18320-18-8Relevant academic research and scientific papers
Kinetic isotope effects in the oxidation of arachidonic acid by soybean lipoxygenase-1
Jacquot, Cyril,Peng, Sheng,van der Donk, Wilfred A.
, p. 5959 - 5962 (2008)
The reaction of soybean lipoxygenase-1 with linoleic acid has been extensively studied and displays very large kinetic isotope effects. In this work, substrate and solvent kinetic isotope effects as well as the viscosity dependence of the oxidation of arachidonic acid were investigated. The hydrogen atom abstraction step was rate-determining at all temperatures, but was partially masked by a viscosity-dependent step at ambient temperatures. The observed KIEs on kcat were large (～100 at 25 °C).
PURIFICATION AND PROPERTIES OF LIPOXYGENASE IN MARCHANTIA POLYMORPHA CULTURED CELLS
Matsui, Kenji,Narahara, Hiroko,Kajiwara, Tadahiko,Hatanaka, Akikazu
, p. 1499 - 1502 (1991)
Lipoxygenase activity has been detected in cultured cells of a bryophyte, Marchantia polymorpha (liverwort).The activity was enhanced in the stationary phase.Most of the activity occurred in the cytosolic fraction.The lipoxygenase was purified to homogeneity by ammonium sulphate fractionation and hydrophobic, ion-exchange, and gel filtration chromatography.From the SDS-polyacrylamide gel electrophoresis, the Mr of the lipoxygenase was estimated as 109600.The pH optimum was ca 9.0 and the pI was 4.8.This enzyme formed mainly 13-(S)-hydroperoxy-(9Z,11E)-octadecadienoic acid from linoleic acid.It showed twice the activity for γ-linolenic acid than for linoleic acid. Key Word Index - Marchantia polymorpha; Marchantiaceae; liverwort; purification; lipoxygenase.
The autooxidation process in linoleic acid screened by Raman spectroscopy
MacHado,De Carvalho, L. A. E. Batista,Otero,Marques
, p. 1991 - 2000 (2012)
The chemical changes associated to the autooxidation process of linoleic acid (LA) were detected by Raman spectroscopy and interpreted in the light of density functional theory (DFT) calculations performed for both the fatty acid and its main oxidation products. The present methodology, applied for a six-day period upon induction of oxidation (through heating), allowed to understand the chemical modifications occurring during the oxidation process. Raman spectroscopy was shown to be a suitable and reliable technique for assessing the oxidation degree of fatty acid samples, particularly pure fatty acids, mainly when computational methods are used alongside to predict the spectral features of the distinct chemical entities involved. Screening of the oxidation process was mostly based on the loss of intensity of the bands assigned to LA cis-double bonds. Copyright
Chemoenzymatic production of (+)-coriolic acid from trilinolein: Coupled synthesis and extraction
Gargouri, Mohamed,Legoy, Marie Dominique
, p. 641 - 645 (1997)
Chemoenzymatic conversion of trilinolein to (+)-coriolic acid was investigated in this work. Lipase-catalyzed hydrolysis of trilinolein and lipoxygenation of liberated linoleic acid were coupled in a two-phase medium that consisted of a pH 9 borate buffer and a water-immiscible organic solvent (octane). High concentrations of trilinolein could be dissolved in the organic phase (up to 340 mM). Linoleic acid, liberated after hydrolysis, transferred to the aqueous phase and was enzymatically converted to the preferred 13(S)-hydroperoxy-9Z, 11E-octadecadienoic acid with soybean lipoxygenase-1. This product, which remained in the aqueous phase, could be recovered by centrifugation and then chemically reduced to (+)-coriolic acid (purity >95%). Recovery of this compound by liquid-liquid extraction was easy. The structure of (+)-coriolic acid has been confirmed by 1H nuclear magnetic resonance spectroscopy, mass spectrometry, and infrared spectroscopy. High yields were obtained with pure trilinolein or sunflower oil as initial substrates.
