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Literature summary for 1.14.19.36 extracted from

  • Roman, A.; Hernandez, M.L.; Soria-Garcia, A.; Lopez-Gomollon, S.; Lagunas, B.; Picorel, R.; Martinez-Rivas, J.M.; Alfonso, M.
    Non-redundant contribution of the plastidial FAD8 omega-3 desaturase to glycerolipid unsaturation at different temperatures in Arabidopsis (2015), Mol. Plant, 8, 1599-1611 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene FAD8, generation of FAD8-YFP overexpressing lines, that show a specific increase in 18:3 fatty acids at 22°C Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
additional information construction of a insertional mutant fad8i (SALK_093590) inactivation mutant of FAD8, analysis of the fatty acid composition of the fad8i mutant shows compensatory responses at the trienoic fatty acid level as a result of inactivation of the FAD8 gene. Genomic analysis of fad8i plants show insertion of an inverted tandem T-DNA 133 bp downstream of the start codon, within exon 1 of the AtFAD8 gene, absence of AtFAD8 transcript in the mutant. Contruction of a fad7/fad8 double knockout mutant. Given the strong reduction (70%) in 18:3 content observed in the fad7/fad8 double mutant, in mutant fad7i after disruption of the AtFAD7 gene, FAD8 enzymatic activity is able to maintain, at least partially (43.7%), the amount of 18:3 and to a much lesser extent that of 16:3 (23.2%) at 22°C. Mutant genotypes and phenotypes, overview. Temperature-dependent expression levels. Disruption of the AtFAD8 gene in the insertion mutant does not result in significant changes in the transcript levels of FAD8. Overexpression of FAD8 increased 18:3 levels in phospholipids but not in galactolipids Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast envelope
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Arabidopsis thaliana 9941
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membrane enzymes FAD8 and FAD7 might be located in close vicinity in the envelope membrane Arabidopsis thaliana 16020
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Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana P48622
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Arabidopsis thaliana Col-0 P48622
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Source Tissue

Source Tissue Comment Organism Textmining
leaf
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Arabidopsis thaliana
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme FAD8 acts preferentially on fatty acids esterified to the sn-1 position of glycerolipids. This might explain why FAD8 acts poorly on 16:2 substrates (always in the sn-2 position) or the higher selectivity for phosphatidylglycerol (which contains 18:2 only in sn-1) Arabidopsis thaliana ?
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?
additional information enzyme FAD8 acts preferentially on fatty acids esterified to the sn-1 position of glycerolipids. This might explain why FAD8 acts poorly on 16:2 substrates (always in the sn-2 position) or the higher selectivity for phosphatidylglycerol (which contains 18:2 only in sn-1) Arabidopsis thaliana Col-0 ?
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?

Synonyms

Synonyms Comment Organism
FAD8
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Arabidopsis thaliana
More cf. EC 1.14.19.35 Arabidopsis thaliana
plastidial FAD8 omega-3 desaturase
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Arabidopsis thaliana
plastidial omega-3 desaturase
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Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
Ferredoxin
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Arabidopsis thaliana

General Information

General Information Comment Organism
malfunction leaf lipid analysis of the Arabidopsis omega-3 desaturase fad7 mutant line at growth temperature of 22°C, overview. Disruption of the AtFAD8 gene in fad8i results in trienoic fatty acid levels almost similar to those from wild-type Col-0. The fad7/fad8 double mutant also shows a considerable reduction in trienoic fatty acid, particularly in 16:3, which is undetectable Arabidopsis thaliana
physiological function fatty acid and lipid analysis of several omega-3 desaturase mutants, including two insertion lines of two plastidial omega-3 desaturases AtFAD7 and AtFAD8, shows that FAD8 partially compensates the disruption of the AtFAD7 gene at 22°C, indicating that FAD8 is active at this growth temperature, contrasting to previous observations that circumscribe the FAD8 activity at low temperature. FAD8 has a higher selectivity for 18:2 acyl-lipid substrates and a higher preference for lipids other than galactolipids, particularly phosphatidylglycerol, at any of the temperatures studied. Differences in the mechanism controlling AtFAD7 and AtFAD8 gene expression at different temperatures. The function of both plastidial omega-3 desaturases is coordinated in a non-redundant manner Arabidopsis thaliana