論文

査読有り 国際誌
2019年11月1日

Glycosylinositol phosphoceramide-specific phospholipase D activity catalyzes transphosphatidylation.

Journal of biochemistry
  • Rumana Yesmin Hasi
  • Makoto Miyagi
  • Katsuya Morito
  • Toshiki Ishikawa
  • Maki Kawai-Yamada
  • Hiroyuki Imai
  • Tatsuya Fukuta
  • Kentaro Kogure
  • Kaori Kanemaru
  • Junji Hayashi
  • Ryushi Kawakami
  • Tamotsu Tanaka
  • 全て表示

166
5
開始ページ
441
終了ページ
448
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1093/jb/mvz056

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.

リンク情報
DOI
https://doi.org/10.1093/jb/mvz056
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/31504617
ID情報
  • DOI : 10.1093/jb/mvz056
  • PubMed ID : 31504617

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