59985-28-3

Usage

InChI:InChI=1/C20H32O3/c1-2-3-4-5-10-13-16-19(21)17-14-11-8-6-7-9-12-15-18-20(22)23/h7-11,13-14,17,19,21H,2-6,12,15-16,18H2,1H3,(H,22,23)/b9-7+,11-8+,13-10+,17-14+

Upstream product

• 506-32-1 all cis 5,8,11,14-eicosatetraenoic acid 
• 200960-01-6 11,12-cis-epoxyeicosatrienoic acid 
• 98678-61-6 (2Z,6Z)-4-Oxo-dodeca-2,6-dienoic acid methyl ester 
• 98678-60-5 (2E,6Z)-4-Oxo-dodeca-2,6-dienoic acid methyl ester 
• 100311-67-9 (5Z,8Z,10E,14Z)-12-(tert-Butyl-diphenyl-silanyloxy)-icosa-5,8,10,14-tetraenoic acid methyl ester 
• 56630-33-2 non-3-ynoic acid 
• 98678-62-7 (2E,6Z)-4-(tert-Butyl-dimethyl-silanyloxy)-dodeca-2,6-dienoic acid methyl ester 
• 98678-58-1 2-Methoxy-5-((Z)-oct-2-enyl)-furan 
• 98678-59-2 methyl 4-hydroxy-2E,6Z-dodecadienoate 
• 126254-48-6 4-hydroxy-2E,6Z-dodecadienal 
• 25466-54-0 (Z)-1-bromo-2-octene 
• 20739-58-6 2-octyn-1-ol 
• 26001-58-1 (Z)-oct-2-en-1-ol 
• 98678-66-1 (5Z,8Z,10E,14Z)-12-Acetoxy-icosa-5,8,10,14-tetraenoic acid methyl ester 

Relevant academic research and scientific papers

Regiospecificity of a novel bacterial lipoxygenase from Myxococcus xanthus for polyunsaturated fatty acids

Lipoxygenase (LOX) is the key enzyme involved in the synthesis of oxylipins as signaling compounds that are important for cell growth and development, inflammation, and pathogenesis in various organisms. The regiospecificity of LOX from Myxococcus xanthus, a gram-negative bacterium, was investigated. The enzyme catalyzed oxygenation at the n-9 position in C20 and C22 polyunsaturated fatty acids (PUFAs) to form 12S- and 14S-hydroxy fatty acids (HFAs), respectively, and oxygenation at the n-6 position in C18 PUFAs to form 13-HFAs. The 12S-form products of C20 and C22 PUFAs by M. xanthus LOX is the first report of bacterial LOXs. The residues involved in regiospecificity were determined to be Thr397, Ala461, and Ile664 by analyzing amino acid alignment and a homology model based on human arachidonate 15-LOX with a sequence identity of 25%. Among these variants, the regiospecificity of the T397Y variant for C20 and C22 PUFAs was changed. This may be because of the reduced size of the substrate-binding pocket by substitution of the smaller Thr to the larger Tyr residue. The T397Y variant catalyzed oxygenation at the n-6 position in C20 and C22 PUFAs to form 15- and 17-hydroperoxy fatty acids, respectively. However, the oxygenation position of T397Y for C18 PUFAs was not changed. The discovery of bacterial LOX with novel regiospecificity will facilitate the biosynthesis of regiospecific?oxygenated signaling compounds.

Repurposing Resveratrol and Fluconazole to Modulate Human Cytochrome P450-Mediated Arachidonic Acid Metabolism

Cytochrome P450 (P450) enzymes metabolize arachidonic acid (AA) to several biologically active epoxyeicosatrienoic acids (EETs) and hydroxyeicosatetraenoic acids (HETEs). Repurposing clinically-approved drugs could provide safe and readily available means

Crystal structure of a lipoxygenase in complex with substrate: The arachidonic acid-binding site of 8R-lipoxygenase

Lipoxygenases (LOX) play critical roles in mammalian biology in the generation of potent lipid mediators of the inflammatory response; consequently, they are targets for the development of isoform-specific inhibitors. The regio- and stereo-specificity of the oxygenation of polyunsaturated fatty acids by the enzymes is understood in terms of the chemistry, but structural observation of the enzyme-substrate interactions is lacking. Although several LOX crystal structures are available, heretofore the rapid oxygenation of bound substrate has precluded capture of the enzyme-substrate complex, leaving a gap between chemical and structural insights. In this report, we describe the 2.0 ? resolution structure of 8R-LOX in complex with arachidonic acid obtained under anaerobic conditions. Subtle rearrangements, primarily in the side chains of three amino acids, allow binding of arachidonic acid in a catalytically competent conformation. Accompanying experimental work supports a model in which both substrate tethering and cavity depth contribute to positioning the appropriate carbon at the catalytic machinery.

