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Information on EC 1.13.11.34 - arachidonate 5-lipoxygenase and Organism(s) Mus musculus and UniProt Accession P48999
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1.13.11.34 arachidonate 5-lipoxygenaseSpecify your search results
Word Map
- 1.13.11.34
-
cyclooxygenase
- prostaglandin
- leukocyte
- neutrophil
-
eicosanoids
- cox-2
- asthma
- indomethacin
-
ionophore
- phospholipase
- zileuton
-
polymorphonuclear
-
thromboxane
- flap
- airway
- peritoneal
-
5-hete
- platelet
-
eosinophil
-
mast
-
cysteinyl
-
allergic
- edema
-
12-lipoxygenase
- histamine
- lta4
-
nordihydroguaiaretic
- lipoxygenases
- paf
- ndga
-
bronchoconstriction
-
5-hydroxyeicosatetraenoic
-
asthmatic
-
basophil
-
platelet-activating
- anaphylaxis
- zymosan
-
antigen-induced
-
lipoxins
- montelukast
-
hetes
- mpges-1
-
carrageenan-induced
-
a23187-stimulated
-
paf-induced
-
pro-resolving
- synthesis
- bronchospasm
- medicine
- drug development
-
14carachidonic
- pharmacology
-
bronchoconstrictors
-
ulcerogenic
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
5-lipoxygenase, 5-lox, arachidonate 5-lipoxygenase, lox-5, leukotriene a4 synthase, lta synthase, arachidonic acid 5-lipoxygenase, lipoxygenase 5, 5-lo1, pmnl 5-lipoxygenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-LO
5DELTA-lipoxygenase
-
-
-
-
arachidonic 5-lipoxygenase
-
-
-
-
arachidonic acid 5-lipoxygenase
-
-
-
-
C-5-lipoxygenase
-
-
-
-
DELTA5-lipoxygenase
-
-
-
-
leukotriene A4 synthase
-
-
-
-
leukotriene-A4 synthase
-
-
-
-
LTA synthase
-
-
-
-
oxygenase, arachidonate, 5-lip-
-
-
-
-
5-LO
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
dioxygenation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
arachidonate:oxygen 5-oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY
80619-02-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(6E,8Z,11Z,14Z)-(5S)-hydroperoxyicosa-6,8,11,14-tetraenoate + O2
leukotriene A4
-
-
-
?
arachidonate + O2
(5S,6E,8Z,11Z,14Z)-5-hydroperoxyicosa-6,8,11,14-tetraenoate
-
-
-
-
?
arachidonic acid + O2
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
-
-
-
-
?
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
leukotriene A4 + H2O
-
-
-
?
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
leukotriene A4 + H2O
-
-
-
-
?
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
leukotriene A4 + H2O
-
-
-
?
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
leukotriene A4 + H2O
-
is unstable and metabolized to leukotriene B4
-
?
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
leukotriene A4 + H2O
-
-
is unstable and metabolized to leukotriene B4
-
?
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
leukotriene A4 + H2O
-
is unstable and metabolized to leukotriene B4
-
?
arachidonic acid + O2
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
-
-
-
?
arachidonic acid + O2
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
-
-
-
-
?
arachidonic acid + O2
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
-
-
-
?
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
leukotriene A4 + H2O
-
-
-
-
?
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
leukotriene A4 + H2O
-
-
a conjugated epoxide intermediate in leukotriene biosynthesis, is unstable and enzymatically metabolized to leukotriene B4 or by spontaneous hydrolysis
-
?
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
leukotriene A4 + H2O
-
-
is unstable and metabolized to leukotriene B4 by leukotriene A4 hydrolase, which binds to its specific receptor
-
?
arachidonate + O2
(6E,8Z,11Z,14Z)-(5S)-hydroperoxyicosa-6,8,11,14-tetraenoate
-
-
-
-
?
arachidonate + O2
(6E,8Z,11Z,14Z)-(5S)-hydroperoxyicosa-6,8,11,14-tetraenoate
-
i.e. 5,8,11,14-eicosatetraenoic acid
-
?
arachidonate + O2
(6E,8Z,11Z,14Z)-(5S)-hydroperoxyicosa-6,8,11,14-tetraenoate
-
i.e. 5,8,11,14-eicosatetraenoic acid
-
?
additional information
?
