Proteins > Polyunsaturated fatty acid lipoxygenase ALOX12
Page last updated: 2024-08-07 13:04:17
Polyunsaturated fatty acid lipoxygenase ALOX12
A polyunsaturated fatty acid lipoxygenase ALOX12 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P18054]
Synonyms
EC 1.13.11.-;
Arachidonate (12S)-lipoxygenase;
12S-LOX;
12S-lipoxygenase;
1.13.11.31;
Arachidonate (15S)-lipoxygenase;
1.13.11.33;
Linoleate (13S)-lipoxygenase;
Lipoxin synthase 12-LO;
3.3.2.-;
Platelet-type lipoxy
Research
Bioassay Publications (19)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (10.53) | 18.2507 |
| 2000's | 6 (31.58) | 29.6817 |
| 2010's | 9 (47.37) | 24.3611 |
| 2020's | 2 (10.53) | 2.80 |
Compounds (41)
Drugs with Inhibition Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| chloroxine | Homo sapiens (human) | IC50 | 1.9000 | 1 | 1 |
| hexylresorcinol | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| masoprocol | Homo sapiens (human) | IC50 | 2.7780 | 5 | 5 |
| tetrabromobisphenol a | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| phenidone | Homo sapiens (human) | IC50 | 0.1000 | 1 | 1 |
| 2-bromophenol | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| 4-bromophenol | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| 3-hydroxyflavone | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| 3-bromophenol | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| 2,6-dibromophenol | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| 2,4-dibromophenol | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| zileuton | Homo sapiens (human) | IC50 | 55.0000 | 1 | 1 |
| 6-hydroxyflavone | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| puupehenone | Homo sapiens (human) | IC50 | 12.2000 | 2 | 2 |
| moracin c | Homo sapiens (human) | IC50 | 0.2100 | 1 | 1 |
| 3,6-dihydroxyflavone | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| N-[(5-chloro-8-hydroxy-7-quinolinyl)-(2-furanyl)methyl]acetamide | Homo sapiens (human) | IC50 | 3.0000 | 1 | 1 |
| 1-phenyl-2-[[4-(trifluoromethyl)phenyl]methylthio]imidazole | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| quercetin | Homo sapiens (human) | IC50 | 0.4400 | 1 | 1 |
| 15-keto-5,8,11,13-eicosatetraenoic acid | Homo sapiens (human) | IC50 | 1.0000 | 1 | 1 |
| baicalein | Homo sapiens (human) | IC50 | 31.5320 | 2 | 5 |
| baicalein | Homo sapiens (human) | Ki | 1.6000 | 1 | 1 |
| fisetin | Homo sapiens (human) | IC50 | 0.9500 | 1 | 1 |
| mangostin | Homo sapiens (human) | IC50 | 0.5800 | 1 | 1 |
| morusin | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| daidzein | Homo sapiens (human) | IC50 | 100.0000 | 1 | 2 |
| 7-hydroxyflavone | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| 5-oxo-6,8,11,14-eicosatetraenoic acid | Homo sapiens (human) | IC50 | 15.0000 | 1 | 1 |
| 6,7,4'-trihydroxyisoflavone | Homo sapiens (human) | IC50 | 8.7000 | 1 | 1 |
| 7-hydroxyisoflavone | Homo sapiens (human) | IC50 | 100.0000 | 1 | 2 |
| 3,7-dihydroxyflavone | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| 13-oxo-9,11-octadecadienoic acid | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| dysidenin | Homo sapiens (human) | Ki | 9.0000 | 1 | 1 |
| jaspaquinol | Homo sapiens (human) | IC50 | 50.0000 | 1 | 1 |
| N-[(5-chloro-8-hydroxy-7-quinolinyl)-cyclopropylmethyl]acetamide | Homo sapiens (human) | IC50 | 3.0000 | 1 | 1 |
| N-[(5-fluoro-8-hydroxy-7-quinolinyl)-thiophen-2-ylmethyl]acetamide | Homo sapiens (human) | IC50 | 2.0000 | 1 | 1 |
| N-[(5-bromo-8-hydroxy-7-quinolinyl)-(2-furanyl)methyl]propanamide | Homo sapiens (human) | IC50 | 2.0000 | 1 | 1 |
| N-[(5-bromo-8-hydroxy-7-quinolinyl)-thiophen-2-ylmethyl]acetamide | Homo sapiens (human) | IC50 | 9.8575 | 2 | 4 |
| ML355 | Homo sapiens (human) | IC50 | 0.3500 | 2 | 2 |
| ML355 | Homo sapiens (human) | Ki | 0.5350 | 2 | 2 |
| hydrazinocurcumin | Homo sapiens (human) | IC50 | 7.3000 | 1 | 1 |
Drugs with Other Measurements
