Glycosylinositol phosphoceramide-specific phospholipase D activity catalyzes transphosphatidylation
Bibliographic Information
- Other Title
-
- Transphosphatidylation by GIPC-PLD
Search this article
Abstract
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.
Journal
-
- The Journal of Biochemistry
-
The Journal of Biochemistry 166 (5), 441-448, 2019-08-26
Oxford University Press
- Tweet
Details 詳細情報について
-
- CRID
- 1050285299951137024
-
- NII Article ID
- 120006879927
-
- NII Book ID
- AA12096002
-
- ISSN
- 17562651
- 0021924X
-
- NDL BIB ID
- 030083624
-
- Text Lang
- en
-
- Article Type
- journal article
-
- Data Source
-
- IRDB
- NDL
- Crossref
- CiNii Articles
- KAKEN