Enantioselective formation of an α, β-epoxy alcohol by reaction of methyl 13(S)-hydroperoxy-9(Z),11(E)-octadecadienoate with titanium isopropoxide
Piazza,Foglia,Nunez
, p. 1385 - 1390 (1997)
Methyl 11(R), 12(R)-epoxy-13(S)-hydroxy-9(Z)-octadecenoate (threo isomer) was generated from linoleic acid by the sequential action of an enzyme and two chemical reagents. Linoleic acid was treated with lipoxygenase to yield its corresponding hydroperoxide [13(S)-hydroperoxy-9(Z),11(E)-octadecadienoic acid]. After methylation with CH2N2, the hydroperoxide was treated with titanium (IV) isopropoxide [Ti(O-i-Pr)4] at 5 °C for 1 h. The products were separated by normal-phase high-performance liquid chromatography and characterized with gas chromatography-mass spectrometry, infrared spectroscopy, and nuclear magnetic resonance spectroscopy. Approximately 30% of the product was methyl 13(S)-hydroxy-9(Z),11(E)-octadecadienoate. Over 60% of the isolated product was methyl 11(R),12(R)-epoxy-13(S)-hydroxy-9(Z)-octadecenoate. After quenching Ti(O-i-Pr)4 with water, the spent catalyst could be removed from the fatty products by partitioning between CH2Cl2 and water. These results demonstrate that Ti(O-i-Pr)4 selectively promotes the formation of an α-epoxide with the threo configuration. It was critically important to start with dry methyl 13(S)-hydroperoxy-9(Z),11(E)-octadecadienoate because the presence of small amounts of water in the reaction medium resulted in the complete hydrolysis of epoxy alcohol to trihydroxy products.
Reaction targets of antioxidants in azo-initiator or lipid hydroperoxide induced lipid peroxidation
Saito, Kota,Matsuoka, Yuta,Yamada, Ken-ichi
, p. 301 - 310 (2020)
Lipid peroxidation (LPO) is reported to be involved in the pathogenesis of several oxidative diseases, and several therapeutic approaches using antioxidants have been proposed. LPO is thought to progress via a complicated series of multistep reactions suggesting that the activity of each antioxidant may be different, and depends on the reacting molecules. Hence, in this study, we evaluated the inhibitory mechanisms of several antioxidants toward arachidonic acid (AA) peroxidation induced by the azo initiator 2,2’-azobis(2-amidinopropane) dihydrochloride (AAPH) or a lipid hydroperoxide, hydroperoxyoctadecadienoic acid (HpODE)/hemin. Edaravone, ferrostatin-1, TEMPO and trolox effectively inhibited the production of malondialdehyde (MDA) and several oxidised AAs generated in the AAPH-induced LPO because of their scavenging ability toward lipid peroxyl radicals. In contrast, ebselen and ferrostatin-1 showed strong antioxidative activity in the HpODE/hemin-induced peroxidation. Under this condition, ebselen and ferrostatin-1 were thought to reduce HpODE and its derived alkoxyl radicals to the corresponding lipid alcohols. In conclusion, we found that each antioxidant had different antioxidative activities that prevented the progression of LPO. We expect that these findings will contribute to the design of novel therapeutic strategies using an appropriate antioxidant targeted to each step of the development of oxidative stress diseases.
The hydroperoxide moiety of aliphatic lipid hydroperoxides is not affected by hypochlorous acid
Zschaler, Josefin,Arnhold, Juergen
, p. 42 - 51 (2014)
The oxidation of polyunsaturated fatty acids to the corresponding hydroperoxide by plant and animal lipoxygenases is an important step for the generation of bioactive lipid mediators. Thereby fatty acid hydroperoxide represent a common intermediate, also in human innate immune cells, like neutrophil granulocytes. In these cells a further key component is the heme protein myeloperoxidase producing HOCl as a reactive oxidant. On the basis of different investigation a reaction of the fatty acid hydroperoxide and hypochlorous acid (HOCl) could be assumed. Here, chromatographic and spectrometric analysis revealed that the hydroperoxide moiety of 15S-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoic acid (15-HpETE) and 13S-hydroperoxy-9Z,11E-octadecadienoic acid (13-HpODE) is not affected by HOCl. No reduction of the hydroperoxide group due to a reaction with HOCl could be measured. It could be demonstrated that the double bonds of the fatty acid hydroperoxides are the major target of HOCl, present either as reagent or formed by the myeloperoxidase-hydrogen peroxide-chloride system.