-
5-LO inhibition in obese mice downregulates genes involved in hepatic fatty acid uptake, i.e. L-FABP and FAT/CD36, and normalizes PPARalpha and acyl-CoA oxidase expression, whereas the expression of lipogenic genes, i.e. FASN and SREBP-1c, remains unaltered. The 5-LO inhibition restores hepatic microsomal triglyceride transfer protein, MTP, activity in parallel with a stimulation of hepatic VLDL-TG and ApoB secretion in obese mice, overview
-
-
?
additional information
?
-
-
5-LO inhibition in obese mice downregulates genes involved in hepatic fatty acid uptake, i.e. L-FABP and FAT/CD36, and normalizes PPARalpha and acyl-CoA oxidase expression, whereas the expression of lipogenic genes, i.e. FASN and SREBP-1c, remains unaltered. The 5-LO inhibition restores hepatic microsomal triglyceride transfer protein, MTP, activity in parallel with a stimulation of hepatic VLDL-TG and ApoB secretion in obese mice, overview
-
-
?
additional information
?
-
inhibition of 5-lipoxygenase does not affect cardiac ischemia-reperfusion injury but the post-ischemic inflammatory response, overview
-
-
?
additional information
?
-
-
arachidonate 5-lipoxygenase and leukotriene A5 synthase are identical
-
-
?
additional information
?
-
-
key enzyme in leukotriene biosynthesis, catalyzes the initial steps in the conversion of arachidonic acid to biologically active leukotrienes. Leukotrienes are considered as potent mediators of inflammatory and allergic reactions
-
-
?
additional information
?
-
-
key enzyme in the leukotriene biosynthesis, pathway overview, regulatory mechanisms underlying the expression and control of 5-LO activity, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
arachidonate + O2
(6E,8Z,11Z,14Z)-(5S)-hydroperoxyicosa-6,8,11,14-tetraenoate
-
-
-
-
?
arachidonic acid + O2
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
-
-
-
-
?
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
leukotriene A4 + H2O
-
is unstable and metabolized to leukotriene B4
-
?
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
leukotriene A4 + H2O
-
-
is unstable and metabolized to leukotriene B4
-
?
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
leukotriene A4 + H2O
-
is unstable and metabolized to leukotriene B4
-
?
arachidonic acid + O2
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
-
-
-
?
arachidonic acid + O2
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
-
-
-
-
?
arachidonic acid + O2
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
-
-
-
?
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
leukotriene A4 + H2O
-
-
-
-
?
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
leukotriene A4 + H2O
-
-
a conjugated epoxide intermediate in leukotriene biosynthesis, is unstable and enzymatically metabolized to leukotriene B4 or by spontaneous hydrolysis
-
?
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyeicosa-6,8,11,14-tetraenoate
leukotriene A4 + H2O
-
-
is unstable and metabolized to leukotriene B4 by leukotriene A4 hydrolase, which binds to its specific receptor
-
?
additional information
?
-
5-LO inhibition in obese mice downregulates genes involved in hepatic fatty acid uptake, i.e. L-FABP and FAT/CD36, and normalizes PPARalpha and acyl-CoA oxidase expression, whereas the expression of lipogenic genes, i.e. FASN and SREBP-1c, remains unaltered. The 5-LO inhibition restores hepatic microsomal triglyceride transfer protein, MTP, activity in parallel with a stimulation of hepatic VLDL-TG and ApoB secretion in obese mice, overview
-
-
?
additional information
?
-
-
5-LO inhibition in obese mice downregulates genes involved in hepatic fatty acid uptake, i.e. L-FABP and FAT/CD36, and normalizes PPARalpha and acyl-CoA oxidase expression, whereas the expression of lipogenic genes, i.e. FASN and SREBP-1c, remains unaltered. The 5-LO inhibition restores hepatic microsomal triglyceride transfer protein, MTP, activity in parallel with a stimulation of hepatic VLDL-TG and ApoB secretion in obese mice, overview
-
-
?
additional information
?