Discovery of potent and selective inhibitors of human platelet-type 12- lipoxygenase.Journal of medicinal chemistry, , Aug-11, Volume: 54, Issue:15, 2011
Using enzyme assays to evaluate the structure and bioactivity of sponge-derived meroterpenes.Journal of natural products, , Volume: 72, Issue:10, 2009
Structure-activity relationship studies of flavonoids as potent inhibitors of human platelet 12-hLO, reticulocyte 15-hLO-1, and prostate epithelial 15-hLO-2.Bioorganic & medicinal chemistry, , Dec-01, Volume: 15, Issue:23, 2007
Exploring sponge-derived terpenoids for their potency and selectivity against 12-human, 15-human, and 15-soybean lipoxygenases.Journal of natural products, , Volume: 66, Issue:2, 2003
Structure-activity relationship studies of nordihydroguaiaretic acid inhibitors toward soybean, 12-human, and 15-human lipoxygenase.Journal of medicinal chemistry, , Jun-06, Volume: 45, Issue:12, 2002
Using enzyme assays to evaluate the structure and bioactivity of sponge-derived meroterpenes.Journal of natural products, , Volume: 72, Issue:10, 2009
Exploring sponge-derived terpenoids for their potency and selectivity against 12-human, 15-human, and 15-soybean lipoxygenases.Journal of natural products, , Volume: 66, Issue:2, 2003
In vitro study of isoflavones and isoflavans as potent inhibitors of human 12- and 15-lipoxygenases.Chemical biology & drug design, , Volume: 82, Issue:3, 2013
Discovery of potent and selective inhibitors of human platelet-type 12- lipoxygenase.Journal of medicinal chemistry, , Aug-11, Volume: 54, Issue:15, 2011
Structure-activity relationship studies of flavonoids as potent inhibitors of human platelet 12-hLO, reticulocyte 15-hLO-1, and prostate epithelial 15-hLO-2.Bioorganic & medicinal chemistry, , Dec-01, Volume: 15, Issue:23, 2007
Enables
This protein enables 6 target(s):
| Target | Category | Definition |
|---|
| arachidonate 12(S)-lipoxygenase activity | molecular function | Catalysis of the reaction: arachidonate + O2 = (5Z,8Z,10E,12S,14Z)-12-hydroperoxyicosa-5,8,10,14-tetraenoate. [EC:1.13.11.31, RHEA:10428] |
| iron ion binding | molecular function | Binding to an iron (Fe) ion. [GOC:ai] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| linoleate 13S-lipoxygenase activity | molecular function | Catalysis of the reaction: linoleate + O2 = (9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate. [EC:1.13.11.12, GOC:lb] |
| hepoxilin-epoxide hydrolase activity | molecular function | Catalysis of the reaction: (5Z,9E,14Z)-(8x,11R,12S)-11,12-epoxy-8-hydroxyicosa-5,9,14-trienoate + H2O = (5Z,9E,14Z)-(8x,11x,12S)-8,11,12-trihydroxyicosa-5,9,14-trienoate. [EC:3.3.2.7, MetaCyc:HEPOXILIN-EPOXIDE-HYDROLASE-RXN] |
| arachidonate 15-lipoxygenase activity | molecular function | Catalysis of the reaction: arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate. [EC:1.13.11.33] |
Located In
This protein is located in 5 target(s):
| Target | Category | Definition |
|---|
| cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
| cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
| membrane | cellular component | A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194] |
| sarcolemma | cellular component | The outer membrane of a muscle cell, consisting of the plasma membrane, a covering basement membrane (about 100 nm thick and sometimes common to more than one fiber), and the associated loose network of collagen fibers. [ISBN:0198506732] |
| extracellular exosome | cellular component | A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894] |
Active In
This protein is active in 2 target(s):
| Target | Category | Definition |
|---|
| cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
| sarcolemma | cellular component | The outer membrane of a muscle cell, consisting of the plasma membrane, a covering basement membrane (about 100 nm thick and sometimes common to more than one fiber), and the associated loose network of collagen fibers. [ISBN:0198506732] |
