HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 1.13.11.33 - arachidonate 15-lipoxygenase
for references in articles please use BRENDA:EC1.13.11.33
Word Map on EC 1.13.11.33
- 1.13.11.33
- lipoxygenases
-
15-hete
-
eicosanoids
-
polyunsaturated
-
leukotriene
-
12-lipoxygenase
-
15s-hydroxyeicosatetraenoic
-
lipoxins
-
cyclooxygenases
-
hetes
-
nordihydroguaiaretic
- alox15b
-
lipid-peroxidating
- 12/15-lipoxygenase
- ndga
-
leukocyte-type
- medicine
-
platelet-type
-
13-s-hydroxyoctadecadienoic
- drug development
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.13.11.33
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
arachidonate 15-lipoxygenase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
important role of Leu597 in the mechanism of lipoxygenases
-
arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
the reaction proceeds via hydrogen abstraction, peroxide cleavage, radical rearrangement, and epoxide formation. To initiate the reaction the ferrous LOX is first activated by peroxide-dependent oxidation to a ferric form. The lipohydroperoxidase activity is initiatedwhen a lipid hydroperoxide (ROOH) is bound at the active site of the enzyme. The enzyme then catalyzes a homolytic cleavage of the hydroperoxy bond, which leads to the formation of an oxygen-centered alkoxy radical, a hydroxyl and oxidizes the ferrous iron to a ferric form. Then the enzyme binds a linoleic acid molecule (or an alterative reductant such as guaiacol) and releases a carbon-centered linoleic radical. This reaction reduces the ferric LOX back to its ferrous form to start the next catalytic cycle. The released radical intermediates may then initiate free radical secondary reactions leading to the formation of mixed oxygenated and non-oxygenated linoleic acid dimer
-
arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
the reaction proceeds via hydrogen abstraction, peroxide cleavage, radical rearrangement, and epoxide formation. To initiate the reaction the ferrous LOX is first activated by peroxide-dependent oxidation to a ferric form. The lipohydroperoxidase activity is initiatedwhen a lipid hydroperoxide (ROOH) is bound at the active site of the enzyme. The enzyme then catalyzes a homolytic cleavage of the hydroperoxy bond, which leads to the formation of an oxygen-centered alkoxy radical, a hydroxyl and oxidizes the ferrous iron to a ferric form. Then the enzyme binds a linoleic acid molecule (or an alterative reductant such as guaiacol) and releases a carbon-centered linoleic radical. This reaction reduces the ferric LOX back to its ferrous form to start the next catalytic cycle. The released radical intermediates may then initiate free radical secondary reactions leading to the formation of mixed oxygenated and non-oxygenated linoleic acid dimer
-
arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
the reaction proceeds via hydrogen abstraction, peroxide cleavage, radical rearrangement, and epoxide formation. To initiate the reaction the ferrous LOX is first activated by peroxide-dependent oxidation to a ferric form. The lipohydroperoxidase activity is initiatedwhen a lipid hydroperoxide (ROOH) is bound at the active site of the enzyme. The enzyme then catalyzes a homolytic cleavage of the hydroperoxy bond, which leads to the formation of an oxygen-centered alkoxy radical, a hydroxyl and oxidizes the ferrous iron to a ferric form. Then the enzyme binds a linoleic acid molecule (or an alterative reductant such as guaiacol) and releases a carbon-centered linoleic radical. This reaction reduces the ferric LOX back to its ferrous form to start the next catalytic cycle. The released radical intermediates may then initiate free radical secondary reactions leading to the formation of mixed oxygenated and non-oxygenated linoleic acid dimer
-
arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
the reaction proceeds via hydrogen abstraction, peroxide cleavage, radical rearrangement, and epoxide formation. To initiate the reaction the ferrous LOX is first activated by peroxide-dependent oxidation to a ferric form. The lipohydroperoxidase activity is initiatedwhen a lipid hydroperoxide (ROOH) is bound at the active site of the enzyme. The enzyme then catalyzes a homolytic cleavage of the hydroperoxy bond, which leads to the formation of an oxygen-centered alkoxy radical, a hydroxyl and oxidizes the ferrous iron to a ferric form. Then the enzyme binds a linoleic acid molecule (or an alterative reductant such as guaiacol) and releases a carbon-centered linoleic radical. This reaction reduces the ferric LOX back to its ferrous form to start the next catalytic cycle. The released radical intermediates may then initiate free radical secondary reactions leading to the formation of mixed oxygenated and non-oxygenated linoleic acid dimer
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dioxygenation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
arachidonate:oxygen 15-oxidoreductase
The product is rapidly reduced to the corresponding 15S-hydroxy compound.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
82249-77-2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
639238, 657880, 658263, 658269, 659680, 685512, 685546, 685558, 688469, 702247, 702550, 712218, 727161
-
-
-
639237, 639240, 639241, 639243, 639245, 639246, 639247, 639248, 639249, 639250, 639252, 639256, 639258, 639260, 639261, 639262, 639264, 639265, 639266, 639267, 657993, 658944, 659222, 659680, 660365, 671247, 672376, 672543, 672899, 672902, 673030, 674995, 675201, 675909, 675970, 676154, 676263, 676923, 676925, 676927, 677081, 677239, 685338, 685584, 686173, 688159, 688509, 688751, 701633, 701642, 701974, 701977, 701978, 701989, 702324, 702344, 702435, 703002, 703235, 703628, 703699, 704066, 704067, 706032, 706579, 706877, 712712, 726871, 727878, 728663
-
-
two human isozymes: platelet 12-hLO, reticulocyte 15-hLO-1, and epithelial 15-hLO-2
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
gene ALOX15 encodes for human 15-LOX type 1 and murine 12/15-LOX. Although the encoded enzymes display slightly different specificities (15- versus 12-lipoxygenating activity), these proteins represent evolutionary and functionally closely-related enzymes that share a high degree of sequence similarity. Of note, these 12/15LOXs that are encoded by the ALOX15 genes have separated from other LOXs early during evolution, although they share close biochemical properties with other LOXs such as ALOX12 or ALOX15B
evolution
-
gene ALOX15 encodes for human 15-LOX type 1 and murine 12/15-LOX. Although the encoded enzymes display slightly different specificities (15- versus 12-lipoxygenating activity), these proteins represent evolutionary and functionally closely-related enzymes that share a high degree of sequence similarity. Of note, these 12/15LOXs that are encoded by the ALOX15 genes have separated from other LOXs early during evolution, although they share close biochemical properties with other LOXs such as ALOX12 or ALOX15B
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
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
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
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
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
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
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
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
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
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
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
-
when 15-LOX-1 activity is knocked down by siRNA, the induction of MIP-1alpha, RANTES, and IP-10 is significantly attenuated
malfunction
-
streptozotocin (STZ)-induced diabetic mice show upregulated expression of 12/15-LOX and inflammatory cytokines such as tumor necrosis factor (TNF)-alpha and nuclear factor (NF)-kappaB in diabetic hearts. Disruption of 12/15-LOX significantly improves STZ-induced cardiac dysfunction and fibrosis. Deletion of 12/15-LOX inhibits the increases of TNF-alpha and NF-kappaB as well as the production of STZ-induced reactive oxygen species in the heart. Administration of N-acetylcysteine in diabetic mice prevents STZ-induced cardiac fibrosis. Neonatal cultured cardiomyocytes exposed to high glucose conditions induce the expression of 12/15-LOX as well as TNF-alpha, NF-kappaB, and collagen markers. These increases are inhibited by treatment of the 12/15-LOX inhibitor. Disruption of 12/15-LOX reduces inflammation, oxidative stress, and fibrosis in the diabetic heart, thereby improving systolic dysfunction. Disruption of 12/15-LOX decreases cardiac inflammation induced by hyperglycemia
malfunction
-
deletion of 12/15-LO negates endothelial tight junctions disruption and monocyte adhesion caused by the high-fat diet
malfunction
-
Alox15 deletion impaired LSC function by affecting cell division and apoptosis, leading to an eventual depletion of leukemia stem cells. Chemical inhibition of enzyme 15-LO function impairs leukemia stem cell function and attenuates chronic myeloid leukemia in mice. The defective chronic myeloid leukemia phenotype in Alox15-deficient animals is rescued by depleting the gene encoding P-selectin, which is upregulated in Alox15-deficient animals. Both deletion and overexpression of P-selectin affects the survival of leukemia stem cells. Loss of Alox15 causes a functional defect in leukemia stem cells
malfunction
-
disruption of normal 12- and 15-LO function by the inflammatory obese condition promotes adipocyte dysfunction and overall metabolic disease including insulin resistance and diabetes
malfunction
-
deletion of 12/15-LO negates endothelial tight junctions disruption and monocyte adhesion caused by the high-fat diet; streptozotocin (STZ)-induced diabetic mice show upregulated expression of 12/15-LOX and inflammatory cytokines such as tumor necrosis factor (TNF)-alpha and nuclear factor (NF)-kappaB in diabetic hearts. Disruption of 12/15-LOX significantly improves STZ-induced cardiac dysfunction and fibrosis. Deletion of 12/15-LOX inhibits the increases of TNF-alpha and NF-kappaB as well as the production of STZ-induced reactive oxygen species in the heart. Administration of N-acetylcysteine in diabetic mice prevents STZ-induced cardiac fibrosis. Neonatal cultured cardiomyocytes exposed to high glucose conditions induce the expression of 12/15-LOX as well as TNF-alpha, NF-kappaB, and collagen markers. These increases are inhibited by treatment of the 12/15-LOX inhibitor. Disruption of 12/15-LOX reduces inflammation, oxidative stress, and fibrosis in the diabetic heart, thereby improving systolic dysfunction. Disruption of 12/15-LOX decreases cardiac inflammation induced by hyperglycemia
-
metabolism
-
shifting linoleic acid metabolism from 15-LOX-1 to COX-2 is procarcinogenic
metabolism
-
cardiac 12/15-LOX pathway induced by high glucose condition increases the expression of cardiac inflammation in vitro
physiological function
-
15-LOX-1 induces chemokine expression in A549 cells. Increased expression and activity of 15-LOX-1 in lung epithelial cells is a proinflammatory event in the pathogenesis of asthma and other inflammatory lung disorders. 15-LOX-1 overexpression results in upregulation of MIP-1alpha, MIP11beta, and RANTES, in increased migration of immature dendritic cells and of activated T cells and increases chemotaxis of mast cells. 15-LOX-1 ectopic expression upregulates NF-kappaB activity
physiological function
-
high levels of 15LO1 activity can contribute to the increases of MUC5AC observed in asthma
physiological function
-
12/15LO activity in the vessel wall contributes to atherogenesis by impairing the macrophage ATP-binding cassette transporter G1 cholesterol efflux pathway. 12/15LO activity reduces high density lipoprotein-mediated cholesterol efflux, ATP-binding cassette transporter G1 cellular expression. 12/15LO activity does not affect ATP-binding cassette transporter G1 mRNA expression
physiological function
-
overexpression of human 15-LO-1 in RAW macrophages promotes reverse cholesterol transport through increased cholesteryl ester hydrolysis and ABCA1-mediated cholesterol efflux
physiological function
-
15-lipoxygenases may have chondroprotective properties by reducing metalloproteinase-1 and -13 expression. Their respective metabolites, 13(S)-hydroxy octadecadienoic and 15(S)-hydroxyeicosatetraenoic acids, suppress interleukin-1beta-induced metalloproteinase-1 and -13 expression in a PPARgamma-dependent pathway
physiological function
-
