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
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polymorphonuclear
-
thromboxane
- flap
- airway
- peritoneal
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5-hete
- platelet
-
eosinophil
-
mast
-
cysteinyl
-
allergic
- edema
-
12-lipoxygenase
- histamine
- lta4
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nordihydroguaiaretic
- lipoxygenases
- paf
- ndga
-
bronchoconstriction
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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
ECTree
1.13.11.34 arachidonate 5-lipoxygenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.13.11.34 - arachidonate 5-lipoxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A603L/Y181A
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
C159S
site-directed mutagenesis, the mutant shows altered susceptibillity to 2-aminothiazole inhibitors compared to the wild-type enzyme
C159S/C300S/C416S/C418S
site-directed mutagenesis, the mutant shows unaltered product synthesis
C240A
site-directed mutagenesis, the mutation renders the enzyme less susceptible to product inactivation
C300S
site-directed mutagenesis, the mutant shows altered susceptibillity to 2-aminothiazole inhibitors compared to the wild-type enzyme
C416S
site-directed mutagenesis, the mutant shows altered susceptibillity to 2-aminothiazole inhibitors compared to the wild-type enzyme
C418S
site-directed mutagenesis, the mutant shows altered susceptibillity to 2-aminothiazole inhibitors compared to the wild-type enzyme
C561A
site-directed mutagenesis, the mutation renders the enzyme less susceptible to product inactivation
D170S/G174N
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E254K
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naturally occuring non-synonymous exonic variant g.760G/A is associated with tuberculosis, genotyping of 1916 sputum-positive patients with pulmonary tuberculosis from Ghana and in 2269 exposed, apparently healthy control individuals, polymorphisms of a variable number of tandem repeats of the ALOX5 promoter and of the exonic non-synonymous variant g.760G>A are analyzed by fragment length determination and fluorescence resonance energy transfer, respectively, and DNA sequencing. The association of the exonic variant is stronger in infections caused by the mycobacterial lineage Mycobacterium africanum West-African 2, overview, distribution of haplotypes, overview
F177A
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
F177A/Y181A
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
F177A/Y181A/H600V
site-directed mutagenesis, the mutant shows about 50% reduced activity compared to the wild-type enzyme
F359W/A424I/N425M/A603I
H367N
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inactive, contains 0.2 mol of iron per mol of protein, compared to 0.86 mol of iron per mol of protein for the wild-type enzyme
H367Q
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inactive, contains 0.5 mol of iron per mol of protein, compared to 0.86 mol of iron per mol of protein for the wild-type enzyme
H367S
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inactive, contains 0.5 mol of iron per mol of protein, compared to 0.86 mol of iron per mol of protein for the wild-type enzyme
S271A
S663A
site-directed mutagenesis, mutation of the phosphorylation site results in impaired cellular 5-LO product formation when transfected cells are selectively activated by arachidonic acid
W102A
W13/75/102A
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triple mutant shows higher total activity than the wild type enzyme
W13A
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the mutation upregulates leukotriene production, the enzyme activity of the mutant 5-LO at low concentrations of phosphatidylcholine (0.005 mg/ml) and arachidonic acid (0.02 mM) is reduced compared to the wild type enzyme
W13A/W75A/W102A
site-directed mutagenesis, the mutant is not activated by Ca2+ and phosphocholine
W75A
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the mutation upregulates leukotriene production, the enzyme activity of the mutant 5-LO at low concentrations of phosphatidylcholine (0.005 mg/ml) and arachidonic acid (0.02 mM) is reduced compared to the wild type enzyme
W75G
site-directed mutagenesis, the mutation causes reduced aggregation and substantially increased thermal stability of the mutant. The mutant still shows Ca2+ interactions. Mutation W75G thermally stabilises the isolated PLAT domain
Y181A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
DELTA1-114
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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
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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
F359W/A424I/N425M/A603I
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oxygenates polyenoic fatty acids containing C11=C12 and C14=C15 double bonds, C20:DELTA11,14,17, C20:DELTA11,14, C18:DELTA9,12, C18:DELTA6,9,12 and C18:DELTA9,12,15 which are not oxygenated by the wild-type enzyme. C20:DELTA5,8,11 that lacks the C11=C12 double bond is not oxygenated
S271A
site-directed mutagenesis, mutation of the phosphorylation site results in impaired cellular 5-LO product formation when transfected cells are selectively activated by arachidonic acid
S271A
site-directed mutagenesis, the mutation changes the localization of the wild-type enzyme to the cytosol
W102A
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the mutation prevents interaction with coactosin-like protein, the mutant shows barely detectable dioxygenase activity
W102A
the mutant shows a diffuse cellular expression, while wild-type 5-LO1 is primarily located in the nucleoplasm
