Enzymatic Oxidation of Polyunsaturated Fatty Acids

Murphy, Sharon Ann; Al-Aaswad, Naser; Nicolaou, Anna

doi:10.1201/b18138-5

Cited by 2 publications

(2 citation statements)

References 210 publications

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“…These reactions are now quite well understood and have been described in detail in several recent reviews [7–9] , showing that the structure of the parent lipid and the site of radical damage determine the products. There are also enzymatic pathways for producing oxidized fatty acids and phospholipids, starting with cytochrome P450 enzymes, lipoxygenases and cyclooxygenases; products of the latter are further metabolized by a variety of prostaglandin synthases [10] . Many of the products generated by both enzymatic and non-enzymatic pathways are reactive and electrophilic owing to the presence of carbonyl groups (aldehydes or ketones) or α, β-unsaturated moieties, and can be categorized into five principal groups: alkanals (and hydroxyalkanals), 2-alkenals, 4-hydroxy–2-alkenals, keto-alkenals, and alkanedial (dialdehydes) [3] .…”

Section: Types Of Oxidized Lipids That Generate Adductsmentioning

confidence: 99%

Protein lipoxidation: Detection strategies and challenges

et al. 2015

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Enzymatic and non-enzymatic lipid metabolism can give rise to reactive species that may covalently modify cellular or plasma proteins through a process known as lipoxidation. Under basal conditions, protein lipoxidation can contribute to normal cell homeostasis and participate in signaling or adaptive mechanisms, as exemplified by lipoxidation of Ras proteins or of the cytoskeletal protein vimentin, both of which behave as sensors of electrophilic species. Nevertheless, increased lipoxidation under pathological conditions may lead to deleterious effects on protein structure or aggregation. This can result in impaired degradation and accumulation of abnormally folded proteins contributing to pathophysiology, as may occur in neurodegenerative diseases. Identification of the protein targets of lipoxidation and its functional consequences under pathophysiological situations can unveil the modification patterns associated with the various outcomes, as well as preventive strategies or potential therapeutic targets. Given the wide structural variability of lipid moieties involved in lipoxidation, highly sensitive and specific methods for its detection are required. Derivatization of reactive carbonyl species is instrumental in the detection of adducts retaining carbonyl groups. In addition, use of tagged derivatives of electrophilic lipids enables enrichment of lipoxidized proteins or peptides. Ultimate confirmation of lipoxidation requires high resolution mass spectrometry approaches to unequivocally identify the adduct and the targeted residue. Moreover, rigorous validation of the targets identified and assessment of the functional consequences of these modifications are essential. Here we present an update on methods to approach the complex field of lipoxidation along with validation strategies and functional assays illustrated with well-studied lipoxidation targets.

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Section: Types Of Oxidized Lipids That Generate Adductsmentioning

confidence: 99%

Protein lipoxidation: Detection strategies and challenges

et al. 2015

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“…The study above suggested that a ω-hydroxydecanoic acid biosynthesis system with high efficiency has been established. It was demonstrated that AlkBGT is known to catalyze the oxyfunctionalization of medium-chain alkanes and fatty acids (Kusunose et al, 1964; Eggink et al, 1987). To further explore the substrate spectrum of this engineered whole-cell catalysis system of NH03 (pBGT- fadL ), octanoic acid and dodecanoic acid, which are medium-chain fatty acids, were employed as substrates.…”

Section: Resultsmentioning

confidence: 99%

Biosynthesis of Medium-Chain ω-Hydroxy Fatty Acids by AlkBGT of Pseudomonas putida GPo1 With Native FadL in Engineered Escherichia coli

Bennett

San

et al. 2019

Front. Bioeng. Biotechnol.

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Hydroxy fatty acids (HFAs) are valuable compounds that are widely used in medical, cosmetic and food fields. Production of ω-HFAs via bioconversion by engineered Escherichia coli has received a lot of attention because this process is environmentally friendly. In this study, a whole-cell bio-catalysis strategy was established to synthesize medium-chain ω-HFAs based on the AlkBGT hydroxylation system from Pseudomonas putida GPo1. The effects of blocking the β-oxidation of fatty acids (FAs) and enhancing the transportation of FAs on ω-HFAs bio-production were also investigated. When fadE and fadD were deleted, the consumption of decanoic acid decreased, and the yield of ω-hydroxydecanoic acid was enhanced remarkably. Additionally, the co-expression of the FA transporter protein, FadL, played an important role in increasing the conversion rate of ω-hydroxydecanoic acid. As a result, the concentration and yield of ω-hydroxydecanoic acid in NH03(pBGT-fadL) increased to 309 mg/L and 0.86 mol/mol, respectively. This whole-cell bio-catalysis system was further applied to the biosynthesis of ω-hydroxyoctanoic acid and ω-hydroxydodecanoic acid using octanoic acid and dodecanoic acid as substrates, respectively. The concentrations of ω-hydroxyoctanoic acid and ω-hydroxydodecanoic acid reached 275.48 and 249.03 mg/L, with yields of 0.63 and 0.56 mol/mol, respectively. This study demonstrated that the overexpression of AlkBGT coupled with native FadL is an efficient strategy to synthesize medium-chain ω-HFAs from medium-chain FAs in fadE and fadD mutant E. coli strains.

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Enzymatic Oxidation of Polyunsaturated Fatty Acids

Cited by 2 publications

References 210 publications

Protein lipoxidation: Detection strategies and challenges

Protein lipoxidation: Detection strategies and challenges

Biosynthesis of Medium-Chain ω-Hydroxy Fatty Acids by AlkBGT of Pseudomonas putida GPo1 With Native FadL in Engineered Escherichia coli

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