macrophages that overexpress 15-LOX-2 show increased secretion of chemokine ligands CXCL10 and CCL2 after 24h incubation. Preconditioned medium from 15-LOX-2-overexpressing cells increases T cell migration, the expression of T cell activation marker CD69 and surface expression of chemokine receptor CXCR3, the CXCL10 chemokine ligand. Increased expression of 15-LOX-2 induced by hypoxia may participate in T cell recruitment in diseases such as atherosclerosis
physiological function
-
lower degree of motional flexibility in aqueous solutions than mammalian isozymes
physiological function
-
high degree of motional flexibility and a high membrane binding affinity
physiological function
-
radiation-induced upregulation of 15-LOX-2 results in significant induction of apoptosis in head-and-neck cancer cells and and enhances killing effect of radiotherapy in head-and-neck cancer. The enzyme inhibits tumor growth through the effect of its main metabolite 15(S)-hydroxyeicosatetranoic acid on PPARgamma signaling pathway
physiological function
-
15-LO-1 plays active roles in vascular remodeling, the progression of atherosclerosis and angiogenesis. The PC-3 prostate cancer cell line, which overexpresses 15-LO-1, secretes high levels of vascular endothelial growth factor and enhances tumor growth and angiogenesis as compared with the parental PC-3 cell lines. Angiogenesis and tumor formation is inhibited in transgenic mice overexpressing 15-LO-1 in endothelial cells under the control of preproendothelin promoter. Potential role of 15-LO-1 in regulating endothelium-derived NO, the expression level and activity of 15-LO-1 in endothelial cells may act as a potential NO barometer by modulating the level of eNOS enzyme and bioactive free NO in endothelial cells. 15-LO-1 in human endothelial cells can inhibit angiogenesis and vascular permeability by removing free NO, and its activity can in turn be modulated by the cytoplasmic NO level
physiological function
-
is a regulator of angiogenesis, antiangiogenic action in skeletal muscle system. 15-LO-1 significantly decreases all angiogenic effects induced by vascular endothelial growth factor-A and placental growth factor, including capillary perfusion, vascular permeability, vasodilatation, and the increase in capillary number
physiological function
-
the expression of 15-lipoxygenase-1 and the putative formation of eoxins by Hodgkin Reed-Sternberg cells in vivo are likely to contribute to the inflammatory features of Hodgkin lymphoma
physiological function
-
15-LOX metabolites (15(S)-hydroxyeicosatetraenoic acid, 15-hydroxyeicosatrienoic acid or 13(S)-hydroxyoctadecadienoic acid) can inhibit insulin-like growth factor II-induced 12-LOX expression and keratinocytes proliferation
physiological function
-
12/15-LOX is a critical mediator of the chronic type 1 inflammatory response. Evolution of the immune response to Toxoplasma gondii is accompanied by an increasing requirement for 12/15-LOX mediated signaling. Although 12/15-LOX deficient mice are resistant to acute Toxoplasma gondii infection, 80% of 12/15-LOX-deficient mice die during chronic toxoplasmosis, compared to no deaths in wild-type controls. The enhanced susceptibility of 12/15-LOX-deficient mice to chronic toxoplasmosis is associated with reduced production of IL-12 and gamma interferon (IFN-gamma) that is not evident during acute infection. Ex vivo IFN-gamma production by 12/15-LOX-deficient splenocytes can be rescued by the addition of recombinant IL-12. 12/15-LOX does not play a role in macrophage killing of Toxoplasma gondii in vitro
physiological function
-
15-LOX-1 induces phosphorylation of tumor suppressor p53 independent of enzymatic activity. HCT-116 cells transiently transfected with either native or mutant 15-LOX-1 show an increase in p53 phosphorylation and an increase in the expression of downstream genes. 15-LOX-1 interacts with, and binds to, DNA-dependent protein kinase, which causes an approximate 3fold enhancement in kinase activity, resulting in increased p53 phosphorylation at Ser15
physiological function
-
15-LOX-2 increases cell cycle arrest at G0/G1 phase. Injected into athymic nu/nu mice, prostate cancer cells with 15-LOX-2 expression can still form palpable tumors without significant changes in tumorigenicity. But, the tumors with 15-LOX-2 expression grow significantly slower than those derived from vector controls and are kept dormant for a long period of time. Increase in cell death in tumors derived from prostate cancer cells with 15- LOX-2 expression. 15-LOX-2 suppresses vascular endothelial growth factor A gene expression and sustains tumor dormancy in prostate cancer
physiological function
-
endogenous 12/15-LOX defines the resident peritoneal macrophage population and regulates both the recruitment of monocytes/peritoneal macrophage and cytokine response to bacterial products in vivo
physiological function
-
12/15LO expression increases chemokine production. 12/15LO mediates early stages of adipose tissue inflammation and whole body insulin resistance induced by high fat feeding. Adipose tissue from high fat diet-fed 12/15LO KO mice is not infiltrated by macrophages and does not display any increase in the inflammatory markers compared to adipose tissue from normal chow-fed mice. 12/15LO KO mice exhibit no high fat diet-induced change in insulin-stimulated glucose disposal rate or hepatic glucose output. Insulin-stimulated Akt phosphorylation in muscle tissue from high fat diet-fed mice is significantly greater in 12/15LO KO mice than in wild-type mice
physiological function
-
pathophysiological role of the enzyme in airway inflammation and atherosclerosis. Role in cell differentiation and importance for maturation of erythrocytes and degradation of cell organells. Role in neoplasia such as prostate cancer and colon carcinoma cells
physiological function
-
pathophysiological role of the enzyme in respiratory inflammation. Mice deficient of 12/15-LO have an attenuated allergic airway inflammation compared to wild type controls
physiological function
-
15-LOX-1 promotes mitogenic response to epidermal growth factor in fibroblasts and NaBT-induced apoptosis in colon cancer cells. Non-steroidal anti-inflammatory drugs-induced apoptosis mediated by 15-LOX-1/GATA-6 in colon cancer
physiological function
-
inhibits tumour growth and metastasis. Enzyme promotes atherosclerosis and can inhibit growth and spread of lung (Lewis lung carcinoma model) and breast (mouse mammary adenocarcinoma model) cancer cells
physiological function
-
high levels of 15LO1 interact with PEBP1 to displace Raf-1 and sustain MAPK/ERK activation
physiological function
enzyme LoxA is a poor catalyst against phosphoester fatty acids, suggesting that LoxA is not involved in membrane decomposition. LoxA also does not react with 5- or 15-HETEs, indicating poor involvement in lipoxin production. The level of LoxA expression is increased when Pseudomonas aeruginosa undergoes the transition to a biofilm mode of growth, but LoxA is not required for biofilm growth on abiotic surfaces. LoxA does appear to be required for biofilm growth in association with the host airway epithelium, suggesting a role for LoxA in mediating bacterium-host interactions during colonization
physiological function
-
isozyme 15-LOX-2 reaction in intact cells: Ca2+ concentrations in the cell increase in response to stress. The Ca2+ binds to the PLAT domain of 15-LOX-2, resulting in a translocation from the cytosol to the membrane. 15-LOX-2 then binds its substrate arachidonate and oxygenates it to form (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate, 15-HpETE. 15-HpETE is further metabolized by downstream enzymes to form lipoxins, which initiate the resolution of inflammation
physiological function
-
12/15-LOX is implicated in the pathogenesis of multiple chronic inflammatory diseases, and its physiologic functions seem to include potent immune modulatory properties that physiologically contribute to the resolution of inflammation and the clearance of inflammation-associated tissue damage. 12/15-LOXs are also involved in the synthesis of lipoxins, which likewise act as anti-inflammatory, pro-resolving mediators. Inflammatory eicosanoids are produced by eosinophils in a 12/15-LOX dependent manner. Docosahexaenoic acid (DHA) is a further substrate of 12/15-LOX. The oxidation of DHA leads to the production of 17S-hydroxy-DHA, an anti-inflammatory mediator, which can be further metabolized into highly active and potent anti-inflammatory resolvins and protectins. 12/15-LOX can metabolize not only free PUFAs, but also PUFAs esterified to membrane-bound phospholipids as well as PUFAs within cholesterol esters. 12/15-LOX-derived mediators as regulators of inflammation, role of 12/15-LOX during inflammation, detailed overview. 12/15-LOX activity in residentmacrophages interferes with theMFG-E8-dependent uptake of apoptotic cells (ACs) by inflammatory, immune-competent phagocytes and thereby fosters the non-immunogenic clearance of ACs, whereas 12/15-LOX-derived lipoxins directly increase the non-inflammatory uptake of dying cells. Possible role of 12/15-LOX in atherosclerosis
physiological function
-
roles of arachidonate 15-lipoxygenase in the clearance of dying adipocytes by adipose tissue macrophages, the Alox15 activation in adipose tissue macrophages functions as a mechanism of non-inflammatory removal of dying adipocytes, overview. Alox15 is required for efferocytosis of apoptotic adipocytes by macrophages in vitro. Alox15 can generate peroxisome proliferatoractivated receptor gamma (PPARgamma) ligands, including 13-HODE and 9-HODE in macrophages after CL316243 treatment. Alox15 is required for differentiation of adipocyte progenitors in beta3-adrenergic stimulation-induced adipose tissue remodeling
physiological function
-
cardiac 12/15-LOX-induced inflammation and oxidative stress are involved in the development of diabetic cardiomyopathy. 12/15-LOX induces cardiac oxidative stress in the diabetic heart
physiological function
-
lipoxygenases (LOX) form a family of lipid peroxidizing enzymes, which are implicated in a number of physiological processes and in the pathogenesis of inflammatory, hyperproliferative and neurodegenerative diseases. Physiological roles of ALOX15, detailed overview
physiological function
-
lipoxygenases (LOX) form a family of lipid peroxidizing enzymes, which are implicated in a number of physiological processes and in the pathogenesis of inflammatory, hyperproliferative and neurodegenerative diseases. Physiological roles of ALOX15, detailed overview
physiological function
-
lipoxygenases (LOX) form a family of lipid peroxidizing enzymes, which are implicated in a number of physiological processes and in the pathogenesis of inflammatory, hyperproliferative and neurodegenerative diseases. Physiological roles of ALOX15, detailed overview
physiological function
-
lipoxygenases (LOX) form a family of lipid peroxidizing enzymes, which are implicated in a number of physiological processes and in the pathogenesis of inflammatory, hyperproliferative and neurodegenerative diseases. Physiological roles of ALOX15, detailed overview
physiological function
-
12/15-lipoxygenase plays a role in atherosclerosis. 15(S)-hydroxyeicosatetraenoic acid (15(S)-HETE), the major 12/15-LO metabolite of arachidonic acid, induces endothelial barrier permeability via Src and Pyk2-dependent zonula occluden (ZO)-2 tyrosine phosphorylation and its dissociation from the tight junction complexes. 15(S)-HETE also stimulates macrophage adhesion to the endothelial monolayer in Src and Pyk2-dependent manner. Exposure of arteries from wild-type mice to arachidonate or 15(S)-HETE leads to Src-Pyk2-dependent ZO-2 tyrosine phosphorylation, tight junction disruption, and macrophage adhesion, whereas the arteries from 12/15-LO knock-out mice are protected from these effects of arachidonate. Feeding wild-type mice with a high-fat diet induces the expression of 12/15-LO in the arteries leading to tight junction disruption and macrophage adhesion, and deletion of the 12/15-LO gene disallows these effects. 15(S)-HETE-induced endothelial tight junctions disruption promotes monocyte transmigration, 15(S)-HETE induces the dislocation of both claudin-1 and claudin-5 from ZO-2, that participates in tight junctions
physiological function
-
arachidonate 15-lipoxygenase is required for chronic myeloid leukemia stem cell survival in a murine model of BCR-ABLinduced chronic myeloid leukemia, in the absence of Alox15, BCRABL is unable to induce CML in mice
physiological function
-
