Nonspecific phospholipase C3 of radish has phospholipase D activity towards glycosylinositol phosphoceramide

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  • Nonspecific phospholipase C3 of radish has phospholipase D activity toward glycosylinositol phosphoceramide

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Previously, we found an enzyme activity that produces phytoceramide 1-phosphate (PC1P) by hydrolysis of D position of glycosylinositol phosphoceramide (GIPC) in cabbage and called its activity as GIPC-phospholipase D (PLD). Here, we purified GIPC-PLD by sequential chromatography from radish roots. Peptide mass fingerprinting analysis revealed that the potential candidate for GIPC-PLD protein was nonspecific phospholipase C3 (NPC3), which has not been characterized as PLD. The recombinant NPC3 protein obtained by heterologous expression system with E. coli produced PC1P from GIPC, and showed essentially the same enzymatic properties as those we characterized as GIPC-PLD in cabbage, radish, and A. thaliana. From these results, we concluded that NPC3 is one of the enzymes that degrade GIPC, a major sphingolipid in plants.

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  • FEBS Letters

    FEBS Letters 596 (23), 3024-3036, 2022-10-20

    Federation of European Biochemical Societies|Wiley

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