy-3'-methylisoflavanone
-
-
6,7-dihydroxy-4'-methoxyisoflavan
-
-
6,7-dihydroxy-4'-methoxyisoflavanone
-
-
6,7-dihydroxy-4'-methoxyisoflavone
-
-
6,7-dihydroxy-4'-nitroisoflavone
-
-
7,8-dihydroxy-3',4'-dimethoxyisoflavan
-
-
7,8-dihydroxy-3'-methylisoflavone
-
-
7,8-dihydroxy-3'-trifluoromethylisoflavone
-
-
7,8-dihydroxy-4'-methoxyisoflavan
-
-
7,8-dihydroxy-4'-methylisoflavan
-
-
7,8-dihydroxy-4'-methylisoflavone
-
-
7,8-dihydroxyisoflavone
-
-
7-hydroxy-H-benzopyran-4-one derivatives
-
weak inhibition
adamantyl caffeate
IC50 value of cytotoxicity against PC-3 cells, 24 h, is 0.074 mM
-
alpha-mangostin
NSC30552, a natural product, caspase-3 pathway inhibitor, performs selective inhibition of 12-LO
baicalein
benzoyl chloride
-
-
bestatin 7
-
IC50: 0.0023 mM
bornyl vanillate
IC50 value of cytotoxicity against PC-3 cells, 24 h, is 0.401 mM
-
caffeic acid
-
0.01 mM, 20-30% inhibition
celecoxib
-
0.01 mM inhibits LOX-12 by 7%
chloroglyoxylic acid ethyl ester
-
-
cinnamyl 3,4-dihydroxy-cyanocinnamate
-
CDC
dysidenin
-
eicosatetraynoic acid
-
0.01 mM, 90-95% inhibition
esculetin
-
0.01 mM, 90-95% inhibition
esculetine
-
inhibits the enzyme and its binding to cytoplasmic muscle fibrills, overview
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
-
H-benzopyran-4-one derivatives
-
weak inhibition
iodoacetate
-
1 mM, 5% inhibition
isonicotinaldehyde
-
-
Lubrol
-
0.2%, 60% inhibition
-
methyl-4-pyridyl ketone
-
-
michellamine B
NSC661755, potent but non-selective inhibitor, a natural anti-viral agent
N-(2,4-dichlorophenyl)-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
-
N-([5-chloro-2-(dimethylamino)-8-hydroxyquinolin-7-yl](furan-2-yl)methyl)acetamide
-
-
N-([5-chloro-8-hydroxy-2-(piperidin-1-yl)quinolin-7-yl](furan-2-yl)methyl)acetamide
-
-
N-benzyl-N-hydroxy-5-phenylpentanamide
-
-
N-[(2,5-dichloro-8-hydroxyquinolin-7-yl)(furan-2-yl)methyl]acetamide
-
-
N-[(4-chloro-1-hydroxynaphthalen-2-yl)(furan-2-yl)methyl]acetamide
-
-
N-[(5-bromo-8-hydroxyquinolin-7-yl)(furan-2-yl)methyl]acetamide
-
-
N-[(5-bromo-8-hydroxyquinolin-7-yl)(furan-2-yl)methyl]propanamide
-
-
N-[(5-bromo-8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]acetamide
-
-
N-[(5-bromo-8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]propanamide
-
-
N-[(5-bromofuran-2-yl)(5-chloro-8-hydroxyquinolin-7-yl)methyl]propanamide
-
-
N-[(5-chloro-8-hydroxy-1,2,3,4,4a,8a-hexahydroquinolin-7-yl)(furan-2-yl)methyl]propanamide
-
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-fluorophenyl)methyl]propanamide
-
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]propanamide
-
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(5-methylthiophen-2-yl)methyl]propanamide
-
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(cyclopropyl)methyl]acetamide
-
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(cyclopropyl)methyl]propanamide
-
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(furan-2-yl)methyl]-4-methylbenzamide
-
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(furan-2-yl)methyl]acetamide
-
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(furan-2-yl)methyl]benzamide
-
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(furan-2-yl)methyl]propanamide
-
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]acetamide
-
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]propanamide
-
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)methyl]acetamide
-
-
N-[(5-chloro-8-methoxyquinolin-7-yl)(furan-2-yl)methyl]propanamide
-
-
N-[(5-fluoro-8-hydroxyquinolin-7-yl)(furan-2-yl)methyl]acetamide
-
-
N-[(5-fluoro-8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]acetamide
-
-
N-[(8-hydroxy-5-nitroquinolin-7-yl)(thiophen-2-yl)methyl]propanamide
-
-
N-[(8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]propanamide
-
-
N-[(R)-(5-bromo-8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]acetamide
-
-
N-[(R)-(5-bromo-8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]propanamide
-
-
N-[(S)-(5-bromo-8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]acetamide
-
-
N-[(S)-(5-bromo-8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]propanamide
-
-
N-[1-(5-chloro-8-hydroxyquinolin-7-yl)-2-methylpropyl]acetamide
-
-
N-[1-(5-chloro-8-hydroxyquinolin-7-yl)-2-methylpropyl]propanamide
-
-
N-[1-(5-chloro-8-hydroxyquinolin-7-yl)ethyl]acetamide
-
-
N-[1-(5-chloro-8-hydroxyquinolin-7-yl)ethyl]propanamide
-
-
N-[1-(5-fluoro-8-hydroxyquinolin-7-yl)ethyl]acetamide