12/15-lipoxygenase metabolites of arachidonic acid activate PPARgamma, involvement of 12(S)- and 15(S)-hydroperoxyicosatetraenoate in the regulation of PPARgamma following cerebral ischemia and effects on ischemia-induced inflammatory response. 12(S)-HETE and 15(S)-HETE elicit neuroprotection in rats exposed to focal ischemia. PPARgamma is a member of the nuclear hormone receptorfamily of ligand-dependent transcription factors. PPARgamma regulates genes that are implicated in adipocyte differentiation, lipid and glucose metabolism, and insulin sensitivity
physiological function
-
ALOX15-encoded 12/15-lipoxygenase orthologs are implicated in maturational degradation of intracellular organelles and in the biosynthesis of antiinflammatory and proresolving eicosanoids
physiological function
-
ALOX15-encoded 12/15-lipoxygenase orthologs are implicated in maturational degradation of intracellular organelles and in the biosynthesis of antiinflammatory and proresolving eicosanoids
physiological function
-
ALOX15-encoded 12/15-lipoxygenase orthologs are implicated in maturational degradation of intracellular organelles and in the biosynthesis of antiinflammatory and proresolving eicosanoids
physiological function
ALOX15-encoded 12/15-lipoxygenase orthologs are implicated in maturational degradation of intracellular organelles and in the biosynthesis of antiinflammatory and proresolving eicosanoids
physiological function
ALOX15-encoded 12/15-lipoxygenase orthologs are implicated in maturational degradation of intracellular organelles and in the biosynthesis of antiinflammatory and proresolving eicosanoids
physiological function
-
ALOX15-encoded 12/15-lipoxygenase orthologs are implicated in maturational degradation of intracellular organelles and in the biosynthesis of antiinflammatory and proresolving eicosanoids
physiological function
-
ALOX15-encoded 12/15-lipoxygenase orthologs are implicated in maturational degradation of intracellular organelles and in the biosynthesis of antiinflammatory and proresolving eicosanoids
physiological function
ALOX15-encoded 12/15-lipoxygenase orthologs are implicated in maturational degradation of intracellular organelles and in the biosynthesis of antiinflammatory and proresolving eicosanoids
physiological function
ALOX15-encoded 12/15-lipoxygenase orthologs are implicated in maturational degradation of intracellular organelles and in the biosynthesis of antiinflammatory and proresolving eicosanoids
physiological function
ALOX15-encoded 12/15-lipoxygenase orthologs are implicated in maturational degradation of intracellular organelles and in the biosynthesis of antiinflammatory and proresolving eicosanoids
physiological function
ALOX15-encoded 12/15-lipoxygenase orthologs are implicated in maturational degradation of intracellular organelles and in the biosynthesis of antiinflammatory and proresolving eicosanoids
physiological function
-
enzyme 15-lipoxygenase is involved in adipose tissue inflammation. The lipoxygenases (LOs) are principal enzymes involved in the oxidative metabolism of polyunsaturated fatty acids, including arachidonic acid. 12- and 15-LO and their lipid metabolites are implicated in the development of insulin resistance and diabetes. Adipose tissue, and in particular visceral adipose tissue, plays a primary role in the development of the inflammation seen in these conditions. 12- and 15-LO and their lipid metabolites act as upstream regulators of many of the cytokines involved in the inflammatory response in adipose tissue. 12- and 15-LO and their lipid metabolites act as upstream regulators of many of the cytokines involved in the inflammatory response in adipose tissue. Significant role for 12- and 15-LO function in white adipose tissue adipogenesis and adipocyte health. 12- and 15-LO function in adipogenesis and has anti-inflammatory roles in adipose tissue, detailed overview. Leukocyte-type 12-LO, or 12/15-LO appears to be a key player in the progression of adipocyte dysfunction and resultant systemic decline. 12/15-LO is upregulated in white adipose tissue in the obese state. Increased expression of all of the 12- and 15-LO enzyme isoforms in omental vs. subcutaneous white adipose tissue suggests that the pathways may contribute to the proinflammatory milieu prominently associated with visceral fat in obesity. 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
physiological function
-
the effects of 15-LOX-generated metabolites of alpha-linolenic acid on lipopolysaccharide-induced inflammation in RAW 264.7 cells and peritoneal macrophages, analysis of the effect of these metabolites on the survival of BALB/c mice in LPS mediated septic shock and also polymicrobial sepsis in Cecal Ligation and Puncture mouse model, overview. Anti-inflammatory effects of 13-(S)-hydroperoxyoctadecatrienoic acid and 13-(S)-hydroxyoctadecatrienoic acid by inactivating NLRP3 inflammasome complex through the PPAR-gama pathway. Both metabolites, especially 13-(S)-hydroperoxyoctadecatrienoic acid, also deactivate autophagy and induce apoptosis
physiological function
-
the effects of 15-LOX-generated metabolites of alpha-linolenic acid on lipopolysaccharide-induced inflammation in RAW 264.7 cells and peritoneal macrophages, analysis of the effect of these metabolites on the survival of BALB/c mice in LPS mediated septic shock and also polymicrobial sepsis in Cecal Ligation and Puncture mouse model, overview. Anti-inflammatory effects of 13-(S)-hydroperoxyoctadecatrienoic acid and 13-(S)-hydroxyoctadecatrienoic acid by inactivating NLRP3 inflammasome complex through the PPAR-gama pathway. Both metabolites, especially 13-(S)-hydroperoxyoctadecatrienoic acid, also deactivate autophagy and induce apoptosis
-
physiological function
-
12/15-lipoxygenase plays a role in atherosclerosis. 15(S)-hydroxyeicosatetraenoic acid (15(S)-HETE), the major 12/15-LO metabolite of arachidonic acid, induces endothelial barrier permeability via Src and Pyk2-dependent zonula occluden (ZO)-2 tyrosine phosphorylation and its dissociation from the tight junction complexes. 15(S)-HETE also stimulates macrophage adhesion to the endothelial monolayer in Src and Pyk2-dependent manner. Exposure of arteries from wild-type mice to arachidonate or 15(S)-HETE leads to Src-Pyk2-dependent ZO-2 tyrosine phosphorylation, tight junction disruption, and macrophage adhesion, whereas the arteries from 12/15-LO knock-out mice are protected from these effects of arachidonate. Feeding wild-type mice with a high-fat diet induces the expression of 12/15-LO in the arteries leading to tight junction disruption and macrophage adhesion, and deletion of the 12/15-LO gene disallows these effects. 15(S)-HETE-induced endothelial tight junctions disruption promotes monocyte transmigration, 15(S)-HETE induces the dislocation of both claudin-1 and claudin-5 from ZO-2, that participates in tight junctions
-
physiological function
-
12/15LO expression increases chemokine production. 12/15LO mediates early stages of adipose tissue inflammation and whole body insulin resistance induced by high fat feeding. Adipose tissue from high fat diet-fed 12/15LO KO mice is not infiltrated by macrophages and does not display any increase in the inflammatory markers compared to adipose tissue from normal chow-fed mice. 12/15LO KO mice exhibit no high fat diet-induced change in insulin-stimulated glucose disposal rate or hepatic glucose output. Insulin-stimulated Akt phosphorylation in muscle tissue from high fat diet-fed mice is significantly greater in 12/15LO KO mice than in wild-type mice
-
physiological function
-
12/15-LOX is a critical mediator of the chronic type 1 inflammatory response. Evolution of the immune response to Toxoplasma gondii is accompanied by an increasing requirement for 12/15-LOX mediated signaling. Although 12/15-LOX deficient mice are resistant to acute Toxoplasma gondii infection, 80% of 12/15-LOX-deficient mice die during chronic toxoplasmosis, compared to no deaths in wild-type controls. The enhanced susceptibility of 12/15-LOX-deficient mice to chronic toxoplasmosis is associated with reduced production of IL-12 and gamma interferon (IFN-gamma) that is not evident during acute infection. Ex vivo IFN-gamma production by 12/15-LOX-deficient splenocytes can be rescued by the addition of recombinant IL-12. 12/15-LOX does not play a role in macrophage killing of Toxoplasma gondii in vitro; cardiac 12/15-LOX-induced inflammation and oxidative stress are involved in the development of diabetic cardiomyopathy. 12/15-LOX induces cardiac oxidative stress in the diabetic heart; endogenous 12/15-LOX defines the resident peritoneal macrophage population and regulates both the recruitment of monocytes/peritoneal macrophage and cytokine response to bacterial products in vivo
-
physiological function
-
12/15-lipoxygenase metabolites of arachidonic acid activate PPARgamma, involvement of 12(S)- and 15(S)-hydroperoxyicosatetraenoate in the regulation of PPARgamma following cerebral ischemia and effects on ischemia-induced inflammatory response. 12(S)-HETE and 15(S)-HETE elicit neuroprotection in rats exposed to focal ischemia. PPARgamma is a member of the nuclear hormone receptorfamily of ligand-dependent transcription factors. PPARgamma regulates genes that are implicated in adipocyte differentiation, lipid and glucose metabolism, and insulin sensitivity
-
additional information
-
conformational dynamics of native 15-LOX-2, mass spectrometric analysis, overview
additional information
-
quantum mechanics/molecular mechanics calculations with molecular dynamics simulations to study the addition of O2 to the pentadienyl radical of arachidonic acid catalyzed by the Leu597Val and Leu597Ala mutants of rabbit 15-lipoxygenase, detailed overview
additional information
-
molecular dynamics simulations and quantum mechanics/molecular mechanics calculations
additional information
-
molecular dynamics simulations and quantum mechanics/molecular mechanics calculations
additional information
-
molecular dynamics simulations and quantum mechanics/molecular mechanics calculations
additional information
molecular dynamics simulations and quantum mechanics/molecular mechanics calculations
additional information
molecular dynamics simulations and quantum mechanics/molecular mechanics calculations
additional information
-
molecular dynamics simulations and quantum mechanics/molecular mechanics calculations
additional information
-
molecular dynamics simulations and quantum mechanics/molecular mechanics calculations
additional information
molecular dynamics simulations and quantum mechanics/molecular mechanics calculations
additional information
molecular dynamics simulations and quantum mechanics/molecular mechanics calculations
additional information
molecular dynamics simulations and quantum mechanics/molecular mechanics calculations
additional information
molecular dynamics simulations and quantum mechanics/molecular mechanics calculations
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
(16(R),5Z,8Z,11Z,14Z)-16-fluoroeicosa-5,8,11,14-tetraenoic acid + O2
?
-
wild-type enzyme: 78% of the 15,16(R) product and 22% of the 12,16(R) product
-
?
(16(R),5Z,8Z,11Z,14Z)-16-hydroxyeicosa-5,8,11,14-tetraenoic acid + O2
?
-
wild-type enzyme and mutant enzyme I593A prouce small amounts of unspecific products. Mutant enzyme F353L produces 6% of 15,16(R) product and 94% of the 12,16(R) product
-
?
(16(S),5Z,8Z,11Z,14Z)-16-fluoroeicosa-5,8,11,14-tetraenoic acid + O2
?
-
wild-type enzyme: 69% of the 15,16(S) product and 31% of the 12,16(S) product
-
?
(16(S)5Z,8Z,11Z,14Z)-16-hydroxyeicosa-5,8,11,14-tetraenoic acid + O2
?
-
wild-type enzyme: 93% of the 15,16(S) product and 7% of the 12,16(S) product
-
?
(17(R),5Z,8Z,11Z,14Z)-17-hydroxyeicosa-5,8,11,14-tetraenoic acid + O2
?
-
wild-type enzyme: 1% of the 15,17(R) product and 99% of the 12,17(R) product
-
?
(17(S),5Z,8Z,11Z,14Z)-17-hydroxyeicosa-5,8,11,14-tetraenoic acid + O2
?
-
wild-type enzyme: 3% of the 15,17(S) product and 97% of the 12,17(S) product
-
?
(18(R),5Z,8Z,11Z,14Z)-18-hydroxyeicosa-5,8,11,14-tetraenoic acid + O2
?
oxygenation proceeds with little if any enantioselectivity
-
-
?
(18(S),5Z,8Z,11Z,14Z)-18-hydroxyeicosa-5,8,11,14-tetraenoic acid + O2
?
oxygenation proceeds with little if any enantioselectivity
-
-
?
1-linoleoyl lysophosphatidic acid + O2
(S)-hydroperoxy 1-linoleoyl lysophosphatidic acid
-
i.e. linoleoyl-lysoPA
major product
-
?
1-linoleoyl lysophosphatidylcholine + O2
(S)-hydroperoxy 1-linoleoyl lysophosphatidylcholine
-
i.e. linoleoyl-lysoPC
major product
-
?
1-palmitoyl-2-arachidonyl phosphatidyl choline + O2
15S-HpETE
-
-
-
-
?
1-palmitoyl-2-docosahexaenoyl phosphatidyl choline + O2
17S-HpDHE
-
-
-
-
?
1-palmitoyl-2-eicosapentaenoyl phosphatidyl choline + O2
15S-HpEPE
-
-
-
-
?
1-palmitoyl-2-linoleoyl phosphatidyl choline + O2
(9E,11E)-13S-hydroperoxy-9,11-octadecadienoic acid
-
-
-
-
?
