ArticleComputational and structural biotechnology journal2016
Classification and substrate head-group specificity of membrane fatty acid desaturases.
Article in Computational and structural biotechnology journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 25 citations in OpenAlex.
- The Specificities of Lysophosphatidic Acid Acyltransferase and Fatty Acid Desaturase Determine the High Content of Myristic and Myristoleic Acids inInternational journal of molecular sciences · 2024Article
- Acyl-Lipid ΔBiomolecules · 2022Article
- Desaturases: Structural and mechanistic insights into the biosynthesis of unsaturated fatty acids.IUBMB life · 2022Review
- Membrane fatty acid desaturase: biosynthesis, mechanism, and architecture.Applied microbiology and biotechnology · 2022Review
- Δ6 fatty acid desaturases in polyunsaturated fatty acid biosynthesis: insights into the evolution, function with substrate specificities and biotechnological use.Applied microbiology and biotechnology · 2020Review
- Plastidic Δ6 Fatty-Acid Desaturases with Distinctive Substrate Specificity Regulate the Pool of C18-PUFAs in the Ancestral PicoalgaPlant physiology · 2020Article
- A conserved evolutionary mechanism permits Δ9 desaturation of very-long-chain fatty acyl lipids.The Journal of biological chemistry · 2020Article
- Two clusters of residues contribute to the activity and substrate specificity of Fm1, a bifunctional oleate and linoleate desaturase of fungal origin.The Journal of biological chemistry · 2018Article
- Structural determinant of functionality in acyl lipid desaturases.Journal of lipid research · 2018Article
- Genomic Enzymology: Web Tools for Leveraging Protein Family Sequence-Function Space and Genome Context to Discover Novel Functions.Biochemistry · 2017Review
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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
Membrane fatty acid desaturases are a diverse superfamily of enzymes that catalyze the introduction of double bonds into fatty acids. They are essential in a range of metabolic processes, such as the production of omega-3 fatty acids. However, our structure-function understanding of this superfamily is still developing and their range of activities and substrate specificities are broad, and often overlapping, which has made their systematic characterization challenging. A central issue with characterizing these proteins has been the lack of a structural model, which has been overcome with the recent publication of the crystal structures of two mammalian fatty acid desaturases. In this work, we have used sequence similarity networks to investigate the similarity among over 5000 related membrane fatty acid desaturase sequences, leading to a detailed classification of the superfamily, families and subfamilies with regard to their function and substrate head-group specificity. This work will facilitate rapid prediction of the function and specificity of new and existing sequences, as well as forming a basis for future efforts to manipulate the substrate specificity of these proteins for biotechnology applications.
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