-
-
N-[furan-2-yl(8-hydroxy-5-nitroquinolin-7-yl)methyl]propanamide
-
-
NCTT-956
-
12-LOX inhibition attenuates platelet aggregation
NEM
-
1 mM, 15% inhibition
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
nicotinoyl chloride
-
-
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
p-hydroxymercuribenzoate
-
1 mM, 75% inhibition
PD146176
-
-
picolinaldehyde
-
-
pyruvoyl chloride
-
-
quercetin
-
-
Renex
-
-
Sn2+
-
3.7 mM, complete inhibition
stylosin
IC50 value of cytotoxicity against PC-3 cells, 24 h, is 0.101 mM
-
Triton X-100
-
-
Tween 20
-
-
Zn2+
-
3.7 mM, complete inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13-hydroperoxy-octadecadienoic acid
-
-
2-arachidonoylglycerol
-
activates 12(S)-HETE production in vivo
ATP
-
2 mM ATP + 1 mM CaCl2 stimulate approximately 2fold
beta-boswellic acid
-
0.03 mM, in the absence of Ca2+
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0009 - 0.0067
4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid
-
0.003 - 0.024
5,8,11,14,17-eicosapentaenoic acid
0.0017 - 0.0078
5S-hydroperoxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
0.0017 - 0.0049
5S-hydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
0.0035 - 0.079
8,11,14-eicosatrienoic acid
0.00095 - 0.011
arachidonate
0.0072 - 0.015
arachidonic acid
7
O2
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.4 - 13
4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid
-
0.13
5S,15S-dihydroperoxyeicosatetraenoic acid
pH 7.5, temperature not specified in the publication
-
0.088 - 1.8
5S-hydroperoxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
1.1 - 9.7
5S-hydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
1.2 - 46
arachidonate
1.4 - 20
arachidonic acid
13.1
O2
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
360 - 14000
4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid
-
0.000011
5S,15S-dihydroperoxyeicosatetraenoic acid
pH 7.5, temperature not specified in the publication
-
51 - 230
5S-hydroperoxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
230 - 5800
5S-hydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
200 - 19000
arachidonate
1.4 - 50
arachidonic acid
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0025
11-thialinoleic acid
-
-
0.017
neodysidenin
pH 8.0, recombinant enzyme
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0007
2,3,4,5-tetrabromo-6-(2,4-dibromophenoxy)phenol
Homo sapiens
-
IC50: 0.0007 mM
0.0041
2,3,4,5-tetrabromo-6-(4,5-dibromo-2-hydroxyphenoxy)phenol
Homo sapiens
-
IC50: 0.0041 mM
0.00041
2,3,5-tribromo-6-(4,5-dibromo-2-hydroxyphenoxy)phenol
Homo sapiens
-
IC50: 0.00041 mM
0.012
2,4-dibromo-6-(2,4-dibromo-6-methoxyphenoxy)phenol
Homo sapiens
-
IC50: 0.012 mM
0.007
2,6-dibromo-4-[1-(3-bromo-4-hydroxyphenyl)-1-methylethyl]phenol
Homo sapiens
-
IC50: 0.007 mM
0.00078
3'-chloro-7,8-dihydroxyisoflavone
Homo sapiens
-
pH 7.5, 22°C
0.0075
3,15-dihydroxy-8,11,13-eicosatrienoic acid
Homo sapiens
-
IC50: 0.0075 mM
0.05
3,4,6,8-tetrabromooxanthren-1-ol
Homo sapiens
-
IC50: 0.05 mM
0.006
3,4,6-tribromo-2-(2,4-dibromophenoxy)phenol
Homo sapiens
-
IC50: 0.006 mM
0.047
3,4-dibromo-2-(5-bromo-2-hydroxyphenoxy)phenol
Homo sapiens
-
IC50: 0.047 mM
0.03
3,6,8-tribromooxanthren-1-ol
Homo sapiens
-
IC50: 0.03 mM
0.0004
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: 0.0004 mM
0.017
4',6,7-trihydroxyisoflavan
Homo sapiens
-
pH 7.5, 22°C
0.0038
4',6,7-trihydroxyisoflavanone
Homo sapiens
-
pH 7.5, 22°C
0.0087
4',6,7-trihydroxyisoflavone
Homo sapiens
-
pH 7.5, 22°C
0.00048
4'-chloro-7,8-dihydroxyisoflavone
Homo sapiens
-
pH 7.5, 22°C
0.0081
4,15-dihydroxy-5,8,11,13-eicosatetraenoic acid
Homo sapiens
-
IC50: 0.0081 mM
0.01
4,4'-propane-2,2-diylbis(2,6-dibromophenol)
Homo sapiens
-
IC50: 0.01 mM
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
0.0008
5,15-dihydroxy-5,8,11,13,17-eicosapentaenoic acid
Homo sapiens
-
IC50: 0.0008 mM
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
-
0.0004
6,17-dihydroxy-4,7,10,13,15,19-eicosahexaenoic acid
Homo sapiens
-
IC50: 0.0004 mM
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
-
0.011
6,7-dihydroxy-3',4'-methylenedioxyisoflavan
Homo sapiens
-
pH 7.5, 22°C
0.1
6,7-dihydroxy-3',4'-methylenedioxyisoflavone
Homo sapiens
-
above, pH 7.5, 22°C
0.015
6,7-dihydroxy-3'-methylisoflavan
Homo sapiens
-
pH 7.5, 22°C
0.014
6,7-dihydroxy-3'-methylisoflavanone
Homo sapiens
-
pH 7.5, 22°C
0.0076
6,7-dihydroxy-4'-methoxyisoflavan
Homo sapiens
-