1-stearyl-2-linoleoyl glycerol + O2
cholesteryl-(9E,11E)-13S-hydroperoxy-9,11-octadecadienoate
-
-
-
-
?
11,14,17-eicosatrienoic acid + O2
15-hydroperoxy-11,13,17-eicosatrienoic acid
-
-
-
?
2 arachidonate + 2 O2 + H+
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate + (5Z,8Z,11Z,13E)-(15S)-15-hydroxyeicosa-5,8,11,13-tetraenoate + H2O
8,11,14-eicosatrienoic acid + O2
15-hydroperoxy-8,11,13-eicosatrienoic acid
-
-
-
?
alpha-linoleic acid + O2
?
72% activity compared to arachidonate
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoic acid + (9Z,11E,13S,15Z)-13-hydroxyoctadeca-9,11,15-trienoic acid
arachidonate + O2
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E,15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
ratio of (5Z,8Z,11Z,13E,15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate to (5Z,8Z,11Z,13E,15R)-15-hydroperoxyicosa-5,8,11,13-tetraenoate is 92:8
-
?
arachidonate + O2
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyicosa-6,8,11,14-tetraenoate
-
-
-
-
?
arachidonic acid + O2
(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid + (12S,5Z,8Z,10E,14Z)-12-hydroperoxyeicosa-5,8,10,14-tetraenoic acid
arachidonic acid + O2
13-hydroperoxyeicosatetraenoic acid + (5Z,8Z,11R,12E,14Z)-11-hydroperoxyicosa-5,8,12,14-tetraenoic acid + (5Z,8E,11Z,13E,15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoic acid
-
-
-
?
arachidonic acid + O2
15S-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoic acid
-
-
-
-
?
cholesteryl linoleate + O2
cholesteryl-(9E,11E)-13S-hydroperoxy-9,11-octadecadienoate
-
-
-
-
?
dihomo-gamma-linolenic acid + O2
?
44% activity compared to arachidonate
-
-
?
dilinoleoyl phosphatidic acid + O2
(S)-hydroperoxy dilinoleoyl phosphatidic acid
-
i.e. dilinoleoylPA
-
-
?
dilinoleoyl phosphatidylcholine + O2
(S)-hydroperoxy dilinoleoyl phosphatidylcholine
-
i.e. dilinoleoylPC
-
-
?
docosahexaenoic acid + O2
?
72% activity compared to arachidonate
-
-
?
eicopentanoic acid + O2
?
61% activity compared to arachidonate
-
-
?
eicosadienoic acid + O2
?
33% activity compared to arachidonate
-
-
?
gamma-linolenic acid + O2
?
44% activity compared to arachidonate
-
-
?
linoleate + O2
(9Z,11R,12Z)-11-hydroperoxyoctadeca-9,12-dienoate + (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate + (9R,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate
-
(9Z,11R,12Z)-11-hydroperoxyoctadeca-9,12-dienoate is the primary product
-
?
linoleic acid + O2
13(S)-hydroxyoctadecadienoic acid
-
-
12/15LO eicosanoid products reduce cholesterol efflux to high density lipoproteins, regulate ATP-binding cassette transporter G1 expression and enhance ATP-binding cassette transporter G1 degradation and ATP-binding cassette transporter G1 serine phosphorylation
-
?
linoleic acid + O2
13-S-hydroxyoctadecadienoic acid
-
both 15-LOX-1, 15-LOX-2 reacts with linoleic acid poorly
-
-
?
linolenate + O2
11-hydroperoxyoctadecatrienoic acid + 9-hydroperoxyoctadecatrienoic acid + 13-hydroperoxyoctadecatrienoic acid
-
-
-
?
2 arachidonate + 2 O2 + H+
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate + (5Z,8Z,11Z,13E)-(15S)-15-hydroxyeicosa-5,8,11,13-tetraenoate + H2O
-
-
(5Z,8Z,11Z,13E)-(15S)-15-hydroxyeicosa-5,8,11,13-tetraenoate slightly increases expression of monocyte chemoattractant protein MCP-1 in macrophages, also but more potent by 12(S)-hydroxyeicosatetranoic acid, overview, i.e. 15(S)-HPETE and 15(S)-HETE, the first is the predominant product
-
?
2 arachidonate + 2 O2 + H+
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate + (5Z,8Z,11Z,13E)-(15S)-15-hydroxyeicosa-5,8,11,13-tetraenoate + H2O
-
-
(5Z,8Z,11Z,13E)-(15S)-15-hydroxyeicosa-5,8,11,13-tetraenoate slightly increases expression of monocyte chemoattractant protein MCP-1 in macrophages, also but more potent by 12(S)-hydroxyeicosatetranoic acid, overview, i.e. 15(S)-HPETE and 15(S)-HETE, the first is the predominant product
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoic acid + (9Z,11E,13S,15Z)-13-hydroxyoctadeca-9,11,15-trienoic acid
-
-
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoic acid + (9Z,11E,13S,15Z)-13-hydroxyoctadeca-9,11,15-trienoic acid
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
671247, 672376, 672543, 672899, 672902, 673030, 675201, 675909, 676263, 676923, 676925, 676927, 677239, 685266, 685525, 685526, 685584, 686173, 687052, 687235, 688159, 688509, 688751, 712712
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
and small amounts of (5Z,8Z,10E,14Z)-12-hydro(pero)xy-5,8,10,14-icosatetraenoic acid
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
15-hydroperoxy-5,8,11,13-eicosatetraenoic acid + 15-hydroxy-5,8,11,13-eicosatetraenoic acid
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
formation of 15S-hydroxyeicosatetraenoic acid and 12S-hydroxyeicosatetraenoic acid in a ratio of 12:1, double oxygenation products 14R,15S-dihydroxyeicosatetraenoic acid and various 8,15-dihydroxyeicosatetraenoic acids are also produced
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
ratio of 15-lipoxygenation to 12-lipoxygenation is 9:1 for the wild-type enzyme and the mutant enzymes V104I, L397M and Q431R. The ratio of 15-lipoxygenation to 12-lipoxygenation is 1:1 for the mutant enzymes V104/L397M/M418V/Q431R, L397M/M418V/Q431R, L397M/M418V and M418V
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
15-hydroxyeicosatetraenoic acid and 12-hydroxyeicosatetraenoic acid in a ratio of 8.6:1
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
further metabolized to (5Z,8Z,11Z,13E)-(15S)-15-hydroxyeicosa-5,8,11,13-tetraenoate, 15-HETE, has no effect on the spontaneous and lipopolysaccharide-stimulated growth of leukemic blasts
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
the bifunctional enzyme also forms (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyeicosa-5,8,10,14-tetraenoate, the product of 12-LO activity, EC 1.13.11.31, in a ratio of 9:1 15(S)-HPETE to 12(S)-HPETE, further reduced to the correspondent (S)-hydroxy fatty acids, in eosinophils, overview, the bifunctional enzyme also forms (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyeicosa-5,8,10,14-tetraenoate, the product of 12-LO activity, EC 1.13.11.31, in a ratio of 9:1 15(S)-HPETE to 12(S)HPETE
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
is further metabolized to (5Z,8Z,11Z,13E)-(15S)-15-hydroxyeicosa-5,8,11,13-tetraenoate, i.e. 15(S)-HETE
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
the enzyme is regulated pretranslational, translational and posttranslational
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
15-lipoxygenase 2 is a negative cell cycle regulator in normal prostate epithelial cells, it could be a suppressor of prostate cancer development, which functions by restricting cell cycle progression
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
catalyzes enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
the enzyme is implicated in inflammatory disorders, 15-lipoxygenase is induced in atherosclerosis and can oxidize low-density lipoprotein to its atherogenic form
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
alternative splicing of 15S-lipoxygenase provides a further level of regulation of fatty acid metabolism
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
12/15LO protein levels and activity are increased in pathologically affected regions of Alzheimers disease brains, enzyme inhibition causes a decrease in amyloid-beta protein, 12/15LO influences amyloid-beta protein precursor protein metabolism, overview
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
15-lipoxygenase type-1 is a prooxidant enzyme, which is expressed in asthmatic lungs leading to formation of pro- and anti-inflammatory mediators, overview
the product is further metabolized to 15(S)-hydroxyeicosatetranoic acid and 15-ketoeicosatetraenoic acid, the latter is the main product, pathway and mechanism, overview
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
15-LOX2 in NHP cells is positively regulated by Sp1 and negatively regulated by Sp3, but 15-LOX2 expression in NHP cells is not directly regulated by androgen/androgen receptor, overview
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
arachidonic acid is metabolized by the 15-lipoxygenase-1 pathway to the vasodilatory eicosanoids hydroxyepoxyeicosatrienoic acid and trihydroxyeicosatrienoic acid
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
arachidonic acid metabolization by lipoxygenases, overview
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
the enzyme is involved in acetylsalicylic acid-triggered production of 15(S)-hydroxyeicosatetranoic acid, 15(S)-HETE, in sensitive asthmatic patients, acetylsalicylate-tolerant asthma patients show reduced 15-LO activity
is metabolized to 15(S)-hydroxyeicosatetranoic, i.e. 15(S)-HETE
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
the enzyme modifies high density lipoprotein 3, the major and most antiatherogenic HDL subfraction, and impairs anti-inflammatory activity of the lipoprotein, which, after modification, fails to inhibit TNFalpha-mediated mRNA and protein induction of adhesion molecules and monocyte chemoattractant protein-1, MCP-1, in endothelial cells, overview
is metabolized to 15(S)-hydroxyeicosatetranoic, i.e. 15(S)-HETE
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
immunohistochemic assay
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
preferred substrate of isozyme 15-hLO-2, reaction of EC 1.13.11.33
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
regioselective oxidation is achieved through control over the position of hydrogen atom abstraction by the geometry and size of the enzyme active site and through control by the protein over the interaction of molecular oxygen with the generated delocalized substrate radical, analysis of catalytic mechanisms of lipoxygenases using 10,10-dideuterated arachidonic acid, 13,13-dideuterated arachidonic acid, and 0,10,13,13-d4-AA, overview
isozymes 15-hLO-1 and 15-hLO-2 also form small amounts of 11-HPETE, 8-HPETE, and 12-HPETE, the rate of 8/12-HPETE production by isozyme 15-hLO-1 with 13,13-dideuterated arachidonic acid as substrate is exeptionally high with 75% of overall production, overview
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
the enzyme is regulated pretranslational, translational and posttranslational
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
induction of experimental anemia leads to a systemic up-regulation of 12/15-lipoxygenases expression
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
and nonenzymatic production of 15-hydroxy-5,8,11,13-eicosatetraenoic acid, 15-keto-5,8,11,13-eicosatetraenoic acid, 13-hydroxy-14,15-epoxy-5,8,11-eicosatrienoic acid and 11,14,15-trihydroxy-5,8,12-eicosatrienoic acid
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
is further metabolized by hydroperoxide isomerase to the acid-sensitive metabolite 15(S)-hydroxy-11,12-epoxyeicosatrienoic acid, which is hydrolyzed to 11,12,15-trihydroxyeicosatrienoic acid, by a soluble epoxid hydrolase, causing endothelium-dependent smooth muscle hyperpolarization and relaxations, mass spectrometrical metabolite analysis and pathway, overview
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
the enzyme is regulated pretranslational, translational and posttranslational
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
induction of experimental anemia leads to a systemic up-regulation of 12/15-lipoxygenases expression
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
catalyzes enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
first step in biotransformation of arachidonic acid to the 15-series of leukotrienes, reaction is involved in inactivation of slow-reacting substrances of anaphylaxis
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
high oxygen affinity is important for effective catalysis, L367 is involved in oxygen access, channel structure, overview, arachidonic acid closes the substrate-binding pocket for oxygen diffusion but opens a fourth oxygen access channel
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
the enzyme is regulated pretranslational, translational and posttranslational
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
induction of experimental anemia leads to a systemic up-regulation of 12/15-lipoxygenases expression
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
Sarcolobus globosus
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
15-H(p)ETE is the major reaction product of 15-LOX-2 and 12/15-LOX independent of the pH
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
product ratio is 9 to 1
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
best substrate
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
5fold higher affinity for arachidonic acid than for linoleic acid for 15-hLO-1
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
both 15-LOX-1 and -2
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
main product is 12(S)-hydroxyeicosatetranoic acid
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
best substrate
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
best substrate
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
15-H(p)ETE is the major reaction product independent of the pH
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
best substrate
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
best substrate
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
12/15LO eicosanoid products reduce cholesterol efflux to high density lipoproteins, regulate ATP-binding cassette transporter G1 expression and enhance ATP-binding cassette transporter G1 degradation and ATP-binding cassette transporter G1 serine phosphorylation
-
?
