ArticleProteins2006
Crystal structures of vegetative soybean lipoxygenase VLX-B and VLX-D, and comparisons with seed isoforms LOX-1 and LOX-3.
Article in Proteins, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed, 63 citations in OpenAlex.
- Description of the rate-limiting hydrogen tunneling mechanism for plant 9- and 13-lipoxygenases.Protein science : a publication of the Protein Society · 2026Article
- Understanding the role of oxylipins inFrontiers in plant science · 2025Review
- Design, synthesis, and pharmacological evaluation of indazole carboxamides of N-substituted pyrrole derivatives as soybean lipoxygenase inhibitors.Molecular diversity · 2024Article
- Discovery of α-Linolenic Acid 16(International journal of molecular sciences · 2023Article
- Recombinant Soybean Lipoxygenase 2 (GmLOX2) Acts Primarily as a ω6(Current issues in molecular biology · 2023Article
- Oxylipin signaling in salt-stressed soybean is modulated by ligand-dependent interaction of Class II acyl-CoA-binding proteins with lipoxygenase.The Plant cell · 2022Article
- Insights into topology and membrane interaction characteristics of plastoglobule-localized AtFBN1a and AtLOX2.Plant signaling & behavior · 2021Article
- Lipoxygenase Inhibition Activity of Coumarin Derivatives-QSAR and Molecular Docking Study.Pharmaceuticals (Basel, Switzerland) · 2020Article
- EPR Spectroscopic Studies of Lipoxygenases.Chemistry, an Asian journal · 2020Review
- ALLENE OXIDE SYNTHASE and HYDROPEROXIDE LYASE, Two Non-Canonical Cytochrome P450s inInternational journal of molecular sciences · 2019Review
- Substrate channeling in oxylipin biosynthesis through a protein complex in the plastid envelope of Arabidopsis thaliana.Journal of experimental botany · 2019Article
- Article
- Crystal Structure of Manganese Lipoxygenase of the Rice Blast Fungus Magnaporthe oryzae.The Journal of biological chemistry · 2016Article
- Programmed chloroplast destruction during leaf senescence involves 13-lipoxygenase (13-LOX).Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The structural basis for specificity in lipoxygenase catalysis.Protein science : a publication of the Protein Society · 2015Review
- Article
- Evolutionary aspects of lipoxygenases and genetic diversity of human leukotriene signaling.Progress in lipid research · 2015Review
- Connecting lipoxygenase function to structure by electron paramagnetic resonance.Accounts of chemical research · 2014Article
- Fluctuations of an exposed π-helix involved in lipoxygenase substrate recognition.Biochemistry · 2014Article
- Crystallization and preliminary crystallographic analysis of manganese lipoxygenase.Acta crystallographica. Section F, Structural biology communications · 2014Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The lipoxygenase family of lipid-peroxidizing, nonheme iron dioxygenases form products that are precursors for diverse physiological processes in both plants and animals. In soybean (Glycine max), five vegetative isoforms, VLX-A, VLX-B, VLX-C, VLX-D, VLX-E, and four seed isoforms LOX-1, LOX-2, LOX-3a, LOX-3b have been identified. In this study, we determined the crystal structures of the substrate-free forms of two major vegetative isoforms, with distinct enzymatic characteristics, VLX-B and VLX-D. Their structures are similar to the two seed isoforms, LOX-1 and LOX-3, having two domains with similar secondary structural elements: a beta-barrel N-terminal domain containing highly flexible loops and an alpha-helix-rich C-terminal catalytic domain. Detailed comparison of the structures of these two vegetative isoforms with the structures of LOX-1 and LOX-3 reveals important differences that help explain distinct aspects of the activity and positional specificity of these enzymes. In particular, the shape of the three branches of the internal subcavity, corresponding to substrate-binding and O(2) access, differs among the isoforms in a manner that reflects the differences in positional specificities.
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