pH 7.5, 22°C
0.0016
6,7-dihydroxy-4'-methoxyisoflavanone
Homo sapiens
-
pH 7.5, 22°C
0.1
6,7-dihydroxy-4'-methoxyisoflavone
Homo sapiens
-
above, pH 7.5, 22°C
0.0058
6,7-dihydroxy-4'-nitroisoflavone
Homo sapiens
-
pH 7.5, 22°C
0.1
7,8-dihydroxy-3',4'-dimethoxyisoflavan
Homo sapiens
-
above, pH 7.5, 22°C
0.0036
7,8-dihydroxy-3'-methylisoflavone
Homo sapiens
-
pH 7.5, 22°C
0.00062
7,8-dihydroxy-3'-trifluoromethylisoflavone
Homo sapiens
-
pH 7.5, 22°C
0.026
7,8-dihydroxy-4'-methoxyisoflavan
Homo sapiens
-
pH 7.5, 22°C
0.07
7,8-dihydroxy-4'-methylisoflavan
Homo sapiens
-
pH 7.5, 22°C
0.0016
7,8-dihydroxy-4'-methylisoflavone
Homo sapiens
-
pH 7.5, 22°C
0.0064
7,8-dihydroxyisoflavone
Homo sapiens
-
pH 7.5, 22°C
0.00058
alpha-mangostin
Homo sapiens
pH 8.0, recombinant enzyme
0.0023
bestatin 7
Homo sapiens
-
IC50: 0.0023 mM
0.009
dysidenin
Homo sapiens
above, pH 8.0, recombinant enzyme
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
-
0.0049
michellamine B
Homo sapiens
pH 8.0, recombinant enzyme
0.00043 - 0.1
ML355
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
0.075
N-([5-chloro-2-(dimethylamino)-8-hydroxyquinolin-7-yl](furan-2-yl)methyl)acetamide
Homo sapiens
-
value above, pH 8.0, 23°C
0.075
N-([5-chloro-8-hydroxy-2-(piperidin-1-yl)quinolin-7-yl](furan-2-yl)methyl)acetamide
Homo sapiens
-
value above, pH 8.0, 23°C
0.075
N-[(2,5-dichloro-8-hydroxyquinolin-7-yl)(furan-2-yl)methyl]acetamide
Homo sapiens
-
value above, pH 8.0, 23°C
0.075
N-[(4-chloro-1-hydroxynaphthalen-2-yl)(furan-2-yl)methyl]acetamide
Homo sapiens
-
value above, pH 8.0, 23°C
0.002
N-[(5-bromo-8-hydroxyquinolin-7-yl)(furan-2-yl)methyl]acetamide
Homo sapiens
-
pH 8.0, 23°C
0.002
N-[(5-bromo-8-hydroxyquinolin-7-yl)(furan-2-yl)methyl]propanamide
Homo sapiens
-
pH 8.0, 23°C
0.001
N-[(5-bromo-8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]acetamide
Homo sapiens
-
pH 8.0, 23°C
0.014
N-[(5-bromo-8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]propanamide
Homo sapiens
-
pH 8.0, 23°C
0.075
N-[(5-bromofuran-2-yl)(5-chloro-8-hydroxyquinolin-7-yl)methyl]propanamide
Homo sapiens
-
value above, pH 8.0, 23°C
0.003
N-[(5-chloro-8-hydroxy-1,2,3,4,4a,8a-hexahydroquinolin-7-yl)(furan-2-yl)methyl]propanamide
Homo sapiens
-
pH 8.0, 23°C
0.05
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-fluorophenyl)methyl]propanamide
Homo sapiens
-
value above, pH 8.0, 23°C
0.15
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]propanamide
Homo sapiens
-
value above, pH 8.0, 23°C
0.0035
N-[(5-chloro-8-hydroxyquinolin-7-yl)(5-methylthiophen-2-yl)methyl]propanamide
Homo sapiens
-
pH 8.0, 23°C
0.003
N-[(5-chloro-8-hydroxyquinolin-7-yl)(cyclopropyl)methyl]acetamide
Homo sapiens
-
pH 8.0, 23°C
0.0016
N-[(5-chloro-8-hydroxyquinolin-7-yl)(cyclopropyl)methyl]propanamide
Homo sapiens
-
pH 8.0, 23°C
0.025
N-[(5-chloro-8-hydroxyquinolin-7-yl)(furan-2-yl)methyl]-4-methylbenzamide
Homo sapiens
-
value above, pH 8.0, 23°C
0.003
N-[(5-chloro-8-hydroxyquinolin-7-yl)(furan-2-yl)methyl]acetamide
Homo sapiens
-
pH 8.0, 23°C
0.025
N-[(5-chloro-8-hydroxyquinolin-7-yl)(furan-2-yl)methyl]benzamide
Homo sapiens
-
value above, pH 8.0, 23°C
0.001
N-[(5-chloro-8-hydroxyquinolin-7-yl)(furan-2-yl)methyl]propanamide
Homo sapiens
-
pH 8.0, 23°C
0.001
N-[(5-chloro-8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]acetamide
Homo sapiens
-
pH 8.0, 23°C
0.001
N-[(5-chloro-8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]propanamide
Homo sapiens
-
pH 8.0, 23°C
0.15
N-[(5-chloro-8-hydroxyquinolin-7-yl)methyl]acetamide
Homo sapiens
-
value above, pH 8.0, 23°C
0.075
N-[(5-chloro-8-methoxyquinolin-7-yl)(furan-2-yl)methyl]propanamide
Homo sapiens
-
value above, pH 8.0, 23°C
0.005
N-[(5-fluoro-8-hydroxyquinolin-7-yl)(furan-2-yl)methyl]acetamide
Homo sapiens
-
pH 8.0, 23°C
0.002
N-[(5-fluoro-8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]acetamide
Homo sapiens
-
pH 8.0, 23°C
0.0008
N-[(8-hydroxy-5-nitroquinolin-7-yl)(thiophen-2-yl)methyl]propanamide
Homo sapiens
-
pH 8.0, 23°C
0.0034
N-[(8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]propanamide
Homo sapiens
-
pH 8.0, 23°C
0.025
N-[(R)-(5-bromo-8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]acetamide
Homo sapiens
-
pH 8.0, 23°C
0.025
N-[(R)-(5-bromo-8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]propanamide
Homo sapiens
-
pH 8.0, 23°C
0.00043
N-[(S)-(5-bromo-8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]acetamide
Homo sapiens
-
pH 8.0, 23°C
