111004-08-1

Usage

Uses

Used in Pharmaceutical Industry:
9(S)-HPOT is used as a pharmaceutical agent for its potential anti-inflammatory and immunomodulatory properties. It is involved in the biosynthesis of leukotrienes, which play a crucial role in the inflammatory response and immune system regulation.
Used in Research Applications:
9(S)-HPOT is used as a research tool for studying the role of 5-lipoxygenase and its metabolites in various biological processes. It helps researchers understand the mechanisms of inflammation, immune response, and other related pathways.
Used in Nutritional Supplements:
9(S)-HPOT may be used as a nutritional supplement to support healthy inflammatory response and immune function. Its potential anti-inflammatory properties can contribute to overall well-being and promote a balanced immune system.

InChI:InChI=1/C18H30O4/c1-2-3-4-5-6-8-11-14-17(22-21)15-12-9-7-10-13-16-18(19)20/h3-4,6,8,11,14,17,21H,2,5,7,9-10,12-13,15-16H2,1H3,(H,19,20)/b4-3-,8-6-,14-11+/t17-/m1/s1

Upstream product

• 463-40-1 (9Z,12Z,15Z)-octadeca-9-12,15-trienoic acid 

Downstream Products

• 3788-56-5 9-hydroxynonanoic acid 
• 52591-16-9 (3′ E)-colnelenic acid 
• 52591-16-9 colnelenic acid 
• 125559-74-2 9-oxo-(10E,12Z,15Z)-octadecatrienoic acid 
• 89886-42-0 (9S,10E,12Z,15Z)-9-hydroxyoctadeca-10,12,15-trienoic acid 

Relevant academic research and scientific papers

Efficient syntheses of (10E,12Z,15Z)-9-oxo- and (9Z,11E,15E)-13-oxo-octadecatrienoic acids; two stress metabolites of wounded plants

Configurationally pure 9-oxo-10E,12Z,15Z- and 13-oxo-9Z,11E,15E-octadecatrienoic acid are available from linolenic acid via regioselective functionalisation using lipoxygenases from soybean or tomato at specific pH conditions. Reduction of the resulting hydroperoxides followed by oxidation of the resulting allylic alcohols with Bobbitt's reagent yields the configurationally pure but labile ketotrienoic acids 4 and 5 without concomitant isomerisation.

Conversion of α-Linolenic Acid to Dihydro(pero)xyoctadecatrienoic Acid Isomers by Soybean and Potato Lipoxygenases

Difference in the conversion of α-linolenic acid into dihydroxyoctadecatrienoic acids by plant lipoxygenases was examined.Reduction of the products from the incubation of α-linolenic acid or 9(S)-hydroperoxyoctadecatrienoic acid with soybean lipoxygenase 1 or potato lipoxygenase gave rise to the formation of two 12-cis isomers and two 12-trans isomers of 9(S),16-dihydroxyoctadecatrienoic acid on the basis of UV and GC/MS spectra analyses and cistrans isomerization analyses.Further studies indicated that 12-cis isomers of 9(S),16-dihydroxyoctadecatrienoic acid are derived from the reduction of 9(S),16-dihydroperoxyoctadecatrienoic acid, a product from another lipoxygenation of 9(S)-hydroperoxyoctadecatrienoic acid at C-16, whereas 12-trans isomers of 9(S),16-dihydroxyoctadecatrienoic acid are supposed to be formed mainly from an epoxide intermediate.In support of the latter assumption, 9(S),10-dihydroxyoctadecatrienoic acid were produced from the incubation of α-linolenic acid with potato lipoxygenase, and the homolytic cleavage of 9(S)-hydroperoxyoctadecatrienoic acid by hemoglobin was observed to produce two isomers of 12-trans-9(S),16-dihydroxyoctadecatrienoic acid as major dihydroxy acids.Whereas the exposure of α-linolenic acid to soybean lipoxygenase 1 gave rise to 12-cis-9(S),16-dihydroperoxyoctadecatrienoic acid, a double lipoxygenation product, as a major product, 12-trans-9(S),16-dihydroxyoctadecatrienoic acid isomers were obtained as predominant products in the incubation of potato lipoxygenase with α-linolenic acid Keywords: Lipoxygenase; α-linolenic acid; dioxygenation; epoxide; 9-hydroperoxyoctadecatrienoic acid; 9,16-dihydroxyoctadecatrienoic acid

