ArticleThe Journal of biological chemistry2010
A bisallylic mini-lipoxygenase from cyanobacterium Cyanothece sp. that has an iron as cofactor.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 58 citations in OpenAlex.
- Activation and execution of lipoxygenase catalysis.Redox biochemistry and chemistry · 2026Article
- Bacterial lipoxygenases for fatty acid oxyfunctionalization: advances and future directions.Applied microbiology and biotechnology · 2026Review
- The Octadecanoids: Synthesis and Bioactivity of 18-Carbon Oxygenated Fatty Acids in Mammals, Bacteria, and Fungi.Chemical reviews · 2025Review
- Promising Anti-Inflammatory Tools: Biomedical Efficacy of Lipoxins and Their Synthetic Pathways.International journal of molecular sciences · 2023Review
- Characterization and Preliminary Application of a Novel Lipoxygenase fromFoods (Basel, Switzerland) · 2022Article
- C-ferroptosis is an iron-dependent form of regulated cell death in cyanobacteria.The Journal of cell biology · 2022Article
- Plastidic membrane lipids are oxidized by a lipoxygenase inFrontiers in plant science · 2022Article
- Anti-Inflammatory and Anticancer Properties of Bioactive Compounds fromMolecules (Basel, Switzerland) · 2019Review
- The green microalga Lobosphaera incisa harbours an arachidonate 15S-lipoxygenase.Plant biology (Stuttgart, Germany) · 2019Article
- Stabilization and improved activity of arachidonate 11Journal of lipid research · 2018Article
- Biotransformation of polyunsaturated fatty acids to bioactive hepoxilins and trioxilins by microbial enzymes.Nature communications · 2018Article
- Lipoxygenase 2 from Cyanothece sp. controls dioxygen insertion by steric shielding and substrate fixation.Scientific reports · 2017Article
- Crystal Structure of Manganese Lipoxygenase of the Rice Blast Fungus Magnaporthe oryzae.The Journal of biological chemistry · 2016Article
- Article
- Crystal structure of a lipoxygenase from Cyanothece sp. may reveal novel features for substrate acquisition.Journal of lipid research · 2016Article
- Manganese lipoxygenase of F. oxysporum and the structural basis for biosynthesis of distinct 11-hydroperoxy stereoisomers.Journal of lipid research · 2015Article
- Evolutionary aspects of lipoxygenases and genetic diversity of human leukotriene signaling.Progress in lipid research · 2015Review
- Secretion of two novel enzymes, manganese 9S-lipoxygenase and epoxy alcohol synthase, by the rice pathogen Magnaporthe salvinii.Journal of lipid research · 2013Article
- An iron 13S-lipoxygenase with an α-linolenic acid specific hydroperoxidase activity from Fusarium oxysporum.PloS one · 2013Article
- Catalytic convergence of manganese and iron lipoxygenases by replacement of a single amino acid.The Journal of biological chemistry · 2012Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipoxygenases are enzymes that are found ubiquitously in higher animals and plants, but have only recently been identified in a number of bacteria. The genome of the diazotrophic unicellular cyanobacterium Cyanothece sp. harbors two genes with homology to lipoxygenases. Here we describe the isolation of one gene, formerly named csplox2. It was cloned, and the protein was expressed in Escherichia coli and purified. The purified enzyme belongs to the group of prokaryotic mini lipoxygenases, because it had a molecular mass of 65 kDa. Interestingly, it catalyzed the conversion of linoleic acid, the only endogenously found polyunsaturated fatty acid, primarily to the bisallylic hydroperoxide 11R-hydroperoxyoctadecadienoic acid. This product had previously only been described for the manganese lipoxygenase from the take all fungus, Gaeumannomyces graminis. By contrast, CspLOX2 was shown to be an iron lipoxygenase. In addition, CspLOX2 formed a mixture of typical conjugated lipoxygenase products, e.g. 9R- and 13S-hydroperoxide. The conversion of linoleic acid took place with a maximum reaction rate of 31 s(-1). Incubation of the enzyme with [(11S)-(2)H]linoleic acid led to the formation of hydroperoxides that had lost the deuterium label, thus suggesting that CspLOX2 catalyzes antarafacial oxygenation as opposed to the mechanism of manganese lipoxygenase. CspLOX2 could also oxidize diarachidonylglycerophosphatidylcholine with similar specificity as the free fatty acid, indicating that binding of the substrate takes place with a "tail-first" orientation. We conclude that CspLOX2 is a novel iron mini-lipoxygenase that catalyzes the formation of bisallylic hydroperoxide as the major product.
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