arachidonic acid + O2
(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid
-
-
the mutant enzyme A416G converts arachidonic acid to (11R)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid and (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid in a 1.5:1 ratio
-
?
arachidonic acid + O2
(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid
-
-
-
-
?
arachidonic acid + O2
(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid
-
an atomic-level study of the binding modes of linoleic acid to rabbit reticulocyte 15-rLO-1 is presented. Results are compared with binding of arachidonic acid to 15-rLO-1. Linoleic acid seems to adapt more easily to the enzyme structure and differs from arachidonic acid on some dynamical aspects that could introduce kinetic differences, as observed experimentally
-
-
?
arachidonic acid + O2
(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid
-
-
-
-
?
arachidonic acid + O2
(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid + (12S,5Z,8Z,10E,14Z)-12-hydroperoxyeicosa-5,8,10,14-tetraenoic acid
-
93% (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid and 7% (12S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid
-
?
arachidonic acid + O2
(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid + (12S,5Z,8Z,10E,14Z)-12-hydroperoxyeicosa-5,8,10,14-tetraenoic acid
-
-
the ratio of (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid to (12S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid is 20 for the wild-type enzyme
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxy-octadeca-9,11-dienoate
-
reaction of EC 1.13.11.12
-
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxy-octadeca-9,11-dienoate
-
-
-
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxy-octadeca-9,11-dienoate
-
preferred substrate of isozyme 15-hLO-1, reaction of EC 1.13.11.12
-
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxy-octadeca-9,11-dienoate
78% activity compared to arachidonate
-
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleic acid + O2
13-hydroxylinoleic acid
-
-
13-hydroperoxy-9,11-octadecadienoic acid + 13-hydroxy-9,11-octadecadienoic acid
?
linoleic acid + O2
?
-
an atomic-level study of the binding modes of linoleic acid to rabbit reticulocyte 15-rLO-1 is presented. Results are compared with binding of arachidonic acid to 15-rLO-1. Linoleic acid seems to adapt more easily to the enzyme structure and differs from arachidonic acid on some dynamical aspects that could introduce kinetic differences, as observed experimentally
-
-
?
additional information
?
-
incubation of the enzyme with [(11S)-2H]-linoleic acid leads to the formation of hydroperoxides that have lost the deuterium label, thus suggesting that LOX2 catalyzes antarafacial oxygenation as opposed to the mechanism of manganese lipoxygenase
-
-
-
additional information
?
-
-
the enzyme may be involved in the development of atherosclerosis
-
-
-
additional information
?
-
-
15-LOX2 and 15-LOX2sv-b suppress prostate tumor development, and the tumor-suppressive functions apparently do not necessarily depend on arachidonic acid-metabolizing activity and nuclear localization
-
-
-
additional information
?
-
-
15-LOX2 is a functional tumor suppressor that regulates prostate epithelial cell differentiation, senescence, and growth size, overview
-
-
-
additional information
?
-
-
eoxins are proinflammatory arachidonic acid metabolites produced via the 15-lipoxygenase-1 pathway in eosinophils and mast cells, metabolism of 14,15-leukotrienes in eosinophils, overview
-
-
-
additional information
?
-
a bifunctional enzyme exhibiting 12-LO and 15-LO activity
-
-
-
additional information
?
-
-
a bifunctional enzyme exhibiting 15-lipoxygenase and 12-lipoxygenase, EC 1.13.11.31, activities
-
-
-
additional information
?
-
-
conjugated linoleic acids are no substrates for 15-LO-1 in vitro, overview
-
-
-
additional information
?
-
-
product distributions of lipoxygenases under various conditions, overview
-
-
-
additional information
?
-
-
substrate specificity of 15-hLO isozymes, the specific activity is affected by cholate and lipoxygenation reaction products, e.g. 13-hydroperoxyoctadienoic acid changes the (kcat/Km)AA/(kcat/Km)LA ratio more than 5fold for 15-hLO-1 and 3fold for 15-hLO-2, while 12-(S)-hydroperoxyeicosatetraenoic acid affects only the ratio of 15-hLO-1 more than 5fold. In addition, 13-(S)-hydroxyoctadecadienoic acid and 12-(S)-hydroxyeicosatetraenoic acid also affect substrate specificity, indicating that iron oxidation is not responsible for the change in the (kcat/Km)AA/(kcat/Km)LA ratio, residues R402, F414, F352, I417, and M418 are located at the active site and involved in catalysis, presence of a product-activated, allosteric regulatory site for both 15-hLO isozymes, competitive substrate capture experiments, overview
-
-
-
additional information
?
-
-
15-LOX-2 does not oxygenate (5Z,8Z,11Z,14Z)-nonadeca-5,8,11,14-tetraene-1,19-dioic acid at various pH
-
-
-
additional information
?
-
-
15LO1 interacts with PEBP1 (phosphatidylethanolamine-binding protein)
-
-
-
additional information
?
-
-
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview. The wild-type subject produces 21% 12-hydroperoxyicosatetraenoate and 79% 15-hydroperoxyicosatetraenoate
-
-
-
additional information
?
-
-
15-LOX is a non-heme iron-containing dioxygenase that oxygenates polyunsaturated fatty acids (PUFA) containing cis,cis-1,4-pentadiene moieties
-
-
-
additional information
?
-
human 15-LOX type 1 (ALOX15) is a predominantly 15-lipoxygenating enzyme, which produces only little amounts of (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate (ratio of 9:1)
-
-
-
additional information
?
-
-
the major reaction products are identified as(8S,15S,5Z,9E,11Z,13E)-8,15-dihydroperoxy-5,9,11,13-eicosatetraenoic acid (8S,15S-DiHpETE) and (5S,15S,6E,8Z,11Z,13E)-5,15-dihydroperoxy-6,8,11,13-eicosatetraenoic acid (5S,15S-DiHPETE) and the stereochemistry of the reaction is compatible with an inverse substrate orientation. Intraenzyme oxygen movement
-
-
-
additional information
?
-
-
enzyme substrate specificity, overview. The ALOX15 enzyme activity is not restricted to free polyenoic fatty acids since phospholipids and even biomembranes and lipoproteins are suitable ALOX15 substrates. The ALOX15 orthologue is capable of converting hydroperoxy fatty acids to epoxy leukotrienes. Product specificity with polyenoic acids and with complex substrates, and alteration of product specificity by substrate modification
-
-
-
additional information
?
-
-
prediction of reaction specificity of mammalian ALOX15 orthologues, and reaction specificity of ALOX15 orthologues during late primate evolution
-
-
-
additional information
?
-
-
specificity of phospholipid binding by 15-LOX-2, overview
-
-
-
additional information
?
-
the enzymatic peroxidation reaction consists of four consecutive steps: At first a hydrogen atom is stereoselectively abstracted from one of the bisallylic methylene-groups forming an enzyme-bound radical. Secondly one of the two associated cis-double bonds is rearranged and forms a conjugated cis-trans-diene. Consecutively a peroxy radical is produced by inserting molecular oxygen. Finally the radical is reduced by antarafacial re-inserting of a hydrogen atom. The resulting product of this peroxidation reaction depends on the respective fatty acid, which is used as a substrate
-
-
-
additional information
?
-
-
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview
-
-
-
additional information
?
-
-
prediction of reaction specificity of mammalian ALOX15 orthologues, and reaction specificity of ALOX15 orthologues during late primate evolution
-
-
-
additional information
?
-
-
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview
-
-
-
additional information
?
-
-
prediction of reaction specificity of mammalian ALOX15 orthologues, and reaction specificity of ALOX15 orthologues during late primate evolution
-
-
-
additional information
?
-
the enzyme also converts linoleate to (9Z,11E,13S)-13-hydroperoxy-11,13-octadecadienoate
-
-
-
additional information
?
-
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview
-
-
-
additional information
?
-
prediction of reaction specificity of mammalian ALOX15 orthologues, and reaction specificity of ALOX15 orthologues during late primate evolution
-
-
-
additional information
?
-
-
a bifunctional enzyme exhibiting 12-LO and 15-LO activity, the enzyme is also able to catalyze stereoselective oxidation of linoleic acid at position 13 over 9 to preferentially form 13(S)-hydroperoxyoctadienoic acid, which enhances MCP-1 expression, overview
-
-
-
additional information
?
-
-
the major reaction products are identified as(8S,15S,5Z,9E,11Z,13E)-8,15-dihydroperoxy-5,9,11,13-eicosatetraenoic acid (8S,15S-DiHpETE) and (5S,15S,6E,8Z,11Z,13E)-5,15-dihydroperoxy-6,8,11,13-eicosatetraenoic acid (5S,15S-DiHPETE) and the stereochemistry of the reaction is compatible with an inverse substrate orientation
-
-
-
additional information
?
-
-
enzyme substrate specificity, overview. The ALOX15 enzyme activity is not restricted to free polyenoic fatty acids since phospholipids and even biomembranes and lipoproteins are suitable ALOX15 substrates. The ALOX15 orthologue is capable of converting hydroperoxy fatty acids to epoxy leukotrienes. Product specificity with polyenoic acids and with complex substrates, and alteration of product specificity by substrate modification. Intraenzyme oxygen movement
-
-
-
additional information
?
-
the enzymatic peroxidation reaction consists of four consecutive steps: At first a hydrogen atom is stereoselectively abstracted from one of the bisallylic methylene-groups forming an enzyme-bound radical. Secondly one of the two associated cis-double bonds is rearranged and forms a conjugated cis-trans-diene. Consecutively a peroxy radical is produced by inserting molecular oxygen. Finally the radical is reduced by antarafacial re-inserting of a hydrogen atom. The resulting product of this peroxidation reaction depends on the respective fatty acid, which is used as a substrate
-
-
-
additional information
?
-
-
a bifunctional enzyme exhibiting 12-LO and 15-LO activity, the enzyme is also able to catalyze stereoselective oxidation of linoleic acid at position 13 over 9 to preferentially form 13(S)-hydroperoxyoctadienoic acid, which enhances MCP-1 expression, overview
-
-
-
additional information
?
-
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview. The wild-type animal produces 54% 12-hydroperoxyicosatetraenoate and 46% 15-hydroperoxyicosatetraenoate with 76% overall activity compared to the human enzyme activity
-
-
-
additional information
?
-
prediction of reaction specificity of mammalian ALOX15 orthologues, and reaction specificity of ALOX15 orthologues during late primate evolution
-
-
-
additional information
?
-
the enzyme also converts linoleate to (9Z,11E,13S)-13-hydroperoxy-11,13-octadecadienoate, alpha-linolenate to (9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoate and gamma-linolenate to (6Z,9Z,11E,13S)-13-hydroperoxy-6,9,11-octadecatrienoate
-
-
-
additional information
?
-
-
15-lipoxygenase is capable of disrupting the pH gradient maintained by mitochondria in living cells without additional factors specific for red blood cell development. Ectopic expression of 15-lipoxygenase leads to the collaps of the mitochondrial pH gradient in nonerythroid cells
-
-
-
additional information
?
-
-
activation of the enzyme at the protein and product levels and increased sensitivity to constriction of pulmonary arteries by the product 15S-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoic acid may contribute to pulmonary hypoxic vasoconstriction in neonatal rabbits
-
-
-
additional information
?
-
-
the enzyme may be involved in the development of atherosclerosis
-
-
-
additional information
?
-
-
stereo-selectivity in LOX-catalyzed oxygenation of lysophospholipids, overview
-
-
-
additional information
?
-
-
the bifunctional enzyme also forms (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyeicosa-5,8,10,14-tetraenoate, the product of 12-LO activity, EC 1.13.11.31, in a ratio of 9:1 15(S)-HPETE to 12(S)HPETE
-
-
-
additional information
?