-
inhibition of 5-lipoxygenase does not affect cardiac ischemia-reperfusion injury but the post-ischemic inflammatory response, overview
-
-
?
additional information
?
-
-
key enzyme in leukotriene biosynthesis, catalyzes the initial steps in the conversion of arachidonic acid to biologically active leukotrienes. Leukotrienes are considered as potent mediators of inflammatory and allergic reactions
-
-
?
additional information
?
-
-
key enzyme in the leukotriene biosynthesis, pathway overview, regulatory mechanisms underlying the expression and control of 5-LO activity, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1-oleoyl-2-acetyl-sn-glycerol
-
both Ca2+ and glyceride, e.g. 1-oleoyl-2-acetyl-sn-glycerol, might decrease the concentration of lipid hydroperoxide needed for activation of 5-LO, enabling cellular 5-LO product formation at a low redox tone
Ca2+
Fe3+
-
because catalysis by 5-LO requires oxidation of Fe2+ to the active Fe3+ state by lipid hydroperoxides, the redox tone is an important parameter of cellular 5-LO activity
Ca2+
-
binds at the C2-like domain, stimulates and induces enzyme translocation from the nuclear soluble to the envelope fraction, both Ca2+ and glyceride might decrease the concentration of lipid hydroperoxide needed for activation of 5-LO, enabling cellular 5-LO product formation at a low redox tone
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-(3,5-di-tert-butyl-4-hydroxybenzylidene)thiazolidin-2,4-dione
-
effective inhibitor of 5-LOX in vivo
glutathione
-
efficiency of non-redox-type 5-LO inhibitors depends on the presence of glutathione peroxidase activity leading to low hydroperoxide concentration
nordihydroguaiaretic acid
-
reduces oxidative damage of erythrocytes in C57BL/6 Trypanosoma cruzi-infected mice but not in C57BL/6 iNOS-/- infected mice
additional information
-
plant extracts with inhibitory activity on arachidonate 5-lipoxygenase, inhibition of the 5-lipoxygenase pathway is considered to be interesting in the treatment of a variety of inflammatory diseases.
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-LO-activating protein
-
i.e. FLAP, a small permanently membrane-bound protein that is essential for the biosynthesis of leukotrienes from endogenous arachidonic acid. FLAP binds arachidonic acid and is thought to assist in the provision of substrate to 5-LO
-
phosphatidyl choline
-
addition increases catalytic activity of wild-type nzyme by 50%
additional information
-
coactosin-like protein, i.e. CLP, can bind to 5-LO and supports Ca2+-induced 5-LO enzyme activity. CLP seems to function as a chaperone or scaffold for 5-LO, upregulation of 5-LO through the C2-like domain
-
additional information
-
in the mouse 5-lipoxygenase gene there are no GC-boxes in tandem, the core promoter contains only one Sp1/3 binding site
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
arachidonate
-
wild-type, pH and temperature not specified in the publication
0.06
arachidonate
-
mutant DELTA1-114, pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
of young and old mice, comparison of enzyme expression and activity in brain regions, e.g. cortex, hippocampus and cerebellum, overview
increased enzyme activity in obese mice compared to twild-type mice, overview
-
retinal blood vessels of wild-type and mutant mice, diabetic mice show increased expression of leukotriene B4 receptors
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
soluble fraction, translocation to the nuclear envelope upon cell activation by Ca2+
additional information
-
localization of enzyme and reactions, and activation in the cell, overview
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
5-lipoxygenase is involved in the production of matrix metalloproteinase-9
physiological function
malfunction
-
5-LO-/- infected with Trypanosoma cruzi, are more susceptible than C57BL/6 and wild-type 129Sv, showing higher parasitemia and mortality
malfunction
-
