1.13.11.34: arachidonate 5-lipoxygenase
This is an abbreviated version!
For detailed information about arachidonate 5-lipoxygenase, go to the full flat file.
Word Map on EC 1.13.11.34
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1.13.11.34
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cyclooxygenase
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prostaglandin
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leukocyte
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neutrophil
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eicosanoids
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cox-2
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asthma
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indomethacin
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ionophore
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phospholipase
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zileuton
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polymorphonuclear
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thromboxane
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flap
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airway
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peritoneal
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5-hete
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platelet
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eosinophil
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mast
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cysteinyl
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allergic
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edema
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12-lipoxygenase
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histamine
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lta4
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nordihydroguaiaretic
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lipoxygenases
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paf
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ndga
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bronchoconstriction
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5-hydroxyeicosatetraenoic
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asthmatic
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basophil
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platelet-activating
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anaphylaxis
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zymosan
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antigen-induced
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lipoxins
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montelukast
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hetes
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mpges-1
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carrageenan-induced
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a23187-stimulated
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paf-induced
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pro-resolving
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synthesis
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bronchospasm
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medicine
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drug development
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14carachidonic
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pharmacology
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bronchoconstrictors
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ulcerogenic
- 1.13.11.34
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cyclooxygenase
- prostaglandin
- leukocyte
- neutrophil
-
eicosanoids
- cox-2
- asthma
- indomethacin
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ionophore
- phospholipase
- zileuton
-
polymorphonuclear
-
thromboxane
- flap
- airway
- peritoneal
-
5-hete
- platelet
-
eosinophil
-
mast
-
cysteinyl
-
allergic
- edema
-
12-lipoxygenase
- histamine
- lta4
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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
Reaction
Synonyms
5-lipoxygenase, 5-LO, 5-LO1, 5-LOX, 5DELTA-lipoxygenase, 5LO, 5LOX-1, ALOX5, arachidonate 5-LO, arachidonate:oxygen oxidoreductase, arachidonic 5-lipoxygenase, arachidonic acid 5-lipoxygenase, C-5-lipoxygenase, DELTA5-lipoxygenase, H5-LO, leukotriene A4 synthase, leukotriene-A4 synthase, lipoxygenase 15, lipoxygenase 5, lipoxygenase-1, LO-1, LOX-15, LOX-5, LTA synthase, LTA4 synthase, oxygenase, arachidonate, 5-lip-, PMNL 5-lipoxygenase
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Metals Ions
Metals Ions on EC 1.13.11.34 - arachidonate 5-lipoxygenase
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1-oleoyl-2-acetyl-sn-glycerol
Ca2+
Fe
Fe2+
Fe3+
Iron
Mg2+
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
1-oleoyl-2-acetyl-sn-glycerol
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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
1-oleoyl-2-acetyl-sn-glycerol
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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+
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5-lipoxygenase product formation in arachidonic acid-stimulated polymorphonuclear leukocytes is independent of Ca2+. Ca2+ and 5-lipoxygenase phosphorylation seem to be required for arachidonic acid-induced 5-lipoxygenase product formation
Ca2+
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activates, Ca2+ induces the translocation of 5-LO from a soluble compartment to nuclear structures, where 5-LO co-localizes with 5-LO activating protein, FLAP
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
Ca2+
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upon stimulation with calcium ionophore, GFP-5-lipoxygenase translocates to the nuclear envelope allowing it to interact with 5-lipoxygenase activating protein (FLAP) and leukotriene C4 synthase
Ca2+
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Ca2+ is required for 5LO activity, the enzyme contains two Ca2+, full activation is reached at 0.004-0.01 mM Ca2+
Ca2+
5-LOX is recruited to the nuclear membrane upon cellular Ca2+ influx. Calcium binds to allosteric sites in the 5-LOX N-terminal polycystin-1/lipoxygenase/alpha-toxin (PLAT) domain, promoting attachment to the membrane via conserved tryptophan residues that embed into the lipid bilayer
Ca2+
phosphocholine in combination with Ca2+ markedly stimulate the formation of leukotrienes by wild-type 5-LO and C159S/C300S/C416S/C418S mutant, whereas their effect on the 5-LO 3W mutant is small
Ca2+
whilst the catalytic domain of wild-type 5-LO is destabilized by calcium, addition of calcium has no influence on the catalytic domain of 5-LODELTA4
Ca2+
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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
Ca2+
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5-lipoxygenase product formation in arachidonic acid-stimulated polymorphonuclear leukocytes is independent of Ca2+
Ca2+
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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
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the iron acts as electron acceptor and donor, during hydrogen abstraction and peroxide formation
Fe2+
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isoflavones reduce active state iron to ferrous state and prevent the activation of the resting enzyme
Fe2+
a non-heme iron-containing enzyme. LOX catalytic activity depends on the presence of iron in the active site. Iron removal is able to affect the membrane binding properties of the enzyme, molecular dynamics simulations, overview
Fe2+
a nonheme Fe2+ ion coordinated by three polar histidines H372, H550, and H367, the carbonyl group of N554, the carboxylic group of the C-terminal I673, and a water moleculein the active site, overview. On interaction with the active site, the ligands replaces the H2O molecule
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
Fe3+
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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
Fe3+
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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
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wild-type enzyme contains 0.65 mol of iron per mol of enzyme, H372 and H550 constitute two of the iron ligands
Iron
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contains one iron atom per molecule, the native enzyme is in a pseudo-axial high-spin ferric state