ArticleJournal of lipid research2015
Molecular mechanism of substrate specificity for delta 6 desaturase from Mortierella alpina and Micromonas pusilla.
Article in Journal of lipid research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 41 citations in OpenAlex.
- Chronic hypoxia and hyperoxia alter tissue-specific fatty acid profile and FD6D and elongase gene expression levels in rainbow trout (Oncorhynchus mykiss).Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2023Article
- Evolution of Linoleic Acid Biosynthesis Paved the Way for Ecological Success of Termites.Molecular biology and evolution · 2023Article
- Investigating the role of FADS family members in breast cancer based on bioinformatic analysis and experimental validation.Frontiers in immunology · 2023Article
- Molecular mechanism of interaction between fatty acid delta 6 desaturase and acyl-CoA by computational prediction.AMB Express · 2022Article
- Key Enzymes in Fatty Acid Synthesis Pathway for Bioactive Lipids Biosynthesis.Frontiers in nutrition · 2022Review
- Advances in improving the biotechnological application of oleaginous fungus Mortierella alpina.Applied microbiology and biotechnology · 2021Review
- 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
- 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
- Δ12 fatty acid desaturase gene fromFEBS open bio · 2019Article
- Production of eicosapentaenoic acid by application of a delta-6 desaturase with the highest ALA catalytic activity in algae.Microbial cell factories · 2018Article
- Molecular mechanisms underlying catalytic activity of delta 6 desaturase fromJournal of lipid research · 2018Article
- Regiospecific Analysis of Fatty Acids and Calculation of Triglyceride Molecular Species in Marine Fish Oils.BioMed research international · 2018Article
- Characterization of Positional Distribution of Fatty Acids and Triacylglycerol Molecular Compositions of Marine Fish Oils Rich in Omega-3 Polyunsaturated Fatty Acids.BioMed research international · 2018Article
- Characterization of an Omega-3 Desaturase FromFrontiers in microbiology · 2018Article
- Substrate specificity and membrane topologies of the iron-containing ω3 and ω6 desaturases from Mortierella alpina.Applied microbiology and biotechnology · 2018Article
- Application of a delta-6 desaturase with α-linolenic acid preference on eicosapentaenoic acid production in Mortierella alpina.Microbial cell factories · 2016Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The ω6 and ω3 pathways are two major pathways in the biosynthesis of PUFAs. In both of these, delta 6 desaturase (FADS6) is a key bifunctional enzyme desaturating linoleic acid or α-linolenic acid. Microbial species have different propensity for accumulating ω6- or ω3-series PUFAs, which may be determined by the substrate preference of FADS6 enzyme. In the present study, we analyzed the molecular mechanism of FADS6 substrate specificity. FADS6 cDNAs were cloned from Mortierella alpina (ATCC 32222) and Micromonas pusilla (CCMP1545) that synthesized high levels of arachidonic acid and EPA, respectively. M. alpina FADS6 (MaFADS6-I) showed substrate preference for LA; whereas, M. pusilla FADS6 (MpFADS6) preferred ALA. To understand the structural basis of substrate specificity, MaFADS6-I and MpFADS6 sequences were divided into five sections and a domain swapping approach was used to examine the role of each section in substrate preference. Our results showed that sequences between the histidine boxes I and II played a pivotal role in substrate preference. Based on our domain swapping results, nine amino acid (aa) residues were targeted for further analysis by site-directed mutagenesis. G194L, E222S, M227K, and V399I/I400E substitutions interfered with substrate recognition, which suggests that the corresponding aa residues play an important role in this process.
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