0.00038
N-[(S)-(5-bromo-8-hydroxyquinolin-7-yl)(thiophen-2-yl)methyl]propanamide
Homo sapiens
-
pH 8.0, 23°C
0.0026
N-[1-(5-chloro-8-hydroxyquinolin-7-yl)-2-methylpropyl]acetamide
Homo sapiens
-
pH 8.0, 23°C
0.0012
N-[1-(5-chloro-8-hydroxyquinolin-7-yl)-2-methylpropyl]propanamide
Homo sapiens
-
pH 8.0, 23°C
0.15
N-[1-(5-chloro-8-hydroxyquinolin-7-yl)ethyl]acetamide
Homo sapiens
-
value above, pH 8.0, 23°C
0.05
N-[1-(5-chloro-8-hydroxyquinolin-7-yl)ethyl]propanamide
Homo sapiens
-
value above, pH 8.0, 23°C
0.075
N-[1-(5-fluoro-8-hydroxyquinolin-7-yl)ethyl]acetamide
Homo sapiens
-
value above, pH 8.0, 23°C
0.0012
N-[furan-2-yl(8-hydroxy-5-nitroquinolin-7-yl)methyl]propanamide
Homo sapiens
-
pH 8.0, 23°C
0.000025
NDGA
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.1
neodysidenin
Homo sapiens
above, pH 8.0, recombinant enzyme
0.0051
nordihydroguaiaretic acid
Homo sapiens
-
IC50: 0.0051 mM
0.00021
NSC172033
Homo sapiens
pH 8.0, recombinant enzyme
0.00015
NSC292213
Homo sapiens
pH 8.0, recombinant enzyme
0.00019
NSC617570
Homo sapiens
pH 8.0, recombinant enzyme
0.00044
quercetin
Homo sapiens
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
7.5 - 8.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 8.7
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at
23
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
high expression level of 12-LOX
Manually annotated by BRENDA team
-
induced by a Ca2+ ionophore, from acute myeloid leukemic and acute lymphoid leukemic patients, upregulation of the enzyme, quantitative expression analysis
Manually annotated by BRENDA team
-
primary human aortic smooth muscle cells
Manually annotated by BRENDA team
-
the 12/15-LOX metabolic pathway is increased and correlates with an oxidative imbalance in the Alzheimer‘s disease brain, implying that this enzyme might contribute to the pathogenesis of this neurodegenerative disorder
Manually annotated by BRENDA team
-
12-LOX is overexpressed in a variety of human tumors
Manually annotated by BRENDA team
bone marrow-derived
Manually annotated by BRENDA team
-
umbelical vein endothelial cells and foreskin dermal microvascular endothelial cells
Manually annotated by BRENDA team
-
12-LOX overexpression
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
vascular smooth muscle, the enzyme associates with alpha-actin fibers
Manually annotated by BRENDA team
-
umbilical artery, the enzyme associates with alpha-actin fibers
Manually annotated by BRENDA team
-
prostate stromal cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
primarily associated with cytoplasmic vascular smooth muscle cell muscle fibrils binding to alpha-actin, a component of the cytoplasmic myofilaments, not associated with 12-LO serine or tyrosine phosphorylation, overview, the binding is induced by angiotensin II
Manually annotated by BRENDA team
membrane binding activities of wild-type platelet 12-lipoxygenase and mutant enzymes at pH 7.4, role of the PLAT domain membrane binding, overview
Manually annotated by BRENDA team
additional information
-
subcellular distribution analysis, overview
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
pharmacologic inhibition of 12-LOX in human platelets results in significant attenuation of FcgammaRIIa-mediated aggregation. Activation of the FcgammaRIIa receptor leads to immune-mediated thrombosis, which is often life threatening in patients undergoing heparin-induced thrombocytopenia or sepsis. Inhibiting FcgammaRIIa-mediated activation, e.g. by inhibiting the enzyme 12-LOX, in platelets limits thrombosis and is the principal target for prevention of immune-mediated platelet activation
physiological function
platelet 12(S)-lipoxygenase (12-LOX), a highly expressed oxylipin-producing enzyme in the human platelet, is an essential component of FcgammaRIIa-mediated thrombosis. Platelet enzyme 12-LOX modulates FcgammaRIIa signaling and is essential for FcgammaRIIa-mediated platelet activation. 12-LOX is essential for FcgammaRIIa-induced phospholipase Cgamma2 activity leading to activation of calcium mobilization, Rap1 and protein kinase C activation, and subsequent activation of the integrin aIIbbeta3. 12-LOX regulates dense and a granule secretion in FcgammaRIIa-activated platelets
evolution