Synthesis of 13R,20-dihydroxy-docosahexaenoic acid by site-directed mutagenesis of lipoxygenase derived from Oscillatoria nigro-viridis PCC 7112
Yi, Jong-Jae,Heo, Sun-Yeon,Ju, Jung-Hyun,Oh, Baek-Rock,Son, Woo Sung,Seo, Jeong-Woo
, p. 893 - 898 (2020)
Lipoxygenases (LOXs) are implicated in the biosynthesis of pro- and anti-inflammatory lipid mediators involved in immune cell signaling, most of which catalyze peroxidation of polyunsaturated fatty acids by distinct regio- and stereoselectivity. Current reports suggested that conserved amino acid, Gly in R-LOXs and Ala in S-LOXs, in the catalytic domain play an important role in determining the position as well as the stereochemistry of the functional group. Recently, we have confirmed that the catalytic specificity of cyanobacterial lipoxygenase, named Osc-LOX, with alanine at 296 was 13S-type toward linoleic acid, and producing a 17S- hydroxy-docosahexaenoic acid from docosahexaenoic acid (DHA). Here, we aimed to change the catalytic property of LOX from13S-LOX to 9R-LOX by replacing Ala with Gly and to produce a lipid mediators different from the wild-type using DHA. Finally, we succeeded in generating human endogenous a 13R-hydroxy-docosahexaenoic acid and a 13R,20-dihydroxy-docosahexaenoic acid from DHA through an enzymatic reaction using the Osc-LOX-A296G. Our study could enable physiological studies and pharmaceutical research for the 13R,20-dihydroxy-docosahexaenoic acid.
Lipoxygenase inhibitory activity of anacardic acids
Ha, Tae Joung,Kubo, Isao
, p. 4350 - 4354 (2005)
6[8′(2)-Pentadecenyl]salicylic acid, otherwise known as anacardic acid (C15:1), inhibited the linoleic acid peroxidation catalyzed by soybean lipoxygenase-1 (EC 1.13.11.12, type 1) with an IC50 of 6.8 μM. The inhibition of the enzyme by anacardic acid (C15:1) is a slow and reversible reaction without residual activity. The inhibition kinetics analyzed by Dixon plots indicates that anacardic acid (C15:1) is a competitive inhibitor and the inhibition constant, K1, was obtained as 2.8 μM. Although anacardic acid (C15:1) inhibited the linoleic acid peroxidation without being oxidized, 6[8′(Z),11′(Z)-pentadecadienyl]salicylic acid, otherwise known as anacardic acid (C15:2), was dioxygenated at low concentrations as a substrate. In addition, anacardic acid (C15:2) was also found to exhibit time-dependent inhibition of lipoxygenase-1. The alk(en)yl side chain of anacardic acids is essential to elicit the inhibitory activity. However, the hydrophobic interaction alone is not enough because cardanol (C15:1), which possesses the same side chain as anacardic acid (C15:1), acted neither as a substrate nor as an inhibitor.
LOXPsa1, the first recombinant lipoxygenase from a basidiomycete fungus
Plagemann, Ina,Zelena, Katerina,Arendt, Philipp,Ringel, Peter D.,Krings, Ulrich,Berger, Ralf G.
, p. 99 - 104 (2013)
A dioxygenase from the edible basidiomycete Pleurotus sapidus, originally researched because of its distinct ability to convert the sequiterpene (+)-valencene to the valuable grapefruit aroma (+)-nootkatone, was identified as a potent lipoxygenase (LOXsu
