ArticlePhytochemistry2016
Characterization of an epoxide hydrolase from the Florida red tide dinoflagellate, Karenia brevis.
Article in Phytochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed.
- Recent Advances in the Detection of Food Toxins Using Mass Spectrometry.Chemical research in toxicology · 2023Review
- Essential components of the xanthophyll cycle differ in high and low toxin Karenia brevis.Harmful algae · 2021Article
- Soluble Epoxide Hydrolase Inhibition in Liver Diseases: A Review of Current Research and Knowledge Gaps.Biology · 2020Review
- Ladder-Shaped Ion Channel Ligands: Current State of Knowledge.Marine drugs · 2017Review
- Marine Biotoxins: Occurrence, Toxicity, Regulatory Limits and Reference Methods.Frontiers in microbiology · 2016Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Epoxide hydrolases (EH, EC 3.3.2.3) have been proposed to be key enzymes in the biosynthesis of polyether (PE) ladder compounds such as the brevetoxins which are produced by the dinoflagellate Karenia brevis. These enzymes have the potential to catalyze kinetically disfavored endo-tet cyclization reactions. Data mining of K. brevis transcriptome libraries revealed two classes of epoxide hydrolases: microsomal and leukotriene A4 (LTA4) hydrolases. A microsomal EH was cloned and expressed for characterization. The enzyme is a monomeric protein with molecular weight 44kDa. Kinetic parameters were evaluated using a variety of epoxide substrates to assess substrate selectivity and enantioselectivity, as well as its potential to catalyze the critical endo-tet cyclization of epoxy alcohols. Monitoring of EH activity in high and low toxin producing cultures of K. brevis over a three week period showed consistently higher activity in the high toxin producing culture implicating the involvement of one or more EH in brevetoxin biosynthesis.
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Registered trials
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