mammals (mice, rats, pigs) express 12-lipoxygenating ALOX15 orthologues. 15-lipoxygenating isoforms are found in primates (orangutans, humans), suggesting an evolution of ALOX15 specificity. Other primates (baboons, rhesus monkeys) express 12-lipoxygenating enzymes. Gibbons, which are flanked in evolution by rhesus monkeys (12-lipoxygenating ALOX15) and orangutans (15-lipoxygenating ALOX15), express an ALOX15 ortholog with pronounced dual specificity, an evolution of ALOX15 specificity, which is aimed at optimizing the biosynthetic capacity for antiinflammatory and proresolving lipoxins. Phylogenetic analysis
malfunction
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LX12B_HUMAN
701
0
80356
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
158000
about, recombinant His-tagged wild-type and mutant enzymes, gel filtration
62650
x * 62650, recombinant no-PLAT-mutant, SDS-PAGE
675000
about, recombinant no-PLAT-mutant, gel filtration
76500
2 * 76500, recombinant His-tagged enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 60000-80000, SDS-PAGE
dimer
oligomer
x * 62650, recombinant no-PLAT-mutant, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
low-resolution 16 A structure of enzyme in solution, dynamic light scattering and SAXS analysis of hp-12LOX shows that this enzyme as a whole is stable in the dimeric form, while mutants without PLAT domains associate into larger aggregates
modeling of the protein dimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C7S
site-directed mutagenesis, the mutant shows highly reduced iron content compared to the wild-type enzyme, but exchange of the surface-exposed cysteine alters neither the catalytic activity nor the reaction specificity
F174A/W176A/L183E/L187E/Y191A
quintuple mutant disrupts both the hydrophobic and pi-pi interactions of the dimer interface, generating an 12-LOX monomer
G441A
-
the mutant enzyme G441A converts arachidonic acid to (8S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid and (12R)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid in a 1.4:1 ratio, wild-type enzyme converts arachidonate only to (12R)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid
G441S
-
the mutant enzyme G441A converts arachidonic acid to 8S-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid (major product) and (12R)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid (minor product), wild-type enzyme converts arachidonate only to (12R)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid
G441T
-
inactive mutant enzyme
G441V
-
inactive mutant enzyme
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
L183E/L187E
mutant mostly forms monomers, product ratio of 12S:15S-enantiomer is 78:22, strong decrease in inhibition by ML355
M419T
naturally occuring mutation, the mutant produces more 12-hydroperoxyicosatetraenoate compared to 15-hydroperoxyicosatetraenoate, incontrast to the wild-type, inversed substrate specificity
Q294L
-
relative catalytic activity: 16.1% compared to wild-type 100%
T560M
T594V
naturally occuring mutation, the mutant produces more 12-hydroperoxyicosatetraenoate compared to 15-hydroperoxyicosatetraenoate, incontrast to the wild-type, inversed substrate specificity
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
-
loses appreciable activity when left overnight in an ice bath
4
-
90% loss of activity after 4 h
50
-
3 min, enzyme solubilized with 1% deoxycholate, 20% loss of activity
65
-
3 min, enzyme solubilized with 1% deoxycholate, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-20°C, remains stable for 6 weeks
-
-80°C, 10-20% glycerol
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by one step Ni2+ affinity chromatography, more than 90% pure
-
recombinant His-tagged enzyme
-
recombinant His-tagged isozyme 12-hLO by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Spodoptera frugiperda Sf9 cells by nickel affinity chromatography
to greater than 90% purity
-
using Ni-NTA chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
-
expressed with hexa-His tags
-
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 enzyme
-
expression of His-tagged wild-type and mutant enzymes in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
expression of isozyme 12-hLO as His-tagged enzyme
expression of N-terminally His6-tagged enzyme
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
-
overexpressed as N-terminally, His6-tagged protein
-
sequence comparisons and phylogenetic analysis
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