Physcomitrella patens has lipoxygenases for both eicosanoid and octadecanoid pathways

Mosses have substantial amounts of long chain C20 polyunsaturated fatty acids, such as arachidonic and eicosapentaenoic acid, in addition to the shorter chain C18 α-linolenic and linoleic acids, which are typical substrates of lipoxygenases in flowering p

Total synthesis of 12(R)-HETE, 12(S)-HETE, 2H2-12(R)-HETE and LTB4 from racemic glycidol via hydrolytic kinetic resolution

The total synthesis of 12(R)-HETE, 12(S)-HETE (Samuelsson's HETE), [14,15-2H2]-12(R)-HETE and Leukotriene B4 from racemic glycidol is described. The key steps are the hydrolytic kinetic resolution of racemic TES-glycidol with salen-Co catalyst and the selective oxidation of primary silyl ethers, in the presence of secondary ones, under Swern conditions to give a short entry to both enantiomers of 12-HETE and LTB4.

Oxidation of oxa and thia fatty acids and related compounds catalysed by 5- and 15-lipoxygenase

The modified fatty acids, (Z,Z,Z)-(octadeca-6,9,12-trienyloxy)acetic acid, (Z,Z,Z)-(octadeca-9,12,15-trienyloxy)acetic acid, (all-Z)-(eicosa-5,8,11,14-tetraenyloxy)acetic acid, (all-Z)-(eicosa-5,8,11,14-tetraenylthio)acetic acid, 3-[(all-Z)-(eicosa-5,8,11,14-tetraenylthio)]propionic acid, (all-Z)-(eicosa-5,8,11,14-tetraenylthio)succinic acid, N-[(all-Z)-(eicosa-5,8,11,14-tetraenoyl)]glycine and N-[(all-Z)-(eicosa-5,8,11,14-tetraenoyl)]aspartic acid, all react with soybean 15-lipoxygenase. The products were treated with triphenylphosphine to give alcohols, which were isolated using HPLC. Analysis of the alcohols using negative ion tandem electrospray mass spectrometry, and by comparison with compounds obtained by autoxidation of arachidonic acid, shows that each enzyme-catalysed oxidation occurs at the ω-6 position of the substrate. In a similar fashion, it has been found that (Z,Z,Z)-(octadeca-6,9,12-trienyloxy)acetic acid, (Z,Z,Z)-(octadeca-9,12,15-trienyloxy)acetic acid, (all-Z)-(eicosa-5,8,11,14-tetraenylthio)acetic acid and 3-[(all-Z)-(eicosa-5,8,11,14-tetraenylthio)]propionic acid each undergoes regioselective oxidation at the carboxyl end of the polyene moiety on treatment with potato 5-lipoxygenase. Neither (all-Z)-(eicosa-5,8,11,14-tetraenylthio)succinic acid nor N-[(all-Z)-(eicosa-5,8,11,14-tetraenoyl)]aspartic acid reacts in the presence of this enzyme, while N-[(all-Z)-(eicosa-5,8,11,14-tetraenoyl)]glycine affords the C11′ oxidation product. The alcohol derived from (Z,Z,Z)-(octadeca-6,9,12-trienyloxy)acetic acid using the 15-lipoxygenase reacts at the C6′ position with the 5-lipoxygenase.

A short catalytic enantioselective synthesis of the proinflammatory eicosanoid 12(R)-hydroxy-5(Z),8(Z),10(E),14(Z)-eicosatetraenoic acid (12(R)-HETE)

(equation presented) A new and effective pathway is described for the synthesis of 12(R)-HETE and the 12(S)-enantiomer from the common intermediates 4 and 8.

A new practical enantiospecific synthesis of unlabelled and tritium labelled 12-HETEs

The oxidative metabolism of arachidonic acid AA is known to yield a variety of biologically active substances.Among them, both enantiomers of 12-hydroxyeicosatetraenoic acid (12-HETE) have been the subject of much interest.In order to extend their biologi

Stereospecific Total Synthesis of Dimorphecolic Acid, 5(S)-HETE, and 12(S)-Hete

First enantiospecific synthesis of dimorphecolic acid is accomplished via an efficient and stereocontrolled route.The convenient synthesis of 5(S)-HETE and 12(S)-HETE is also described.