ArticleJournal of lipid research2016
Crystal structure of a lipoxygenase from Cyanothece sp. may reveal novel features for substrate acquisition.
Article in Journal of lipid research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 40 citations in OpenAlex.
- Bacterial lipoxygenases for fatty acid oxyfunctionalization: advances and future directions.Applied microbiology and biotechnology · 2026Review
- Octadecanoids as emerging lipid mediators in cnidarian-dinoflagellate symbiosis.Communications biology · 2025Article
- Understanding the role of oxylipins inFrontiers in plant science · 2025Review
- Versatile ferrous oxidation-xylenol orange assay for high-throughput screening of lipoxygenase activity.Applied microbiology and biotechnology · 2024Article
- Conformational Dynamics of Lipoxygenases and Their Interaction with Biological Membranes.International journal of molecular sciences · 2024Review
- Discovery of α-Linolenic Acid 16(International journal of molecular sciences · 2023Article
- Computational Insights and In Silico Characterization of a Novel Mini-Lipoxygenase from Nostoc Sphaeroides and Its Application in the Quality Improvement of Steamed Bread.International journal of molecular sciences · 2023Article
- Characterization and Preliminary Application of a Novel Lipoxygenase fromFoods (Basel, Switzerland) · 2022Article
- Plastidic membrane lipids are oxidized by a lipoxygenase inFrontiers in plant science · 2022Article
- An ensemble of lipoxygenase structures reveals novel conformations of the Fe coordination sphere.Protein science : a publication of the Protein Society · 2019Article
- 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
- Consensus design for improved thermostability of lipoxygenase from Anabaena sp. PCC 7120.BMC biotechnology · 2018Article
- Jasmonates: News on Occurrence, Biosynthesis, Metabolism and Action of an Ancient Group of Signaling Compounds.International journal of molecular sciences · 2018Review
- Lipoxygenase 2 from Cyanothece sp. controls dioxygen insertion by steric shielding and substrate fixation.Scientific reports · 2017Article
- Crystal structure of linoleate 13R-manganese lipoxygenase in complex with an adhesion protein.Journal of lipid research · 2016Article
- Crystal Structure of Manganese Lipoxygenase of the Rice Blast Fungus Magnaporthe oryzae.The Journal of biological chemistry · 2016Article
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Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In eukaryotes, oxidized PUFAs, so-called oxylipins, are vital signaling molecules. The first step in their biosynthesis may be catalyzed by a lipoxygenase (LOX), which forms hydroperoxides by introducing dioxygen into PUFAs. Here we characterized CspLOX1, a phylogenetically distant LOX family member from Cyanothece sp. PCC 8801 and determined its crystal structure. In addition to the classical two domains found in plant, animal, and coral LOXs, we identified an N-terminal helical extension, reminiscent of the long α-helical insertion in Pseudomonas aeruginosa LOX. In liposome flotation studies, this helical extension, rather than the β-barrel domain, was crucial for a membrane binding function. Additionally, CspLOX1 could oxygenate 1,2-diarachidonyl-sn-glycero-3-phosphocholine, suggesting that the enzyme may act directly on membranes and that fatty acids bind to the active site in a tail-first orientation. This binding mode is further supported by the fact that CspLOX1 catalyzed oxygenation at the n-10 position of both linoleic and arachidonic acid, resulting in 9R- and 11R-hydroperoxides, respectively. Together these results reveal unifying structural features of LOXs and their function. While the core of the active site is important for lipoxygenation and thus highly conserved, peripheral domains functioning in membrane and substrate binding are more variable.
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