ALOX12 expression and its metabolite 12(S)-hydroxyeicosatetraenoic acid are significantly increased in the visceral adipose tissue of type 2 diabetes subjects with body mass index of 21. ALOX12 expression positively correlated with expression of inflammatory genes encoding IL-6, IL-12a, CXCL10, and lipocalin-2
an increase of ALOX15B expression during the differentiation of monocytes to macrophages is shown. Stimulation of macrophages with a set of cytokines and with hypoxia reveals that IL-4, IL-13, LPS and hypoxia further increase the ALOX15B mRNA
-
expression of ALOX12 remains on the same level during differentiation from monocyte to macrophage
-
insulin-like growth factor II induces 12-LOX expression and blocks cell cycle progression
-
level of 12-LOX expression is dose-dependently decreased by UVB and UVA-irradiation. Successful psoralen plus ultraviolet A, UVA-photochemotherapy-mediated inhibition of cell growth and inflammation via decreased 12-LOX expression. 15(S)-hydroxyeicosatetraenoic acid, 15-HETrE and 13(S)-hydroxyoctadecadienoic acid (15-LOX metabolites) significantly inhibit insulin-like growth factor II-induced 12-LOX expression
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
blood platelet enzyme 12-LOX modulates FcgammaRIIa signaling and presents a viable therapeutic target in the prevention of immune-mediated thrombosis
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hada, T.; Ueda, N.; Takahashi, Y.; Yamamoto, S.
Catalytic properties of human platelet 12-lipoxygenase as compared with the enzymes of other origins
Biochim. Biophys. Acta
1083
89-93
1991
Bos taurus, Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Flatman, S.; Hurst, J.S.; McDonald-Gibson, R.G.; Jonas, G.E.G.; Slater, T.F.
Biochemical studies on a 12-lipoxygenase in human uterine cervix
Biochim. Biophys. Acta
883
7-14
1986
Homo sapiens
Manually annotated by BRENDA team
Mitchell, P.D.; Hallam, C.; Hemsley, P.E.; Lord, G.H.; Wilkinson, D.
Inhibition of platelet 12-lipoxygenase by hydroxy-fatty acids
Biochem. Soc. Trans.
12
839-841
1984
Homo sapiens
-
Manually annotated by BRENDA team
Wallach, D.P.; Brown, V.R.
A novel preparation of human platelet lipoxygenase. Characteristics and inhibition by a variety of phenyl hydrazones and comparisons with other lipoxygenases
Biochim. Biophys. Acta
663
361-372
1981
Homo sapiens
Manually annotated by BRENDA team
Krieg, P.; Kinzig, A.; Ress-Lschke, M.; Vogel, S.; Vanlandingham, B.; Stephan, M.; Lehmann, W.D.; Marks, F.; Furstenberger, G.
12-Lipoxygenase isoenzymes in mouse skin tumor development
Mol. Carcinog.
14
118-129
1995
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Nie, D.; Tang, K.; Diglio, C.; Honn, K.V.
Eicosanoid regulation of angiogenesis: role of endothelial arachidonate 12-lipoxygenase
Blood
95
2304-2311
2000
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Takahashi, Y.; Reddy, G.R.; Ueda, N.; Yamamoto, S.; Arase, S.
Arachidonate 12-lipoxygenase of platelet-type in human epidermal cells
J. Biol. Chem.
268
16443-16448
1993
Homo sapiens
Manually annotated by BRENDA team
Pratico, D.; Zhukareva, V.; Yao, Y.; Uryu, K.; Funk, C.D.; Lawson, J.A.; Trojanowski, J.Q.; Lee, V.M.
12/15-lipoxygenase is increased in Alzheimer's disease: possible involvement in brain oxidative stress
Am. J. Pathol.
164
1655-1662
2004
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
Chen, C.J.; Huang, H.S.; Chang, W.C.
Depletion of phospholipid hydroperoxide glutathione peroxidase up-regulates arachidonate metabolism by 12(S)-lipoxygenase and cyclooxygenase 1 in human epidermoid carcinoma A431 cells
FASEB J.
17
1694-1696
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
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
Chang, W.C.
Cell signaling and gene regulation of human 12(S)-lipoxygenase expression
Prostaglandins
71
277-285
2003
Homo sapiens
Manually annotated by BRENDA team
Poeckel, D.; Tausch, L.; Kather, N.; Jauch, J.; Werz, O.
Boswellic acids stimulate arachidonic acid release and 12-lipoxygenase activity in human platelets independent of Ca2+ and differentially interact with platelet-type 12-lipoxygenase
Mol. Pharmacol.
70
1071-1078
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, Mus musculus, Mus musculus C57BL/6
Manually annotated by BRENDA team
Weisinger, G.; Limor, R.; Marcus-Perlman, Y.; Knoll, E.; Kohen, F.; Schinder, V.; Firer, M.; Stern, N.
12S-lipoxygenase protein associates with alpha-actin fibers in human umbilical artery vascular smooth muscle cells
Biochem. Biophys. Res. Commun.