-
-
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. The wild-type animal produces 3% 12-hydroperoxyicosatetraenoate and 97% 15-hydroperoxyicosatetraenoate
-
-
-
additional information
?
-
-
the major reaction products are identified as(8S,15S,5Z,9E,11Z,13E)-8,15-dihydroperoxy-5,9,11,13-eicosatetraenoic acid (8S,15S-DiHpETE) and (5S,15S,6E,8Z,11Z,13E)-5,15-dihydroperoxy-6,8,11,13-eicosatetraenoic acid (5S,15S-DiHPETE) and the stereochemistry of the reaction is compatible with an inverse substrate orientation
-
-
-
additional information
?
-
-
enzyme substrate specificity, overview. The ALOX15 enzyme activity is not restricted to free polyenoic fatty acids since phospholipids and even biomembranes and lipoproteins are suitable ALOX15 substrates. The ALOX15 orthologue is capable of converting hydroperoxy fatty acids to epoxy leukotrienes. Molecular docking studies of a phospholipid molecule at the active site of rabbit ALOX15. Product specificity with polyenoic acids and with complex substrates, and alteration of product specificity by substrate modification. Intraenzyme oxygen movement
-
-
-
additional information
?
-
-
prediction of reaction specificity of mammalian ALOX15 orthologues, and reaction specificity of ALOX15 orthologues during late primate evolution
-
-
-
additional information
?
-
-
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview
-
-
-
additional information
?
-
-
prediction of reaction specificity of mammalian ALOX15 orthologues, and reaction specificity of ALOX15 orthologues during late primate evolution
-
-
-
additional information
?
-
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview. The wild-type animal produces 20% 12-hydroperoxyicosatetraenoate and 80% 15-hydroperoxyicosatetraenoate with 135% overall activity compared to the human enzyme activity
-
-
-
additional information
?
-
prediction of reaction specificity of mammalian ALOX15 orthologues, and reaction specificity of ALOX15 orthologues during late primate evolution
-
-
-
additional information
?
-
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview. The wild-type animal produces 78% 12-hydroperoxyicosatetraenoate and 22% 15-hydroperoxyicosatetraenoate with 37% overall activity compared to the human enzyme activity
-
-
-
additional information
?
-
prediction of reaction specificity of mammalian ALOX15 orthologues, and reaction specificity of ALOX15 orthologues during late primate evolution
-
-
-
additional information
?
-
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview
-
-
-
additional information
?
-
prediction of reaction specificity of mammalian ALOX15 orthologues, and reaction specificity of ALOX15 orthologues during late primate evolution
-
-
-
additional information
?
-
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview. The wild-type animal produces 14% 12-hydroperoxyicosatetraenoate and 86% 15-hydroperoxyicosatetraenoate
-
-
-
additional information
?
-
prediction of reaction specificity of mammalian ALOX15 orthologues, and reaction specificity of ALOX15 orthologues during late primate evolution
-
-
-
additional information
?
-
-
production of antiinflammatory lipid mediators by the enzyme may be a general strategy by which pathogens regulate the host-pathogen relationship
-
-
-
additional information
?
-
enzyme LoxA is capable of efficiently catalyzing the peroxidation of a broad range of free fatty acid substrates, e.g. arachidonate and linoleate with high positional specificity, indicating a 15-LOX, its mechanism includes hydrogen atom abstraction. LoxA also does not react with 5- or 15-15-hydroperoxyicosatetraenoates, or phosphoester fatty acids
-
-
-
additional information
?
-
-
trans-10,cis-12-conjugated linoleic acid is not a substrate for 15-LOX-1
-
-
-
additional information
?
-
-
in the brain, the principal 12/15-LOX metabolites of arachidonate are (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate, cf. EC 1.13.11.31, and (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
additional information
?
-
the major reaction products are identified as(8S,15S,5Z,9E,11Z,13E)-8,15-dihydroperoxy-5,9,11,13-eicosatetraenoic acid (8S,15S-DiHpETE) and (5S,15S,6E,8Z,11Z,13E)-5,15-dihydroperoxy-6,8,11,13-eicosatetraenoic acid (5S,15S-DiHPETE) and the stereochemistry of the reaction is compatible with an inverse substrate orientation
-
-
-
additional information
?
-
enzyme substrate specificity, overview. The ALOX15 enzyme activity is not restricted to free polyenoic fatty acids since phospholipids and even biomembranes and lipoproteins are suitable ALOX15 substrates. The ALOX15 orthologue is capable of converting hydroperoxy fatty acids to epoxy leukotrienes. Product specificity with polyenoic acids and with complex substrates, and alteration of product specificity by substrate modification. Intraenzyme oxygen movement
-
-
-
additional information
?
-
in the brain, the principal 12/15-LOX metabolites of arachidonate are (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate, cf. EC 1.13.11.31, and (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
2 arachidonate + 2 O2 + H+
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate + (5Z,8Z,11Z,13E)-(15S)-15-hydroxyeicosa-5,8,11,13-tetraenoate + H2O
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxy-octadeca-9,11-dienoate
-
-
-
-
?
2 arachidonate + 2 O2 + H+
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate + (5Z,8Z,11Z,13E)-(15S)-15-hydroxyeicosa-5,8,11,13-tetraenoate + H2O
-
-
(5Z,8Z,11Z,13E)-(15S)-15-hydroxyeicosa-5,8,11,13-tetraenoate slightly increases expression of monocyte chemoattractant protein MCP-1 in macrophages, also but more potent by 12(S)-hydroxyeicosatetranoic acid, overview
-
?
2 arachidonate + 2 O2 + H+
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate + (5Z,8Z,11Z,13E)-(15S)-15-hydroxyeicosa-5,8,11,13-tetraenoate + H2O
-
-
(5Z,8Z,11Z,13E)-(15S)-15-hydroxyeicosa-5,8,11,13-tetraenoate slightly increases expression of monocyte chemoattractant protein MCP-1 in macrophages, also but more potent by 12(S)-hydroxyeicosatetranoic acid, overview
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
further metabolized to (5Z,8Z,11Z,13E)-(15S)-15-hydroxyeicosa-5,8,11,13-tetraenoate, 15-HETE, has no effect on the spontaneous and lipopolysaccharide-stimulated growth of leukemic blasts
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
the bifunctional enzyme also forms (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyeicosa-5,8,10,14-tetraenoate, the product of 12-LO activity, EC 1.13.11.31, in a ratio of 9:1 15(S)-HPETE to 12(S)-HPETE, further reduced to the correspondent (S)-hydroxy fatty acids, in eosinophils, overview
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
the enzyme is regulated pretranslational, translational and posttranslational
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
O15296
15-lipoxygenase 2 is a negative cell cycle regulator in normal prostate epithelial cells, it could be a suppressor of prostate cancer development, which functions by restricting cell cycle progression
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
catalyzes enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
the enzyme is implicated in inflammatory disorders, 15-lipoxygenase is induced in atherosclerosis and can oxidize low-density lipoprotein to its atherogenic form
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
alternative splicing of 15S-lipoxygenase provides a further level of regulation of fatty acid metabolism
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
12/15LO protein levels and activity are increased in pathologically affected regions of Alzheimers disease brains, enzyme inhibition causes a decrease in amyloid-beta protein, 12/15LO influences amyloid-beta protein precursor protein metabolism, overview
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
15-lipoxygenase type-1 is a prooxidant enzyme, which is expressed in asthmatic lungs leading to formation of pro- and anti-inflammatory mediators, overview
the product is further metabolized to 15(S)-hydroxyeicosatetranoic acid and 15-ketoeicosatetraenoic acid, the latter is the main product, pathway and mechanism, overview
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
15-LOX2 in NHP cells is positively regulated by Sp1 and negatively regulated by Sp3, but 15-LOX2 expression in NHP cells is not directly regulated by androgen/androgen receptor, overview
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
arachidonic acid is metabolized by the 15-lipoxygenase-1 pathway to the vasodilatory eicosanoids hydroxyepoxyeicosatrienoic acid and trihydroxyeicosatrienoic acid
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
arachidonic acid metabolization by lipoxygenases, overview
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
the enzyme is involved in acetylsalicylic acid-triggered production of 15(S)-hydroxyeicosatetranoic acid, 15(S)-HETE, in sensitive asthmatic patients, acetylsalicylate-tolerant asthma patients show reduced 15-LO activity
is metabolized to 15(S)-hydroxyeicosatetranoic, i.e. 15(S)-HETE
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
the enzyme modifies high density lipoprotein 3, the major and most antiatherogenic HDL subfraction, and impairs anti-inflammatory activity of the lipoprotein, which, after modification, fails to inhibit TNFalpha-mediated mRNA and protein induction of adhesion molecules and monocyte chemoattractant protein-1, MCP-1, in endothelial cells, overview
is metabolized to 15(S)-hydroxyeicosatetranoic, i.e. 15(S)-HETE
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
the enzyme is regulated pretranslational, translational and posttranslational
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
induction of experimental anemia leads to a systemic up-regulation of 12/15-lipoxygenases expression
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
is further metabolized by hydroperoxide isomerase to the acid-sensitive metabolite 15(S)-hydroxy-11,12-epoxyeicosatrienoic acid, which is hydrolyzed to 11,12,15-trihydroxyeicosatrienoic acid, by a soluble epoxid hydrolase, causing endothelium-dependent smooth muscle hyperpolarization and relaxations, mass spectrometrical metabolite analysis and pathway, overview
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
the enzyme is regulated pretranslational, translational and posttranslational
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
induction of experimental anemia leads to a systemic up-regulation of 12/15-lipoxygenases expression
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
catalyzes enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
first step in biotransformation of arachidonic acid to the 15-series of leukotrienes, reaction is involved in inactivation of slow-reacting substrances of anaphylaxis
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
the enzyme is regulated pretranslational, translational and posttranslational
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
induction of experimental anemia leads to a systemic up-regulation of 12/15-lipoxygenases expression
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
P16050
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
best substrate
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
F7EPQ4
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
P39654
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
best substrate
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
P39654
best substrate
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
P39654
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
G1S6D2
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
best substrate
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
H2QBX9
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
A0A096P2G1
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
Q5RBE8
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
Q5RBE8
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
Q9I4G8
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
Q02759
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
Q02759
-
-
-
?
additional information
?
-
-
the enzyme may be involved in the development of atherosclerosis
-
-
-
additional information
?
-
-
15-LOX2 and 15-LOX2sv-b suppress prostate tumor development, and the tumor-suppressive functions apparently do not necessarily depend on arachidonic acid-metabolizing activity and nuclear localization
-
-
-
additional information
?
-
-
15-LOX2 is a functional tumor suppressor that regulates prostate epithelial cell differentiation, senescence, and growth size, overview
-
-
-
additional information
?
-
-
eoxins are proinflammatory arachidonic acid metabolites produced via the 15-lipoxygenase-1 pathway in eosinophils and mast cells, metabolism of 14,15-leukotrienes in eosinophils, overview
-
-
-
additional information
?
-
-
15LO1 interacts with PEBP1 (phosphatidylethanolamine-binding protein)
-
-
-
additional information
?
-
-
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview. The wild-type subject produces 21% 12-hydroperoxyicosatetraenoate and 79% 15-hydroperoxyicosatetraenoate
-
-
-
additional information
?
-
-
15-LOX is a non-heme iron-containing dioxygenase that oxygenates polyunsaturated fatty acids (PUFA) containing cis,cis-1,4-pentadiene moieties
-
-
-
additional information
?
-
P16050
human 15-LOX type 1 (ALOX15) is a predominantly 15-lipoxygenating enzyme, which produces only little amounts of (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate (ratio of 9:1)
-
-
-
additional information
?
-
-
the major reaction products are identified as(8S,15S,5Z,9E,11Z,13E)-8,15-dihydroperoxy-5,9,11,13-eicosatetraenoic acid (8S,15S-DiHpETE) and (5S,15S,6E,8Z,11Z,13E)-5,15-dihydroperoxy-6,8,11,13-eicosatetraenoic acid (5S,15S-DiHPETE) and the stereochemistry of the reaction is compatible with an inverse substrate orientation. Intraenzyme oxygen movement
-
-
-
additional information
?
-
-
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview
-
-
-
additional information
?
