lipoxygenases การใช้

• Some examples of iron metalloproteins are ferritin and rubredoxin . lipoxygenases, and IRE-BP.
• The lipoxygenases are related to each other based upon their similar genetic structure and dioxygenation activity.
• The flavonoid has been shown to inhibit certain types of lipoxygenases and act as an anti-inflammatory agent.
• This serial metabolism may occur in different cell types that express only one of the two lipoxygenases in a process termed transcellular metabolism.
• Two lipoxygenases may act in series to make di-hydroxy or tri-hydroxy products that have activities quite different than either lipoxyenases'products.
• Hence, model Alox5 studies in rodents appear to be valuable for defining the function of ALOX5 in humans ( see lipoxygenase # Mouse lipoxygenases ).
• Dioxygenases include lipoxygenases ( plants, animals, fungi ), heme-dependent fatty acid oxygenases ( plants, fungi ), and cyclooxygenases ( animals ).
• The distribution of ALOXE3 and Aloxe3 ( see Tissue distribution, above ) suggests that these lipoxygenases may serve functions not only in the skin but also in other tissues.
• Structural analogies have been recognised between a developmental protein ( Dickkopf ), the pancreatic lipase C-terminal domain, the N-terminal domains of lipoxygenases and the C-terminal domain of alpha-toxin.
• ALOX12B, like most of the other lipoxygenases, possesses dioxygenase ( EC 1.13.11 ) activity : it catalyzes the incorporate dioxygen ( i . e . molecular oxygen [ O 2 ] ) into a single substrate.
• This hepoxilin is esterified to sphinganine in a lipid complex termed EOS ( i . e . esterified omega-hydroxyacyl-sphingosine, see Lipoxygenase # Biological function and classification # Human lipoxygenases ) that also contains a very long chain fatty acid.
• Lipoxygenases are found in plants, including fungi, and animals; while the third domain of terrestrial life, the archaea, possesses proteins with a slight ( ~ 20 % ) amino acid sequence similarity to lipoxygenases, these proteins lack iron-binding residues and therefore are not projected to possess lipoxygenase activity.
• Lipoxygenases are found in plants, including fungi, and animals; while the third domain of terrestrial life, the archaea, possesses proteins with a slight ( ~ 20 % ) amino acid sequence similarity to lipoxygenases, these proteins lack iron-binding residues and therefore are not projected to possess lipoxygenase activity.
• The " ALOX5 " gene, which occupies 71.9 kilobase pairs ( kb ) on chromosome 10 ( all other human lipoxygenases are clustered together on chromosome 17 ), is composed of 14 exons divided by 13 introns encoding the mature 78 kilodalton ( kD ) ALOX5 protein consisting of 673 amino acids.
• However, transfection of HEK293 human embryonic kidney cells with each of the 6 rat lipoxygenases, including rat eLOX3, found that hepoxilin B3 production required eLOX3; furthermore, the development of inflammation-induced tactile pain hypersensitivity ( hyperesthesia; tactile Allodynia ) in rats required eLOX3-dependent production of hepoxilin B3 by spinal tissue.
• LA is converted by various lipoxygenases, cyclooxygenases, certain cytochrome P450 enzymes ( the CYP monooxygenases ), and non-enzymatic autooxidation mechanisms to mono-hydroxyl products viz ., 13-Hydroxyoctadecadienoic acid and 9-Hydroxyoctadecadienoic acid; these two hydroxy metabolites are enzymatically oxidized to their keto metabolites, 13-oxo-octadecadienoic acid and 9-oxo-octadecdienoic acid.
• "' Lipoxygenases "'( ) are a family of ( non-heme ), iron-containing enzymes most of which catalyze the dioxygenation of polyunsaturated fatty acids in lipids containing a cis, cis-1, 4-pentadiene into cell signaling agents that serve diverse roles as autocrine signals that regulate the function of their parent cells, paracrine signals that regulate the function of nearby cells, and endocrine signals that regulate the function of distant cells.
• Human ALOX12 and ALOX15 along with rodent leukocyte-type " Alox12 " and " Alox15 " are commonly termed 12 / 15-lipoxygenases based on their ability to metabolize arachidonic acid to both 12 ( " S " )-HpETE and 15 ( " S " )-HpETE and to conduct this same metabolism on arachidonic acid that is esterified to membrane phospholipids; human ALOX15B makes 15 ( " S " )-HpETE but not 12 ( " S " )-HpETE and therefore is not regarded as a 12 / 15-lipoxygenase.