356
554-560
2007
Homo sapiens
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 (P18054), 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 (P18054), 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
Chen, F.L.; Wang, X.Z.; Li, J.Y.; Yu, J.P.; Huang, C.Y.; Chen, Z.X.
12-lipoxygenase induces apoptosis of human gastric cancer AGS cells via the ERK1/2 signal pathway
Digest. Dis. Sci.
53
181-187
2008
Homo sapiens
Manually annotated by BRENDA team
Chen, C.J.; Chang, W.C.; Chen, B.K.
Attenuation of c-Jun and Sp1 expression and p300 recruitment to gene promoter confers the trichostatin A-induced inhibition of 12(S)-lipoxygenase expression in EGF-treated A431 cells
Eur. J. Pharmacol.
591
36-42
2008
Homo sapiens
Manually annotated by BRENDA team
Endsley, M.P.; Aggarwal, N.; Isbell, M.A.; Wheelock, C.E.; Hammock, B.D.; Falck, J.R.; Campbell, W.B.; Nithipatikom, K.
Diverse roles of 2-arachidonoylglycerol in invasion of prostate carcinoma cells: location, hydrolysis and 12-lipoxygenase metabolism
Int. J. Cancer
121
984-991
2007
Homo sapiens
Manually annotated by BRENDA team
Aleem, A.M.; Jankun, J.; Dignam, J.D.; Walther, M.; Kuehn, H.; Svergun, D.I.; Skrzypczak-Jankun, E.
Human platelet 12-lipoxygenase, new findings about its activity, membrane binding and low-resolution structure
J. Mol. Biol.
376
193-209
2008
Homo sapiens (P18054), 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
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
Reddy, M.V.; Billa, V.K.; Pallela, V.R.; Mallireddigari, M.R.; Boominathan, R.; Gabriel, J.L.; Reddy, E.P.
Design, synthesis, and biological evaluation of 1-(4-sulfamylphenyl)-3-trifluoromethyl-5-indolyl pyrazolines as cyclooxygenase-2 (COX-2) and lipoxygenase (LOX) inhibitors
Bioorg. Med. Chem.
16
3907-3916
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
Aparoy, P.; Leela, T.; Reddy, R.N.; Reddanna, P.
Computational analysis of R and S isoforms of 12-lipoxygenases: homology modeling and docking studies
J. Mol. Graph. Model.
27
744-750
2009
Homo sapiens (O75342), 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
Mascayano, C.; Nez, G.; Acevedo, W.; Rezende, M.
Binding of arachidonic acid and two flavonoid inhibitors to human 12- and 15-lipoxygenases: A steered molecular dynamics study
J. Mol. Model.
16
1039-1045
2010
Homo sapiens
Manually annotated by BRENDA team
Wuest, S.J.; Crucet, M.; Gemperle, C.; Loretz, C.; Hersberger, M.
Expression and regulation of 12/15-lipoxygenases in human primary macrophages
Atherosclerosis
225
121-127
2012
Homo sapiens
Manually annotated by BRENDA team
Dilly, A.K.; Ekambaram, P.; Guo, Y.; Cai, Y.; Tucker, S.C.; Fridman, R.; Kandouz, M.; Honn, K.V.
Platelet-type 12-lipoxygenase induces MMP9 expression and cellular invasion via activation of PI3K/Akt/NF-kappaB
Int. J. Cancer
133
1784-1791
2013
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, Mus musculus
Manually annotated by BRENDA team
Blazevic, T.; Schwaiberger, A.V.; Schreiner, C.E.; Schachner, D.; Schaible, A.M.; Grojer, C.S.; Atanasov, A.G.; Werz, O.; Dirsch, V.M.; Heiss, E.H.
12/15-Lipoxygenase contributes to platelet-derived growth factor- induced activation of signal transducer and activator of transcription 3
J. Biol. Chem.
288
35592-35603
2013
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Kenyon, V.; Rai, G.; Jadhav, A.; Schultz, L.; Armstrong, M.; Jameson, J.B.; Perry, S.; Joshi, N.; Bougie, J.M.; Leister, W.; Taylor-Fishwick, D.A.; Nadler, J.L.; Holinstat, M.; Simeonov, A.; Maloney, D.J.; Holman, T.R.
Discovery of potent and selective inhibitors of human platelet-type 12- lipoxygenase
J. Med. Chem.
54
5485-5497
2011
Homo sapiens
Manually annotated by BRENDA team
Yeung, J.; Apopa, P.L.; Vesci, J.; Stolla, M.; Rai, G.; Simeonov, A.; Jadhav, A.; Fernandez-Perez, P.; Maloney, D.J.; Boutaud, O.; Holman, T.R.; Holinstat, M.
12-lipoxygenase activity plays an important role in PAR4 and GPVI-mediated platelet reactivity
Thromb. Haemost.
110
569-581
2013
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Yeung, J.; Tourdot, B.E.; Fernandez-Perez, P.; Vesci, J.; Ren, J.; Smyrniotis, C.J.; Luci, D.K.; Jadhav, A.; Simeonov, A.; Maloney, D.J.; Holman, T.R.; McKenzie, S.E.; Holinstat, M.