-
-
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview
-
-
-
additional information
?
-
F7EPQ4
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview
-
-
-
additional information
?
-
-
the major reaction products are identified as(8S,15S,5Z,9E,11Z,13E)-8,15-dihydroperoxy-5,9,11,13-eicosatetraenoic acid (8S,15S-DiHpETE) and (5S,15S,6E,8Z,11Z,13E)-5,15-dihydroperoxy-6,8,11,13-eicosatetraenoic acid (5S,15S-DiHPETE) and the stereochemistry of the reaction is compatible with an inverse substrate orientation
-
-
-
additional information
?
-
G1S6D2
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview. The wild-type animal produces 54% 12-hydroperoxyicosatetraenoate and 46% 15-hydroperoxyicosatetraenoate with 76% overall activity compared to the human enzyme activity
-
-
-
additional information
?
-
-
15-lipoxygenase is capable of disrupting the pH gradient maintained by mitochondria in living cells without additional factors specific for red blood cell development. Ectopic expression of 15-lipoxygenase leads to the collaps of the mitochondrial pH gradient in nonerythroid cells
-
-
-
additional information
?
-
-
activation of the enzyme at the protein and product levels and increased sensitivity to constriction of pulmonary arteries by the product 15S-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoic acid may contribute to pulmonary hypoxic vasoconstriction in neonatal rabbits
-
-
-
additional information
?
-
-
the enzyme may be involved in the development of atherosclerosis
-
-
-
additional information
?
-
-
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. The wild-type animal produces 3% 12-hydroperoxyicosatetraenoate and 97% 15-hydroperoxyicosatetraenoate
-
-
-
additional information
?
-
-
the major reaction products are identified as(8S,15S,5Z,9E,11Z,13E)-8,15-dihydroperoxy-5,9,11,13-eicosatetraenoic acid (8S,15S-DiHpETE) and (5S,15S,6E,8Z,11Z,13E)-5,15-dihydroperoxy-6,8,11,13-eicosatetraenoic acid (5S,15S-DiHPETE) and the stereochemistry of the reaction is compatible with an inverse substrate orientation
-
-
-
additional information
?
-
-
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview
-
-
-
additional information
?
-
H2QBX9
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview. The wild-type animal produces 20% 12-hydroperoxyicosatetraenoate and 80% 15-hydroperoxyicosatetraenoate with 135% overall activity compared to the human enzyme activity
-
-
-
additional information
?
-
A0A096P2G1
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview. The wild-type animal produces 78% 12-hydroperoxyicosatetraenoate and 22% 15-hydroperoxyicosatetraenoate with 37% overall activity compared to the human enzyme activity
-
-
-
additional information
?
-
Q5RBE8
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview
-
-
-
additional information
?
-
Q5RBE8
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview. The wild-type animal produces 14% 12-hydroperoxyicosatetraenoate and 86% 15-hydroperoxyicosatetraenoate
-
-
-
additional information
?
-
-
production of antiinflammatory lipid mediators by the enzyme may be a general strategy by which pathogens regulate the host-pathogen relationship
-
-
-
additional information
?
-
-
in the brain, the principal 12/15-LOX metabolites of arachidonate are (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate, cf. EC 1.13.11.31, and (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
additional information
?
-
Q02759
the major reaction products are identified as(8S,15S,5Z,9E,11Z,13E)-8,15-dihydroperoxy-5,9,11,13-eicosatetraenoic acid (8S,15S-DiHpETE) and (5S,15S,6E,8Z,11Z,13E)-5,15-dihydroperoxy-6,8,11,13-eicosatetraenoic acid (5S,15S-DiHPETE) and the stereochemistry of the reaction is compatible with an inverse substrate orientation
-
-
-
additional information
?
-
Q02759
in the brain, the principal 12/15-LOX metabolites of arachidonate are (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate, cf. EC 1.13.11.31, and (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Fe
Fe2+
Iron
Mg2+
Ca2+
-
enhances activity, reversible by EGTA, inhibited by phosphatidyl serine and phosphatidyl choline
Ca2+
-
in the presence of Ca2+, with or without calcium ionophore, the majority of 15-LO-1 is found in the membrane fraction, although significant amounts are also detected in the supernatant fraction
Ca2+
-
Ca2+ binds to the PLAT domain of 15-LOX-2, resulting in a translocation from the cytosol to the membrane
Ca2+
-
for maximal intracellular activity, 12/15-lipoxygenases require a rise in cytosolic calcium concentration inducing a translocation of the enzyme from the cytosol to cellular membranes
Fe2+
-
addition in a molar excess, more than 50:1 purified protein:Fe2+, leads to a 3fold increase in the specific activity
Fe2+
-
required for the catalytic cycle of fatty acid oxidation by lipoxygenase, overview
Fe2+
-
required, iron content of the 15-hLO isozymes determined with a Finnigan inductively coupled plasma mass spectrometer, ICP-MS, using cobalt-EDTA as an internal standard
Iron
-
the recombinant enzyme contains a variable amount of iron, often as low as 0.2 mol per mol of enzyme
Iron
-
the iron is liganded by four histidines at positions 361, 366, 541 and 545 asell as the C-terminal isoleucine
Mg2+
-
in the presence of Mg2+, with or without calcium ionophore, the majority of 15-LO-1 is found in the membrane fraction, although significant amounts are also detected in the supernatant fraction
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(-)-5,7-O-diacetyl-3',4',5'-O-triacetylepigallocatechin-3-O-(3'',4'',5''-O-triacetyl)gallate
-
IC50: 0.061 mM
(-)-5,7-O-dibutyryl-3',4',5'-O-tributyrylepigallocatechin-3-O-(3'',4'',5''-O-tributyryl) gallate
-
IC50: 0.033 mM
(-)-5,7-O-dimethyl-3',4',5'-O-trimethylepigallocatechin-3-O-(3'',4'',5''-O-trimethyl) gallate
-
IC50: 0.03 mM
(-)-5,7-O-dipropionyl-3',4',5'-O-tripropionylepigallocatechin-3-O-(3'',4'',5''-O-tripropionyl) gallate
-
IC50: 0.031 mM
1-(((2,4,6-trimethylphenyl)sulfonyl)oxy)-2,3-diphenyl-7-indolizinecarbonitrile
-
IC50: 0.017 mM
1-(((2,4-dimethoxyphenyl)sulfonyl)oxy)-2,3-diphenyl-7-indolizinecarbonitrile
-
IC50: 0.027 mM
1-(((2,5-dimethoxyphenyl)sulfonyl)oxy)-2,3-diphenyl-7-indolizinecarbonitrile
-
IC50: 0.015 mM
1-(((2-methyl)ethylsulfonyl)oxy)-2,3-diphenyl-7-indolizinecarbonitrile
-
IC50: 0.042 mM
1-(((2-methyl)sulfonyl)oxy)-2,3-diphenyl-7-indolizinecarbonitrile
-
IC50: 0.022 mM
1-(((2-thienyl)sulfonyl)oxy)-2,3-diphenyl-7-indolizinecarbonitrile
-
IC50: 0.021 mM
1-(((3,4-dimethoxyphenyl)sulfonyl)oxy)-2,3-diphenyl-7-indolizinecarbonitrile
-
IC50: 0.019 mM
1-(((3-thienyl)sulfonyl)oxy)-2,3-diphenyl-7-indolizinecarbonitrile
-
IC50: 0.023 mM
1-(((4-(2-methylethyl)phenl)sulfonyl)oxy)-2,3-diphenyl-7-indolizinecarbonitrile
-
IC50: 0.016 mM
1-(((4-chlorophenyl)sulfonyl)oxy)-2,3-diphenyl-7-indolizinecarbonitrile
-
IC50: 0.022 mM
1-(((4-methoxyphenyl)sulfonyl)oxy)-2,3-bis(4-methylphenyl)-7-indolizinecarbonitrile
-
IC50: 0.025 mM
1-(((4-methoxyphenyl)sulfonyl)oxy)-2,3-diphenyl-7-indolizinecarbonitrile
-
IC50: 0.025 mM
1-(((4-methylphenyl)sulfonyl)oxy)-2,3-bis(4-chlorophenyl)-7-indolizinecarbonitrile
-
IC50: 0.2 mM
1-(((4-methylphenyl)sulfonyl)oxy)-2,3-bis(4-fluorophenyl)-7-indolizinecarbonitrile
-
IC50: 0.22 mM
1-(((4-methylphenyl)sulfonyl)oxy)-2,3-bis(4-methoxyphenyl)-7-indolizinecarbonitrile
-
IC50: 0.024 mM
1-(((4-methylphenyl)sulfonyl)oxy)-2,3-bis(4-methylphenyl)-7-indolizinecarbonitrile
-
IC50: 0.2 mM
1-(((4-methylphenyl)sulfonyl)oxy)-2,3-dibutyl-7-indolizinecarbonitrile
-
IC50: 0.03 mM
1-(((4-methylphenyl)sulfonyl)oxy)-2,3-diethyl-7-indolizinecarbonitrile
-
IC50: 0.029 mM
1-(((4-methylphenyl)sulfonyl)oxy)-2,3-diphenyl-7-indolizinecarboxaldehyde
-
IC50: 0.02 mM
1-(((4-methylphenyl)sulfonyl)oxy)-2,3-diphenyl-7-indolizinylethanone
-
IC50: 0.023 mM
1-(((4-methysulfonyllphenyl)sulfonyl)oxy)-2,3-diphenyl-7-indolizinecarbonitrile
-
IC50: 0.024 mM
1-(((4-trifluoromethylphenyl)sulfonyl)oxy)-2,3-diphenyl-7-indolizinecarbonitrile
-
IC50: 0.023 mM
1-((4-methylphenyl)sulfonyl)2,3-diphenyl-7-indolizinecarbonitrile
-
IC50: 0.029 mM
1-((N,N-dimethylaminosulfonyl)oxy)-2,3-diphenyl-7-indolizinecarbonitrile
-
IC50: 0.025 mM
1-(1,3-dibenzyloxy-2-propyloxy)methoxy-2,3-diphenyl-7-indolizinecarbonitrile
-
IC50: 0.031 mM
1-(1-Hydroxy-1-phenyl-ethyl)-2,3-diphenyl-indolizine-7-carbonitrile
-
IC50: 0.017 mM
1-(2-methoxyphenyl)methoxy-2,3-diphenyl-7-indolizinecarbonitrile
-
IC50: 0.029 mM
1-(4-methoxyphenyl)methoxy-2,3-diphenyl-7-indolizinecarbonitrile
-
IC50: 0.032 mM
1-(4-tert-butylphenyl)-4-[4-(diphenylmethoxy)piperidin-1-yl]butan-1-one
-
1-(Cyclohexyl-hydroxy-methyl)-2,3-diphenyl-indolizine-7-carbonitrile
-
IC50: 0.023 mM
1-(Hydroxy-p-tolyl-methyl)-2,3-diphenyl-indolizine-7-carbonitrile
-
IC50: 0.022 mM
1-(hydroxymethyl)-2,3-diphenylindolizine-7-carbonitrile
-
IC50: 0.034 mM
1-(Methoxy-phenyl-methyl)-2,3-diphenyl-indolizine-7-carbonitrile
-
IC50: 0.021 mM
1-[(2H-1,3-benzodioxol-5-yl)carbamothioyl]-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
-
-
1-[(4-Chloro-phenyl)-hydroxy-methyl]-2,3-diphenyl-indolizine-7-carbonitrile
-
IC50: 0.023 mM
1-[1-[4,4-bis(4-fluorophenyl)butyl]piperidin-4-yl]-1,3-dihydro-2H-benzimidazol-2-one
-
1-[2-[bis(4-fluorophenyl)methoxy]ethyl]-4-(3-phenylpropyl)piperazine
-
1-[4-[4-([[5-(3-chlorophenyl)furan-2-yl]methyl]amino)phenyl]piperazin-1-yl]ethan-1-one
-
1-[bis(4-fluorophenyl)methyl]-4-[(2E)-3-phenylprop-2-en-1-yl]piperazine
-
1-[Hydroxy-(4-methoxy-phenyl)-methyl]-2,3-diphenyl-indolizine-7-carbonitrile
-
IC50: 0.017 mM
11-thialinoleic acid
-
is a noncompetitive inhibitor of 15-lipoxygenase-1 with respect to arachidonate or linoleic acid as substrates. Presence of inhibitor does not alter the product distribution for 15-lipoxygenase-1. It does not change the regioselectivity of 15-lipoxygenase-1
2,3-Dihydroxybenzoic acid
-
47.7% inhibition at 0.015 mM, active site binding structure
2,4-dihydroxybenzoic acid
-
49.9% inhibition at 0.015 mM, active site binding structure
2,5-dihydroxybenzoic acid
-