The CYP74B and CYP74D divinyl ether synthases possess a side hydroperoxide lyase and epoxyalcohol synthase activities that are enhanced by the site-directed mutagenesis

The CYP74 family of cytochromes P450 includes four enzymes of fatty acid hydroperoxide metabolism: allene oxide synthase (AOS), hydroperoxide lyase (HPL), divinyl ether synthase (DES), and epoxyalcohol synthase (EAS). The present work is concerned with catalytic specificities of three recombinant DESs, namely, the 9-DES (LeDES, CYP74D1) of tomato (Solanum lycopersicum), 9-DES (NtDES, CYP74D3) of tobacco (Nicotiana tabacum), and 13-DES (LuDES, CYP74B16) of flax (Linum usitatissimum), as well as their alterations upon the site-directed mutagenesis. Both LeDES and NtDES converted 9-hydroperoxides of linoleic and α?linolenic acids to divinyl ethers colneleic and colnelenic acids (respectively) with only minorities of HPL and EAS products. In contrast, LeDES and NtDES showed low efficiency towards the linoleate 13-hydroperoxide, affording only the low yield of epoxyalcohols. LuDES exhibited mainly the DES activity towards α?linolenate 13-hydroperoxide (preferred substrate), and HPL activity towards linoleate 13-hydroperoxide, respectively. In contrast, LuDES converted 9-hydroperoxides primarily to the epoxyalcohols. The F291V and A287G mutations within the I-helix groove region (SRS-4) of LuDES resulted in the loss of DES activity and the acquirement of the epoxyalcohol synthase activity. Thus, the studied enzymes exhibited the versatility of catalysis and its qualitative alterations upon the site-directed mutagenesis.

Epoxyalcohol Synthase RjEAS (CYP74A88) from the Japanese Buttercup (Ranunculus japonicus): Cloning and Characterization of Catalytic Properties

Cytochromes P450 of the CYP74 family play a key role in the lipoxygenase cascade generating oxylipins (products of polyunsaturated fatty acid oxidation). The CYP74 family includes allene oxide synthases, hydroperoxide lyases, divinyl ether synthases, and epoxyalcohol synthases. In this work, we cloned the CYP74A88 gene from the Japanese buttercup (Ranunculus japonicus) and studied the properties of the encoded recombinant protein. The CYP74A88 enzyme specifically converts linoleic acid 9-and 13-hydroperoxides to oxiranyl carbinols 9,10-epoxy-11-hydroxy-12-octadecenoic acid and 11-hydroxy-12,13-epoxy-9-octadecenoic acid, respectively, which was confirmed by GC-MS analysis and kinetic studies. Therefore, the CYP74A88 enzyme is a specific epoxyalcohol synthase.

Allene Oxide Synthase Pathway in Cereal Roots: Detection of Novel Oxylipin Graminoxins

Young roots of wheat, barley, and sorghum, as well as methyl jasmonate pretreated rice seedlings, undergo an unprecedented allene oxide synthase pathway targeted to previously unknown oxylipins 1–3. These Favorskii-type products, (4Z)-2-pentyl-4-tridecene-1,13-dioic acid (1), (2′Z)-2-(2′-octenyl)-decane-1,10-dioic acid (2), and (2′Z,5′Z)-2-(2′,5′-octadienyl)-decane-1,10-dioic acid (3), have a carboxy function at the side chain, as revealed by their MS and NMR spectral data. Compounds 1–3 were the major oxylipins detected, along with the related α-ketols. Products 1–3 were biosynthesized from (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid, (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid (9-HPOD), and (9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid, respectively, via the corresponding allene oxides and cyclopropanones. The data indicate that conversion of the allene oxide into the cyclopropanone is controlled by soluble cyclase. The short-lived cyclopropanones are hydrolyzed to products 1–3. The collective name “graminoxins” has been ascribed to oxylipins 1–3.