LMPD Database

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LMP000895

UniProt Annotations

Entry Information
Gene Namearachidonate 8-lipoxygenase
Protein EntryALOX8_MOUSE
UniProt IDO35936
SpeciesMouse
Comments
Comment typeDescription
Biophysicochemical PropertiesKinetic parameters: KM=1.2 uM for arachidonate (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:16112079}; KM=2.1 uM for (8S)-HPETE (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:16112079}; KM=5.7 uM for (8S)-HETE (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:16112079}; KM=39 uM for (15S)-HPETE (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:16112079}; KM=15 uM for (15S)-HETE (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:16112079}; Note=The highest catalytic efficiency is observed with arachidonate followed by (8S)-HPETE and(15S)-HPETE with similar efficiencies.;
Catalytic ActivityArachidonate + O(2) = (5Z,9E,11Z,14Z)-8- hydroperoxyicosa-5,9,11,14-tetraenoate. {ECO:0000269|PubMed:10625675, ECO:0000269|PubMed:16112079, ECO:0000269|PubMed:16143298}.
CautionDespite its homology with human ALOX15B (AC O15296), it seems not to have any 15S-lipoxygenase activity on arachidonate. Based on its catalytic activity it is referred to as the mouse arachidonate 8S-lipoxygenase. {ECO:0000305}.
CofactorName=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726}; Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE- ProRule:PRU00726};
DomainThe PLAT domain can bind calcium ions; this promotes association with membranes. {ECO:0000250}.
FunctionNon-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Catalyzes the peroxidation of arachidonate and linoleate into (8S)-HPETE and (9S)-HPODE respectively. From arachidonate mainly produces (8S)-HPETE and in addition, minor products derived from (8S)-HPETE itself that may include leukotriene A4 and 8,15-diHPETE. With arachidonate as substrate, has no detectable 15S-lipoxygenase activity and only displays a 8S-lipoxygenase activity. However, it may have a 15S-lipoxygenase activity with (8S)-HPETE to produce (8S,15S)-diHPETE. May also catalyze (15S)-HPETE peroxidation to produce 8,15-diHPETE. May play a role in keratinocyte differentiation through activation of the peroxisome proliferator activated receptor signaling pathway. {ECO:0000269|PubMed:10625675, ECO:0000269|PubMed:10965849, ECO:0000269|PubMed:16143298, ECO:0000269|PubMed:9305900}.
InductionBy phorbol ester. {ECO:0000269|PubMed:9305900}.
PathwayLipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis.
SimilarityBelongs to the lipoxygenase family. {ECO:0000305}.
SimilarityContains 1 lipoxygenase domain. {ECO:0000255|PROSITE- ProRule:PRU00726}.
SimilarityContains 1 PLAT domain. {ECO:0000255|PROSITE- ProRule:PRU00152}.
Subcellular LocationCytoplasm, cytosol {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Predominantly cytosolic; becomes enriched at membranes upon calcium binding. {ECO:0000250}.
Tissue SpecificityExpressed in epidermis and brain. No expression found in heart, spleen, liver, skeletal muscle, kidney or testis. {ECO:0000269|PubMed:9305900, ECO:0000269|PubMed:9518531}.