The enzyme, characterized from the marine diatom Thalassiosira pseudonana, produces an all-trans product. Similar triunsaturated sphingoid bases are found in some marine invertebrates. The enzyme determines the position of the double bond by its distance from the alcohol end of the sphingoid base, and contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase.
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SYSTEMATIC NAME
IUBMB Comments
a (4E,8E)-sphinga-4,8-dienine ceramide,ferrocytochrome b5:oxygen oxidoreductase (10,11 trans-dehydrogenating)
The enzyme, characterized from the marine diatom Thalassiosira pseudonana, produces an all-trans product. Similar triunsaturated sphingoid bases are found in some marine invertebrates. The enzyme determines the position of the double bond by its distance from the alcohol end of the sphingoid base, and contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase.
LC-MS screenings of sphingolipid-enriched fractions and in vitro enzymatic synthesis of fusaruside by recombinant DELTA 10(E)-SD. The enzyme shows no reactivity towards 2-methylbutene-bearing molecules including citral, isochromophilone VI, nerolidol, phytolorvitamin D1 and cerebroside B derived ceramide. The presence of the C9-methyl group is essential for the sphingolipid DELTA 10-desaturase activity, mutational analysis
LC-MS screenings of sphingolipid-enriched fractions and in vitro enzymatic synthesis of fusaruside by recombinant DELTA 10(E)-SD. The enzyme shows no reactivity towards 2-methylbutene-bearing molecules including citral, isochromophilone VI, nerolidol, phytolorvitamin D1 and cerebroside B derived ceramide. The presence of the C9-methyl group is essential for the sphingolipid DELTA 10-desaturase activity, mutational analysis
the enzyme catalyzes the regiospecific biosynthesis of fusaruside, a 10,11-unsaturated immunosuppressive fungal sphingolipid through desaturation of cerebroside B, an abundant fungal sphingolipid. The conserved histidines of DELTA 10(E)-SD are essential for the 10,11-desaturation catalysis, which is also preconditioned by the C9-methylation of the substrate. Enzyme DELTA 10(E)-SD improves survival of fungal strains in chill and salinity
the enzyme catalyzes the regiospecific biosynthesis of fusaruside, a 10,11-unsaturated immunosuppressive fungal sphingolipid through desaturation of cerebroside B, an abundant fungal sphingolipid. The conserved histidines of DELTA 10(E)-SD are essential for the 10,11-desaturation catalysis, which is also preconditioned by the C9-methylation of the substrate. Enzyme DELTA 10(E)-SD improves survival of fungal strains in chill and salinity
the enzyme can be useful for production of fusaruside, a 10,11-unsaturated immunosuppressive fungal sphingolipid with medical potentials for treating liver injury and colitis
the enzyme can be useful for production of fusaruside, a 10,11-unsaturated immunosuppressive fungal sphingolipid with medical potentials for treating liver injury and colitis
the enzyme can be useful for production of fusaruside, a 10,11-unsaturated immunosuppressive fungal sphingolipid with medical potentials for treating liver injury and colitis, DELTA 10(E)-sphingolipid desaturase as a new regiospecific biocatalyst
the enzyme can be useful for production of fusaruside, a 10,11-unsaturated immunosuppressive fungal sphingolipid with medical potentials for treating liver injury and colitis, DELTA 10(E)-sphingolipid desaturase as a new regiospecific biocatalyst
Michaelson, L.; Markham, J.; Zeuner, S.; Matsumoto, M.; Chen, M.; Cahoon, E.; Napier, J.
Identification of a cytochrome b5-fusion desaturase responsible for the synthesis of triunsaturated sphingolipid long chain bases in the marine diatom Thalassiosira pseudonana