ArticleLipids2014
Four amino acid residues influence the substrate chain-length and regioselectivity of Siganus canaliculatus Δ4 and Δ5/6 desaturases.
Article in Lipids, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed.
- Lipidomic and transcriptomic analysis and its therapeutic implications in Chinese Kazakh patients with esophageal squamous cell carcinoma.BMC cancer · 2025Article
- The Torreya grandis genome illuminates the origin and evolution of gymnosperm-specific sciadonic acid biosynthesis.Nature communications · 2023Article
- A complete inventory of long-chain polyunsaturated fatty acid biosynthesis pathway enzymes in the miniaturized cyprinid Paedocypris micromegethes.Fish physiology and biochemistry · 2022Article
- Flatfishes colonised freshwater environments by acquisition of various DHA biosynthetic pathways.Communications biology · 2020Article
- The Relationship between the Expression of Fatty Acyl Desaturase 2 (Life (Basel, Switzerland) · 2020Article
- Identification of a crucial amino acid implicated in the hydroxylation/desaturation ratio of CpFAH12 bifunctional hydroxylase.Biotechnology and bioengineering · 2019Article
- Functional diversification of teleost Fads2 fatty acyl desaturases occurs independently of the trophic level.Scientific reports · 2019Article
- Structural Determinants of Substrate Specificity of Omega-3 Desaturases fromInternational journal of molecular sciences · 2019Article
- Characterization and molecular docking of new Δ17 fatty acid desaturase genes fromRSC advances · 2019Article
- Retention of fatty acyl desaturase 1 (fads1) in Elopomorpha and Cyclostomata provides novel insights into the evolution of long-chain polyunsaturated fatty acid biosynthesis in vertebrates.BMC evolutionary biology · 2018Article
- Purification and function analysis of the Δ-17 fatty acid desaturase with or without transmembrane domain.Experimental and therapeutic medicine · 2017Article
- Two alternative pathways for docosahexaenoic acid (DHA, 22:6n-3) biosynthesis are widespread among teleost fish.Scientific reports · 2017Article
- Identification of amino acid residues that determine the substrate specificity of mammalian membrane-bound front-end fatty acid desaturases.Journal of lipid research · 2016Article
- Evolution of moth sex pheromone composition by a single amino acid substitution in a fatty acid desaturase.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although ω3- and ω6- desaturases have been well studied in terms of substrate preference and regiospecificity, relatively little is known about the membrane-bound, "front-end" long chain fatty acid desaturases, such as ∆4, Δ5 or Δ6 desaturases. The first vertebrate ∆4 desaturase was recently identified in the marine teleost fish Siganus canaliculatus (S. canaliculatus), which also possesses a bifunctional Δ5/6 desaturase. These two long chain polyunsaturated fatty acid desaturases are very different in terms of regiospecificity and substrate chain-length, but share an unusually high degree of amino acid identity (83 %). We took advantage of this similarity by constructing a series of chimeric enzymes, replacing regions of one enzyme with the corresponding sequence of the other. Heterologous expression of the chimeric series of enzymes in yeast indicated that the substitution of a four amino acid region was sufficient to convert a ∆4 desaturase to an enzyme with ∆6 desaturase activity, and convert a ∆5/6 desaturase to an enzyme with a low level of ∆4 desaturase activity. In addition, enzymes having both ∆4 and ∆6 desaturase activities were produced by single or double amino acid substitutions within this four-amino acid region.
Indexed as
Identifiers
24477708What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.