21.2% inhibition at 0.015 mM, active site binding structure
2,6-dibromo-4-[1-(3-bromo-4-hydroxyphenyl)-1-methylethyl]phenol
-
IC50: 0.005 mM
2-([4-[(4-fluorobenzyl)oxy]butyl]sulfanyl)-5-(naphthalen-1-yl)-1,3,4-oxadiazole
-
-
2-alkyl-6-hydroxy-4-H-benzopyran-4-one
-
weak inhibition of isozymes 15-hLO-1 and 15-hLO-2
2-hydroxybenzoic acid
-
46.0% inhibition at 0.015 mM, active site binding structure
2-[2-[2-(1-benzofuran-2-yl)-1H-indol-3-yl]ethyl]-1H-isoindole-1,3(2H)-dione
-
-
2-[4-[(1Z)-1,2-diphenylbut-1-en-1-yl]phenoxy]-N,N-dimethylethan-1-amine
-
3,4,5-Trihydroxybenzoic acid
-
60.5% inhibition at 0.015 mM, active site binding structure
3,4-dihydroxybenzoic acid
-
51.6% inhibition at 0.015 mM, active site binding structure; 73.3% inhibition at 0.015 mM, active site binding structure
3,5-Dihydroxybenzoic acid
-
58.1% inhibition at 0.015 mM, active site binding structure
3-(2-[[(4-pentylphenyl)sulfonyl]amino]ethyl)-1H-indole-6-carboxylic acid
-
-
3-(4-bromophenyl)-6-(4-chlorophenyl)-N-(2,4,4-trimethylpentan-2-yl)imidazo[2,1-b][1,3]thiazol-5-amine
-
-
3-(4-bromophenyl)-6-(4-chlorophenyl)-N-cyclohexylimidazo[2,1-b][1,3]thiazol-5-amine
-
-
3-(4-bromophenyl)-N-cyclohexyl-6-(2-nitrophenyl)imidazo[2,1-b][1,3]thiazol-5-amine
-
-
3-(4-methoxyphenyl)-6-phenyl-N-(2,4,4-trimethylpentan-2-yl)imidazo[2,1-b][1,3]thiazol-5-amine
-
protective activity of compound 5i against H2O2-induced cell death in differentiated PC12 cells
3-hydroxy-H-benzopyran-4-one derivatives
-
weak inhibition of isozymes 15-hLO-1 and 15-hLO-2
3-Hydroxybenzoic acid
-
47.6% inhibition at 0.015 mM, active site binding structure
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
4'-butyl-N-[2-(1H-indol-3-yl)ethyl]biphenyl-4-sulfonamide
-
IC50: 0.00053 mM in the presence of arachidonate, IC50: 0.0002 mM in the presence of linoleic acid
4'-ethyl-N-[2-(1H-indol-3-yl)ethyl]biphenyl-4-sulfonamide
-
IC50: 0.00026 mM in the presence of arachidonate, IC50: 0.00047 mM in the presence of linoleic acid
4'-tert-butyl-N-[2-(1H-indol-3-yl)ethyl]biphenyl-4-sulfonamide
-
IC50: 0.00027 mM in the presence of arachidonate, IC50: 0.00023 mM in the presence of linoleic acid
4-((5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)methyl)-benzyl-4-fluorobenzoate
-
-
4-(2-chlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
-
-
4-(3,4-dichlorophenyl)-N-methyl-1,2,3,4-tetrahydronaphthalen-1-amine
-
4-(3,4-dichlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
-
-
4-(3,4-dichlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
-
-
4-(5-(3-hydroxynaphthalen-2-yl)-1,3,4-oxadiazol-2-ylthio)-but-2-ynyl-4-fluorobenzoate
-
low solubility
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylamino)but-2-ynyl-thiophene-2-carboxylate
-
-
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-1H-indole-4-carboxylate
-
-
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-benzofuran-2-carboxylate
-
-
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-thiophene-2-carboxylate
-
-
4-(5-(naphthalen-1-yl)-1,3,4-thiadiazol-2-ylthio)but-2-ynyl-thiophene-2-carboxylate
-
low solubility
4-([2-[2-(1-benzofuran-2-yl)-1H-indol-3-yl]ethyl]sulfamoyl)-N-(3-hydroxypropyl)benzamide
-
-
4-([2-[2-(1-benzofuran-2-yl)-1H-indol-3-yl]ethyl]sulfamoyl)-N-(4-methoxyphenyl)benzamide
-
-
4-([2-[2-(1-benzofuran-2-yl)-1H-indol-3-yl]ethyl]sulfamoyl)-N-butylbenzamide
-
-
4-([2-[2-(1-benzofuran-2-yl)-1H-indol-3-yl]ethyl]sulfamoyl)-N-cyclohexylbenzamide
-
-
4-([2-[2-(1-benzofuran-2-yl)-1H-indol-3-yl]ethyl]sulfamoyl)-N-phenylbenzamide
-
-
4-([2-[2-(1-benzofuran-2-yl)-1H-indol-3-yl]ethyl]sulfamoyl)-N-[3-(dimethylamino)propyl]benzamide
-
-
4-([2-[2-(4-methoxyphenyl)-1H-indol-3-yl]ethyl]sulfamoyl)benzoic acid
-
-
4-butyl-N-[2-(1H-indol-3-yl)ethyl]benzenesulfonamide
-
IC50: 0.00307 mM in the presence of arachidonate, IC50: 0.004 mM in the presence of linoleic acid
4-butyl-N-[2-[2-(4-methoxyphenyl)-1H-indol-3-yl]ethyl]benzenesulfonamide
-
-
4-butyl-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
-
-
4-chloro-N-(2-chloro-4-fluorophenyl)-5-(difluoromethyl)-1H-pyrazole-3-carboxamide
-
-
4-chloro-N-(2-chloro-4-fluorophenyl)-5-(trifluoromethyl)-1H-pyrazole-3-carboxamide
-
-
4-ethyl-N-[2-(1H-indol-3-yl)ethyl]benzenesulfonamide
-
IC50: 0.01 mM in the presence of arachidonate, IC50: 0.01 mM in the presence of linoleic acid
4-hydroxy-3-methoxybenzoic acid
-
45.4% inhibition at 0.015 mM, active site binding structure
4-hydroxybenzoic acid
-
47.0% inhibition at 0.015 mM, active site binding structure
4-pentyl-N-(2-[2-phenyl-5-[4-(trifluoromethyl)phenyl]-1H-imidazol-4-yl]ethyl)benzenesulfonamide
-
-
4-pentyl-N-(2-[2-[4-(trifluoromethyl)phenyl]-1H-indol-3-yl]ethyl)benzenesulfonamide
-
-
4-pentyl-N-[2-(2-quinolin-3-yl-1H-indol-3-yl)ethyl]benzenesulfonamide
-
-
4-pentyl-N-[2-(5-phenyl-2-pyrazin-2-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
-
-
4-pentyl-N-[2-(5-phenyl-2-pyridin-2-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
-
-
4-pentyl-N-[2-(5-phenyl-2-pyridin-3-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
-
-
4-pentyl-N-[2-(5-phenyl-2-pyridin-4-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
-
-
4-pentyl-N-[2-(5-phenyl-2-thioformyl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
-
-
4-pentyl-N-[2-[5-(1H-pyrrol-2-yl)-1H-indol-3-yl]ethyl]benzenesulfonamide
-
-
4-pentyl-N-[3-(5-phenyl-2-thioformyl-1H-imidazol-4-yl)propyl]benzenesulfonamide
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 1-benzothiophene-2-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 1-benzothiophene-3-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 1H-imidazole-4-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2,4-difluorobenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2-fluorobenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2-fluoropyridine-3-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2-methoxybenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3,4,5-trichlorothiophene-2-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3,4,5-trifluorobenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3,4-difluorobenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-(trifluoromethyl)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-chloro-1-benzothiophene-2-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-chlorothiophene-2-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-fluorobenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(difluoromethoxy)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(methylsulfonyl)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(triazan-2-yl)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(trifluoromethoxy)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(trifluoromethyl)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-bromobenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-chloro-3-(trifluoromethyl)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-[(trifluoromethyl)sulfanyl]benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl cyclobutanecarboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl cyclopentanecarboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl cyclopropanecarboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl furan-2-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl naphthalene-2-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl thiophene-3-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]butyl 4-fluorobenzoate
-
-
4-[[5-(naphthalen-2-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-fluorobenzoate
-
-
4-{[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}but-2-yn-1-yl 4-chlorobenzoate
-
-
4-{[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}but-2-yn-1-yl 4-fluorobenzoate
-
-
4-{[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}but-2-yn-1-yl 4-methoxybenzoate
-
-
6,7-diphenylpyrrolo[1,2-b]pyridazin-5-yl trifluoromethanesulfonate
-
IC50: 0.043 mM
6-(2-nitrophenyl)-3-phenyl-N-(2,4,4-trimethylpentan-2-yl)imidazo[2,1-b][1,3]thiazol-5-amine
-
-
6-(4-nitrophenyl)-3-phenyl-N-(2,4,4-trimethylpentan-2-yl)imidazo[2,1-b][1,3]thiazol-5-amine
-
-
6-[4-([1,1'-biphenyl]-2-yl)piperazin-1-yl]-N-(1,2,3,4-tetrahydronaphthalen-1-yl)hexanamide
-
6-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]-1-phenylhexan-1-one
-
low solubility
7,8-dihydroxy-3'-trifluoromethylisoflavone
-
weak inhibition of isozyme 15-hLO-2
7-cyclopentyl-5-(4-phenoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine
-
7-hydroxy-H-benzopyran-4-one derivatives
-
weak inhibition of isozymes 15-hLO-1 and 15-hLO-2
8-[4,4-bis(4-fluorophenyl)butyl]-1-phenyl-1,3,8-triazaspiro[4.5]decan-4-one
-
alpha-mangostin
-
NSC30552, a natural product, caspase-3 pathway inhibitor, performs selective inhibition of 12-LO
arachidonic acid
-
autoinactivates 15-hLO-1 to a much greater extent than linoleic acid at high substrate concentrations. No autoinactivation at low substrate concentrations
conjugated linoleic acids
-
conjugated linoleic acids may function as inhibitors of 15-LO-1 activity in macrophages/in vivo, overview
-
ethyl 6-([3-[(2-chloro-4-fluorophenyl)carbamoyl]-1H-pyrazole-1-carbonyl]amino)hexanoate
-
-
GATA-6
-
inhibits non-steroidal anti-inflammatory drugs-induced transcription of 15-LOX-1 in colorectal cancer cells
-
methyl 11,17-dimethoxy-18-[(3,4,5-trimethoxybenzoyl)oxy]yohimban-16-carboxylate
-
methyl 3-(2-[[(4-pentylphenyl)sulfonyl]amino]ethyl)-1H-indole-6-carboxylate
-
-
michellamine B
-
NSC661755, potent but non-selective inhibitor, a natural anti-viral agent
N'-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
-
-
N'-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3S)-1-phenoxypyrrolidin-3-yl]sulfamide
-
-
N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
-
-
N-(2-chloro-4-fluorophenyl)-1-[3-(trifluoromethyl)benzene-1-sulfonyl]-1H-pyrazole-3-carboxamide
-
-
N-(2-chloro-4-fluorophenyl)-4,5-bis(trifluoromethyl)-1H-pyrazole-3-carboxamide
-
-
N-(2-chloro-4-fluorophenyl)-4-methyl-5-(trimethylsilyl)-1H-pyrazole-3-carboxamide
-
-
N-(2-chloro-4-fluorophenyl)-4-[(methanesulfonyl)amino]-1H-pyrazole-3-carboxamide
-
-