Involved In
This protein is involved in 15 target(s):
| Target | Category | Definition |
|---|
| lipid metabolic process | biological process | The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids. [GOC:ma] |
| negative regulation of muscle cell apoptotic process | biological process | Any process that decreases the rate or frequency of muscle cell apoptotic process, a form of programmed cell death induced by external or internal signals that trigger the activity of proteolytic caspases whose actions dismantle a muscle cell and result in its death. [GOC:dph, GOC:mtg_apoptosis, GOC:tb] |
| arachidonic acid metabolic process | biological process | The chemical reactions and pathways involving arachidonic acid, a straight chain fatty acid with 20 carbon atoms and four double bonds per molecule. Arachidonic acid is the all-Z-(5,8,11,14)-isomer. [ISBN:0198506732] |
| lipoxygenase pathway | biological process | The chemical reactions and pathways by which an unsaturated fatty acid (such as arachidonic acid or linolenic acid) is converted to other compounds, and in which the first step is hydroperoxide formation catalyzed by lipoxygenase. [GOC:mah, PMID:17163881] |
| fatty acid oxidation | biological process | The removal of one or more electrons from a fatty acid, with or without the concomitant removal of a proton or protons, by reaction with an electron-accepting substance, by addition of oxygen or by removal of hydrogen. [ISBN:0198506732, MetaCyc:FAO-PWY] |
| unsaturated fatty acid metabolic process | biological process | The chemical reactions and pathways involving an unsaturated fatty acid, any fatty acid containing one or more double bonds between carbon atoms. [GOC:mah] |
| superoxide anion generation | biological process | The enzymatic generation of superoxide, the superoxide anion O2- (superoxide free radical), or any compound containing this species, by a cell in response to environmental stress, thereby mediating the activation of various stress-inducible signaling pathways. [GOC:jl, PMID:12359750] |
| linoleic acid metabolic process | biological process | The chemical reactions and pathways involving linoleic acid, an unsaturated omega-6 fatty acid that has the molecular formula C18H32O2. [Wikipedia:Linoleic_Acid] |
| hepoxilin biosynthetic process | biological process | The chemical reactions and pathways resulting in the formation of hepoxilins, a class of bioactive icosanoids with roles in the regulation of cell physiology. [GOC:ai] |
| establishment of skin barrier | biological process | Establishment of the epithelial barrier, the functional barrier in the skin that limits its permeability. [GOC:dph] |
| negative regulation of platelet aggregation | biological process | Any process that decreases the rate, frequency or extent of platelet aggregation. Platelet aggregation is the adhesion of one platelet to one or more other platelets via adhesion molecules. [GOC:BHF] |
| leukotriene A4 metabolic process | biological process | The chemical reactions and pathways involving leukotriene A4. [GOC:TermGenie, GOC:yaf] |
| lipoxin A4 biosynthetic process | biological process | The chemical reactions and pathways resulting in the formation of lipoxin A4. Lipoxin A4 is a C20 hydroxy fatty acid having (5S)-, (6R)- and (15S)-hydroxy groups as well as (7E)- (9E)-, (11Z)- and (13E)-double bonds. [GOC:mw] |
| lipoxin B4 biosynthetic process | biological process | The chemical reactions and pathways resulting in the formation of lipoxin B4. Lipoxin B4 is a C20 hydroxy fatty acid having (5S)-, (14R)- and (15S)-hydroxy groups as well as (6E)- (8Z)-, (10E)- and (12E)-double bonds. [GOC:mw] |
| lipid oxidation | biological process | The removal of one or more electrons from a lipid, with or without the concomitant removal of a proton or protons, by reaction with an electron-accepting substance, by addition of oxygen or by removal of hydrogen. [GOC:BHF, GOC:mah] |