additional information
identification of a protein isoform of human 5-LO that lacks exon 4, termed 5-LODELTA4, identified in cells of lymphoid origin, namely the Burkitt lymphoma cell lines Raji and BL41 as well as primary B and T cells, semiquantitative PCR enzyme expression analysis. Deletion of exon 4 does not shift the reading frame and therefore the mRNA is not subjected to non-mediated mRNA decay. Enzyme mutant 5-LODELTA4 isoform is a stable protein in eukaryotic cells. The isoform itself lacks canonical enzymatic activity as it misses the non-heme iron but it still retains ATP-binding affinity. 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. The enzyme mutant 5-LODELTA4 stimulates wild-type 5-LO activity and product formation at low protein concentrations
additional information
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identification of a protein isoform of human 5-LO that lacks exon 4, termed 5-LODELTA4, identified in cells of lymphoid origin, namely the Burkitt lymphoma cell lines Raji and BL41 as well as primary B and T cells, semiquantitative PCR enzyme expression analysis. Deletion of exon 4 does not shift the reading frame and therefore the mRNA is not subjected to non-mediated mRNA decay. Enzyme mutant 5-LODELTA4 isoform is a stable protein in eukaryotic cells. The isoform itself lacks canonical enzymatic activity as it misses the non-heme iron but it still retains ATP-binding affinity. 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. The enzyme mutant 5-LODELTA4 stimulates wild-type 5-LO activity and product formation at low protein concentrations
additional information
identification of the mutant catalytically inactive DELTA13 isoform (5-LODELTA13) whose transcript lacks exon 13, intracellular localisation and phosphorylation profile of the human 5-lipoxygenase DELTA13 isoform differs from that of its full-length wild-type counterpart. Mutant 5-LODELTA13 inhibits 5-LO product biosynthesis when co-expressed with active wild-type 5-LO1. Mutant 5-LODELTA13 is hyperphosphorylated on S523 and S273 compared to wild-type 5-LO1. Mutant 5-LODELTA13 is cytosolic and concentrated in endoplasmic reticulum-rich perinuclear regions where its effect on LT biosynthesis may occur. Known regulatory factors are retained in the protein sequence of 5-LODELTA13., overview
additional information
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identification of the mutant catalytically inactive DELTA13 isoform (5-LODELTA13) whose transcript lacks exon 13, intracellular localisation and phosphorylation profile of the human 5-lipoxygenase DELTA13 isoform differs from that of its full-length wild-type counterpart. Mutant 5-LODELTA13 inhibits 5-LO product biosynthesis when co-expressed with active wild-type 5-LO1. Mutant 5-LODELTA13 is hyperphosphorylated on S523 and S273 compared to wild-type 5-LO1. Mutant 5-LODELTA13 is cytosolic and concentrated in endoplasmic reticulum-rich perinuclear regions where its effect on LT biosynthesis may occur. Known regulatory factors are retained in the protein sequence of 5-LODELTA13., overview
additional information
in vitro glutathionylation of recombinant purified 5-LO wild-type as well as 5-LO 4C, a mutant where the four surface cysteines are replaced by serines (Cys159/300/416/418Ser), does not alter product synthesis
additional information
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in vitro glutathionylation of recombinant purified 5-LO wild-type as well as 5-LO 4C, a mutant where the four surface cysteines are replaced by serines (Cys159/300/416/418Ser), does not alter product synthesis
additional information
the isolated PLAT W75G interacts with calcium and the Dicer fragment
additional information
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the isolated PLAT W75G interacts with calcium and the Dicer fragment
additional information
the naturally occuring mutant 5-LO catalytically inactive isoforms 5-LODELTA13, 5-LODELTA4 and 5-LOp12, lacking the exons 13, 4 or a part of exon 12, respectively, are identified in B and T cell lines as well as in primary B and T cells and monocytes. Wild-type 5-LO is localized in the nucleus whereas all natural mutant isoforms are located in the cytosol, Despite colocalization with the S271A mutant, the isoforms do not affect leukotriene biosynthesis. Coexpression of the truncated natural isoforms inhibits or stimulates 5-LO-wild-type expression in transiently and stably transfected HEK-293T cells suggesting that the isoforms have other functions than canonical leukotriene biosynthesis
additional information
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the naturally occuring mutant 5-LO catalytically inactive isoforms 5-LODELTA13, 5-LODELTA4 and 5-LOp12, lacking the exons 13, 4 or a part of exon 12, respectively, are identified in B and T cell lines as well as in primary B and T cells and monocytes. Wild-type 5-LO is localized in the nucleus whereas all natural mutant isoforms are located in the cytosol, Despite colocalization with the S271A mutant, the isoforms do not affect leukotriene biosynthesis. Coexpression of the truncated natural isoforms inhibits or stimulates 5-LO-wild-type expression in transiently and stably transfected HEK-293T cells suggesting that the isoforms have other functions than canonical leukotriene biosynthesis
additional information
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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
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
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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
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