Trypanosoma cruzi infection in mice deficient in 5-lipoxygenase (5-LO) results in transiently increased parasitemia, and improved survival rate compared with wild type mice. Myocardia from 5-LO-deficient mice exhibit reduced inflammation, collagen deposition, and migration of CD4+, CD8+, and interferon-gamma-producer cells compared with wild type littermates. Moreover, decreased amounts of tumor necrosis factor-alpha, interferon-gamma, and nitric oxide synthase are found in the hearts of 5-LO-deficient mice
physiological function
-
5-lipoxygenase products may not only play a major role in controlling heart tissue parasitism, i.e., host resistance to acute infection with Trypanosoma cruzi in vivo, but in the event of an infection also play an important part in erythrocyte oxidative stress, an NO-dependent effect. 5-lipoxygenase metabolites increase lipid peroxidation levels in erythrocytes during the early phase of murine Trypanosoma cruzi infection, but do not participate in the development of anemia, thrombocytopenia or leukopenia in Trypanosoma cruzi-infected mice
physiological function
-
5-lipoxygenase is a key determinant of acute myocardial inflammation and mortality during Trypanosoma cruzi infection
physiological function
-
5-lipoxygenase plays a pivotal role in atherogenesis and is involved in plaque stability
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LOX5_MOUSE
674
0
77967
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA1-114
-
D114 truncation mutant shows 6.8% residual activity compared to wild-type, Km (arachidonate) increased compared to wild-type. Vmax: 9.3% compared to wild-type (100%). Addition of phosphatidyl choline or Ca2+ increases catalytic activity only by 11% compared to 50% in wild-type. Truncated mutant exhibits impaired membrane binding properties
DELTA1-125
-
I125 truncation mutant shows 1.8% residual activity compared to wild-type, addition of phosphatidyl choline or Ca2+ increases catalytic activity only by 11% compared to 50% in wild-type. Truncated mutant exhibits impaired membrane binding properties
additional information
additional information
construction of enzyme-deficient knockout mice, 5-LOX deficient and wild-type mice show no significant difference in infarct size after 30 min of coronary artery ligation and 24 h of reperfusion, but neutrophil infiltration as well as tumor necrosis factor expression are increased in 5-lipoxygenase-deficient mice, overview
additional information
-
5-LO-deficient mice show an inhibition of diabetes-induced acellular capillary formation in retina, and show reduced leukostasis and superoxide generation, diabetic enzyme-deficient mice show suppression of NF-kappaB expression, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
stimulation of J774A.1 cells with 0.01 mM acrolein for 4-24 h leads to increased 5-LO expression through activation of the ERK pathway. Acrolein-induced 5-LO expression is inhibited in a dose-dependent manner by pretreatment with AG1478, but not by pretreatment with AG1295
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
the enzyme is an emerging target in obesity, insulin resistance, and artherosclerosis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shimizu, T.; Izumi, T.; Seyama, Y.; Tadokoro, K.; Radmark, O.
Characterization of leukotriene A4 synthase from murine mast cells: evidence for its identity to arachidonate 5-lipoxygenase
Proc. Natl. Acad. Sci. USA
83
4175-4179
1986
Mus musculus
Radmark, O.
Arachidonate 5-lipoxygenase
Prostaglandins
68-69
211-234
2002
Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus, Solanum tuberosum, Sus scrofa
Schneider, I.; Bucar, F.
Lipoxygenase inhibitors from natural plant sources. Part 1: Medicinal plants with inhibitory activity on arachidonate 5-lipoxygenase and 5-lipoxygenase/cyclooxygenase
Phytother. Res.
19
81-102
2005
Bos taurus, Cavia porcellus, Glycine max, Helianthus tuberosus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Son, M.J.; Moon, T.C.; Lee, E.K.; Son, K.H.; Kim, H.P.; Kang, S.S.; Son, J.K.; Lee, S.H.; Chang, H.W.
Naturally occurring biflavonoid, ochnaflavone, inhibits cyclooxygenases-2 and 5-lipoxygenase in mouse bone marrow-derived mast cells
Arch. Pharm. Res.
29
282-286
2006
Mus musculus
Gubitosi-Klug, R.A.; Talahalli, R.; Du, Y.; Nadler, J.L.; Kern, T.S.
