Compounds > 9-hydroperoxy-11-12-octadecadienoic-acid

9-hydroperoxy-11-12-octadecadienoic-acid and 15-hydroxy-5-8-11-13-17-eicosapentaenoic-acid

9-hydroperoxy-11-12-octadecadienoic-acid has been researched along with 15-hydroxy-5-8-11-13-17-eicosapentaenoic-acid* in 1 studies

Other Studies

1 other study(ies) available for 9-hydroperoxy-11-12-octadecadienoic-acid and 15-hydroxy-5-8-11-13-17-eicosapentaenoic-acid

Article	Year
Identification of CYP443D1 (CYP74 clan) of Nematostella vectensis as a first cnidarian epoxyalcohol synthase and insights into its catalytic mechanism. Biochimica et biophysica acta. Molecular and cell biology of lipids, 2017, Volume: 1862, Issue:10 Pt A The CYP74 clan enzymes are responsible for the biosynthesis of numerous bioactive oxylipins in higher plants, some Proteobacteria, brown and green algae, and Metazoa. A novel putative CYP74 clan gene CYP443D1 of the starlet sea anemone (Nematostella vectensis, Cnidaria) has been cloned, and the properties of the corresponding recombinant protein have been studied in the present work. The recombinant CYP443D1 was incubated with the 9- and 13-hydroperoxides of linoleic and α-linolenic acids (9-HPOD, 13-HPOD, 9-HPOT, and 13-HPOT, respectively), as well as with the 9-hydroperoxide of γ-linolenic acid (γ-9-HPOT) and 15-hydroperoxide of eicosapentaenoic acid (15-HPEPE). The enzyme was active towards all C Topics: Animals; Catalysis; Cloning, Molecular; Cytochrome P-450 Enzyme System; Eicosapentaenoic Acid; Linoleic Acids; Lipid Peroxides; Sea Anemones; Substrate Specificity	2017

Article

Year

Identification of CYP443D1 (CYP74 clan) of Nematostella vectensis as a first cnidarian epoxyalcohol synthase and insights into its catalytic mechanism.

Biochimica et biophysica acta. Molecular and cell biology of lipids, 2017, Volume: 1862, Issue:10 Pt A

The CYP74 clan enzymes are responsible for the biosynthesis of numerous bioactive oxylipins in higher plants, some Proteobacteria, brown and green algae, and Metazoa. A novel putative CYP74 clan gene CYP443D1 of the starlet sea anemone (Nematostella vectensis, Cnidaria) has been cloned, and the properties of the corresponding recombinant protein have been studied in the present work. The recombinant CYP443D1 was incubated with the 9- and 13-hydroperoxides of linoleic and α-linolenic acids (9-HPOD, 13-HPOD, 9-HPOT, and 13-HPOT, respectively), as well as with the 9-hydroperoxide of γ-linolenic acid (γ-9-HPOT) and 15-hydroperoxide of eicosapentaenoic acid (15-HPEPE). The enzyme was active towards all C

Topics: Animals; Catalysis; Cloning, Molecular; Cytochrome P-450 Enzyme System; Eicosapentaenoic Acid; Linoleic Acids; Lipid Peroxides; Sea Anemones; Substrate Specificity

2017