Characterization of two fungal lipoxygenases expressed in Aspergillus oryzae

Sugio, Akiko; Østergaard, Lars; Matsui, Kenji; Takagi, Shinobu

doi:10.1016/j.jbiosc.2018.04.005

Cited by 16 publications

(14 citation statements)

References 40 publications

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“…LOXs are a group of nonheme iron‐containing dioxygenases that are encoded by a multigenic family ubiquitous in plants and mammals but also described in fungi, invertebrates, fish, algae, bacteria and microalgae (Ivanov et al ., 2010; Chen et al ., 2015; Zhu et al ., 2015; Teng et al ., 2017; Sugio et al ., 2018; Djian et al ., 2019). LOXs with manganese instead of iron in the active site also have been described in fungi (Oliw et al ., 2011).…”

Section: Introductionmentioning

confidence: 99%

Silencing of a Pseudo‐nitzschia arenysensis lipoxygenase transcript leads to reduced oxylipin production and impaired growth

et al. 2021

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Because of their importance as chemical mediators, the presence of a rich and varied family of lipoxygenase (LOX) products, collectively named oxylipins, has been investigated thoroughly in diatoms, and the involvement of these products in important processes such as bloom regulation has been postulated. Nevertheless, little information is available on the enzymes and pathways operating in these protists.Exploiting transcriptome data, we identified and characterized a LOX gene, PaLOX, in Pseudo-nitzschia arenysensis, a marine diatom known to produce different species of oxylipins by stereo-and regio-selective oxidation of eicosapentaenoic acid (EPA) at C12 and C15.PaLOX RNA interference correlated with a decrease of the lipid-peroxidizing activity and oxylipin synthesis, as well as with a reduction of growth of P. arenysensis. In addition, sequence analysis and structure models of the C-terminal part of the predicted protein closely fitted with the data for established LOXs from other organisms.The presence in the genome of a single LOX gene, whose downregulation impairs both 12and 15-oxylipins synthesis, together with the in silico 3D protein modelling suggest that PaLOX encodes for a 12/15S-LOX with a dual specificity, and provides additional support to the correlation between cell growth and oxylipin biosynthesis in diatoms.

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Section: Introductionmentioning

confidence: 99%

Silencing of a Pseudo‐nitzschia arenysensis lipoxygenase transcript leads to reduced oxylipin production and impaired growth

et al. 2021

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“…Hydroperoxyoctadecadienoic acids (HPODEs), i.e., the primary products of LA oxidation by porcine 12-LOXcd, were reduced to hydroxyoctadecadienoic acids (HODEs) by potassium borohydride. The reduction transforms chemically-active hydroperoxides into relatively stable hydroxides without changing their isomerization characteristics; the latter can then be conveniently and precisely detected by HPLC-based methods [ 23 , 29 ].…”

Section: Resultsmentioning

confidence: 99%

Recombinant Porcine 12-Lipoxygenase Catalytic Domain: Effect of Inhibitors, Selectivity of Substrates and Specificity of Oxidation Products of Linoleic Acid

Liu

et al. 2022

Foods

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Lipoxygenase (LOX) is a major endogenous enzyme for the enzymatic oxidation of lipids during meat storage and meat product manufacturing. In the present work, some characteristics, i.e., effects of inhibitors, selectivity of substrates and specificity of oxidation products, were studied using recombinant porcine 12-lipoxygenase catalytic domain (12-LOXcd). Several familiar inhibitors were found inhibit the activity of recombinant porcine 12-LOXcd;nordihydroguaiaretic acid demonstrated the strongest inhibitory effect. The enzyme could oxygenate common polyunsaturated fatty acids, and showed the highest affinity to linoleic acid (LA), followed by arachidonic acid (AA), linolenic acid (LN) and docosahexaenoic acid (DHA). Under the action of porcine 12-LOXcd, LA was oxidized into four hydroxyoctadecadienoic acid (HODE) isomers, i.e., 13-Z,E-HODE, 13-E,E-HODE, 9-Z,E-HODE and 9-E,E-HODE. Variation of pH not only affected the yield of LA oxidation products, but also the distribution of HODE isomers. These results indicated that endogenous LOX activity and LOX-catalyzed lipid oxidation can be regulated during meat storage and meat product manufacturing.

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“…The E. coli membrane fraction was mixed separately with 30 µM each of (9Z,11E,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoic acid (13HPOT), (10E,12Z,15Z)-9-hydroperoxyoctadeca-10,12,15-trienoic acid (9HPOT), (9Z,11E)-13-hydroperoxyoctadeca-9,11-dienoic acid (13HPOD), and (10E,12Z)-9-hydroperoxyoctadeca-10,12dienoic acid (9HPOD) in 50 mM MES-KOH (pH 6.0) at 25 • C. The HPO substrates were prepared from α-linolenic acid and linoleic acid (MilliporeSigma) with soybean lipoxygenase-1 partially purified from soybean seeds and Magnaporthe salvinii lipoxygenase provided by Novozyme Japan (Chiba, Japan) as described previously (Koeduka et al, 2015;Sugio et al, 2018). The compositions of HPOs were analyzed using the straight-phase HPLC system after reducing the hydroperoxide group to hydroxide with triphenylphosphine (Sugio et al, 2018). The contamination of the positional and geometrical isomers in each HPO preparation was mostly negligible except for 9HPOT, which contained 26.2% of 13HPOT (Supplementary Figure 2).…”

Section: Enzyme Assay and Product Analysismentioning

confidence: 99%

Green Leaf Volatile-Burst in Selaginella moellendorffii

2021

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Green leaf volatiles (GLVs) consist of six-carbon volatile aldehydes, alcohols, and their esters. They are formed from polyunsaturated fatty acids and are involved in the defense of plants against herbivores and pathogens. GLVs generally have low concentrations in intact healthy plant tissues, but the biosynthetic pathway to form GLVs is quickly activated by mechanical damage to tissues, an event called the GLV-burst. Most seed plants have the ability to implement GLV-burst; however, this potential in non-seed plants has not been extensively researched. In this study, we examined the GLV-burst capacity of monilophytes, lycophytes, and bryophytes, and confirmed that monilophytes and lycophytes showed substantial GLV-burst ability, while bryophytes did not, with a few exceptions. When the genome sequence of a model lycophyte, Selaginella moellendorffii was reviewed, 10 genes were found that showed high similarity with the non-canonical cytochrome P450 enzymes, CYP74s, specialized in oxylipin formation. Recombinant proteins expressed with Escherichia coli showed that one of them had the ability to encode allene oxide synthase, and another encoded hydroperoxide lyase (HPL), preferring linolenic acid 13-hydroperoxide, and it was inferred that this gene was responsible for GLV-burst in S. moellendorffii. Based on the phylogenetic tree constructed with CYP74s of non-seed and seed plants, we hypothesized that HPL was acquired independently in the lycophyte and seed plants through diversification of CYP74 genes.

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Characterization of two fungal lipoxygenases expressed in Aspergillus oryzae

Cited by 16 publications

References 40 publications

Silencing of a Pseudo‐nitzschia arenysensis lipoxygenase transcript leads to reduced oxylipin production and impaired growth

Silencing of a Pseudo‐nitzschia arenysensis lipoxygenase transcript leads to reduced oxylipin production and impaired growth

Recombinant Porcine 12-Lipoxygenase Catalytic Domain: Effect of Inhibitors, Selectivity of Substrates and Specificity of Oxidation Products of Linoleic Acid

Green Leaf Volatile-Burst in Selaginella moellendorffii

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