Glycosylinositol phosphoceramide-specific phospholipase D activity catalyzes transphosphatidylation

Glycosylinositol phosphoceramide (GIPC) is the most abundant sphingolipid in plants and fungi. Recently, we detected GIPC-specific phospholipase D (GIPC-PLD) activity in plants. Here, we found that GIPC-PLD activity in young cabbage leaves catalyzes transphosphatidylation. The available alcohol for this reaction is a primary alcohol with a chain length below C4. Neither secondary alcohol, tertiary alcohol, choline, serine nor glycerol serves as an acceptor for transphosphatidylation of GIPC-PLD. We also found that cabbage GIPC-PLD prefers GIPC containing two sugars. Neither inositol phosphoceramide, mannosylinositol phosphoceramide nor GIPC with three sugar chains served as substrate. GIPC-PLD will become a useful catalyst for modification of polar head group of sphingophospholipid.

This is a pre-copyedited, author-produced version of an article accepted for publication in The Journal of Biochemistry following peer review. The version of record The Journal of Biochemistry, (2019) Vol.166 Issue.5 p.441-448 is available online at: https://doi.org/10.1093/jb/mvz056.