ArticleComputational and structural biotechnology journal2020
Desaturase specificity is controlled by the physicochemical properties of a single amino acid residue in the substrate binding tunnel.
Article in Computational and structural biotechnology journal, 2020. 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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Who cites it
5 citing papers in PubMed, 11 citations in OpenAlex.
- Metabolic Pathways and Molecular Regulatory Mechanisms of Nervonic Acid Biosynthesis inInternational journal of molecular sciences · 2026Review
- Structure and Function of Alkane Monooxygenase (AlkB).Accounts of chemical research · 2023Review
- Evolution of Linoleic Acid Biosynthesis Paved the Way for Ecological Success of Termites.Molecular biology and evolution · 2023Article
- The Torreya grandis genome illuminates the origin and evolution of gymnosperm-specific sciadonic acid biosynthesis.Nature communications · 2023Article
- Biosynthesis of Fatty Acid Derivatives by RecombinantJournal of fungi (Basel, Switzerland) · 2023Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane fatty acyl desaturases (mFAD) are ubiquitous enzymes in eukaryotes. They introduce double bonds into fatty acids (FAs), producing structurally diverse unsaturated FAs which serve as membrane lipid components or precursors of signaling molecules. The mechanisms controlling enzymatic specificity and selectivity of desaturation are, however, poorly understood. We found that the physicochemical properties, particularly side chain volume, of a single amino acid (aa) residue in insect mFADs (Lepidoptera:
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Registered trials
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