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ID 113685
Title Alternative
Transphosphatidylation by GIPC-PLD
Author
Hasi, Rumana Yesmin Tokushima University
Miyagi, Makoto Tokushima University
Morito, Katsuya Tokushima University
Ishikawa, Toshiki Saitama University
Kawai-Yamada, Maki Saitama University
Imai, Hiroyuki Konan University
Keywords
Sphingolipid
Phytoceramide 1-phosphate
Glycosylinositol phosphoceramide
Phospholipase D
Content Type
Journal Article
Description
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 Title
The Journal of Biochemistry
ISSN
17562651
0021924X
NCID
AA12096002
AA00694073
Publisher
Oxford University Press
Volume
166
Issue
5
Start Page
441
End Page
448
Published Date
2019-08-26
Remark
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.
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DOI (Published Version)
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language
eng
TextVersion
Author
departments
Pharmaceutical Sciences
Bioscience and Bioindustry