Platelet 12-LOX is essential for FcgammaRIIa-mediated platelet activation
Blood
124
2271-2279
2014
Mus musculus, Homo sapiens (O75342), Homo sapiens
Manually annotated by BRENDA team
Weisinger, G.; Grafi-Cohen, M.; Hirsh, M.; Knoll, E.; Sharon, O.; Many, A.; Limor, R.; Stern, N.
12S-Lipoxygenase is necessary for human vascular smooth muscle cell survival
Exp. Cell Res.
319
1586-1593
2013
Homo sapiens (P18054), Homo sapiens
Manually annotated by BRENDA team
Ho, X.L.; Liu, J.J.; Loke, W.M.
Plant sterol-enriched soy milk consumption modulates 5-lipoxygenase, 12-lipoxygenase, and myeloperoxidase activities in healthy adults - a randomized-controlled trial
Free Radic. Res.
50
1396-1407
2016
Homo sapiens (P18054)
Manually annotated by BRENDA team
Lieb, D.C.; Brotman, J.J.; Hatcher, M.A.; Aye, M.S.; Cole, B.K.; Haynes, B.A.; Wohlgemuth, S.D.; Fontana, M.A.; Beydoun, H.; Nadler, J.L.; Dobrian, A.D.
Adipose tissue 12/15 lipoxygenase pathway in human obesity and diabetes
J. Clin. Endocrinol. Metab.
99
E1713-E1720
2014
Homo sapiens (P16050), Homo sapiens
Manually annotated by BRENDA team
Rothe, T.; Gruber, F.; Uderhardt, S.; Ipseiz, N.; Roessner, S.; Oskolkova, O.; Blueml, S.; Leitinger, N.; Bicker, W.; Bochkov, V.N.; Yamamoto, M.; Steinkasserer, A.; Schett, G.; Zinser, E.; Kroenke, G.
12/15-Lipoxygenase-mediated enzymatic lipid oxidation regulates DC maturation and function
J. Clin. Invest.
125
1944-1954
2015
Homo sapiens (P16050), Homo sapiens, Mus musculus (P39654), Mus musculus, Mus musculus C57BL/6 (P39654)
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
Pan paniscus, Homo sapiens neanderthalensis, Homo sapiens subsp. 'Denisova', Papio anubis (A0A096P2G1), Macaca mulatta (F7EPQ4), Macaca mulatta, Nomascus leucogenys (G1S6D2), Pan troglodytes (H2QBX9), Pan troglodytes, Oryctolagus cuniculus (P12530), Oryctolagus cuniculus, Homo sapiens (P16050), Pongo pygmaeus (Q5RBE8), Pongo pygmaeus, Pongo abelii (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 (P18054)
-
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 (P18054), 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 (P16050), Homo sapiens (P18054)
Manually annotated by BRENDA team
Tsai, W.C.; Aleem, A.M.; Whittington, C.; Cortopassi, W.A.; Kalyanaraman, C.; Baroz, A.; Iavarone, A.T.; Skrzypczak-Jankun, E.; Jacobson, M.P.; Offenbacher, A.R.; Holman, T.
Mutagenesis, hydrogen-deuterium exchange, and molecular docking investigations establish the dimeric interface of human platelet-type 12-lipoxygenase
Biochemistry
60
802-812
2021
Homo sapiens (P18054), Homo sapiens
Manually annotated by BRENDA team
Leiria, L.O.; Wang, C.H.; Lynes, M.D.; Yang, K.; Shamsi, F.; Sato, M.; Sugimoto, S.; Chen, E.Y.; Bussberg, V.; Narain, N.R.; Sansbury, B.E.; Darcy, J.; Huang, T.L.; Kodani, S.D.; Sakaguchi, M.; Rocha, A.L.; Schulz, T.J.; Bartelt, A.; Hotamisligil, G.S.; Hirshman, M.F.; van Leyen, K.; Goodyear, L.J.; Blueher, M.
12-Lipoxygenase regulates cold adaptation and glucose metabolism by producing the omega-3 lipid 12-HEPE from brown fat
Cell Metab.
30
768-783.e7
2019
Homo sapiens, Mus musculus (P55249), Mus musculus
Manually annotated by BRENDA team
Sarsour, E.H.; Son, J.M.; Kalen, A.L.; Xiao, W.; Du, J.; Alexander, M.S.; OLeary, B.R.; Cullen, J.J.; Goswami, P.C.
Arachidonate 12-lipoxygenase and 12-hydroxyeicosatetraenoic acid contribute to stromal aging-induced progression of pancreatic cancer
J. Biol. Chem.
295
6946-6957
2020
Homo sapiens (P18054), Homo sapiens
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), Homo sapiens
Manually annotated by BRENDA team
Adams, W.; Bhowmick, R.; Bou Ghanem, E.N.; Wade, K.; Shchepetov, M.; Weiser, J.N.; McCormick, B.A.; Tweten, R.K.; Leong, J.M.
Pneumolysin induces 12-lipoxygenase-dependent neutrophil migration during Streptococcus pneumoniae infection
J. Immunol.
204
101-111
2020
Homo sapiens, Mus musculus (P55249)
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 (P16050), Homo sapiens
Manually annotated by BRENDA team