5-Lipoxygenase, but not 12/15-lipoxygenase, contributes to degeneration of retinal capillaries in a mouse model of diabetic retinopathy
Diabetes
57
1387-1393
2008
Mus musculus, Mus musculus C57BL/6
Adamek, A.; Jung, S.; Dienesch, C.; Laser, M.; Ertl, G.; Bauersachs, J.; Frantz, S.
Role of 5-lipoxygenase in myocardial ischemia-reperfusion injury in mice
Eur. J. Pharmacol.
571
51-54
2007
Mus musculus (P48999)
Lopez-Parra, M.; Titos, E.; Horrillo, R.; Ferre, N.; Gonzalez-Periz, A.; Martinez-Clemente, M.; Planaguma, A.; Masferrer, J.L.; Arroyo, V.; Claria, J.
Regulatory effects of arachidonate 5-lipoxygenase on hepatic MTP activity and VLDL-TG and ApoB secretion in obese mice
J. Lipid Res.
49
2513-2523
2008
Mus musculus (P48999), Mus musculus, Mus musculus C57/BL6J (P48999)
Chinnici, C.M.; Yao, Y.; Pratico, D.
The 5-lipoxygenase enzymatic pathway in the mouse brain: Young versus old
Neurobiol. Aging
28
1457-1462
2007
Mus musculus (P48999), Mus musculus, Mus musculus C57BL/6 (P48999)
Radmark, O.; Werz, O.; Steinhilber, D.; Samuelsson, B.
5-Lipoxygenase: regulation of expression and enzyme activity
Trends Biochem. Sci.
32
332-341
2007
Mus musculus, Rattus norvegicus, Homo sapiens (P09917)
Borges, C.L.; Cecchini, R.; Tatakihara, V.L.; Malvezi, A.D.; Yamada-Ogatta, S.F.; Rizzo, L.V.; Pinge-Filho, P.
5-Lipoxygenase plays a role in the control of parasite burden and contributes to oxidative damage of erythrocytes in murine Chagas disease
Immunol. Lett.
123
38-45
2009
Mus musculus
Radmark, O.; Samuelsson, B.
5-Lipoxygenase: mechanisms of regulation
J. Lipid Res.
50 Suppl
S40-S45
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Choi, J.H.; Jeon, H.J.; Park, J.G.; Sonn, S.K.; Lee, M.R.; Lee, M.N.; You, H.J.; Kim, G.Y.; Kim, J.H.; Lee, M.H.; Kwon, O.S.; Nam, K.H.; Kim, H.C.; Jeong, T.S.; Lee, W.S.; Oh, G.T.
Anti-atherogenic effect of BHB-TZD having inhibitory activities on cyclooxygenase and 5-lipoxygenase in hyperlipidemic mice
Atherosclerosis
212
146-152
2010
Mus musculus
Pavanelli, W.R.; Gutierrez, F.R.; Mariano, F.S.; Prado, C.M.; Ferreira, B.R.; Teixeira, M.M.; Canetti, C.; Rossi, M.A.; Cunha, F.Q.; Silva, J.S.
5-Lipoxygenase is a key determinant of acute myocardial inflammation and mortality during Trypanosoma cruzi infection
Microbes Infect.
12
587-597
2010
Mus musculus
Kim, C.E.; Lee, S.J.; Seo, K.W.; Park, H.M.; Yun, J.W.; Bae, J.U.; Bae, S.S.; Kim, C.D.
Acrolein increases 5-lipoxygenase expression in murine macrophages through activation of ERK pathway
Toxicol. Appl. Pharmacol.
245
76-82
2010
Mus musculus
Walther, M.; Hofheinz, K.; Vogel, R.; Roffeis, J.; Kuehn, H.
The N-terminal beta-barrel domain of mammalian lipoxygenases including mouse 5-lipoxygenase is not essential for catalytic activity and membrane binding but exhibits regulatory functions
Arch. Biochem. Biophys.
516
1-9
2011
Mus musculus
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