Nonspecific phospholipase <scp>C3</scp> of radish has phospholipase D activity towards glycosylinositol phosphoceramide
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- Rumana Yesmin Hasi
- Graduate School of Technology, Industrial and Social Sciences Tokushima University Japan
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- Toshiki Ishikawa
- Graduate School of Science and Engineering Saitama University Japan
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- Keigo Sunagawa
- Graduate School of Technology, Industrial and Social Sciences Tokushima University Japan
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- Yoshimichi Takai
- Graduate School of Technology, Industrial and Social Sciences Tokushima University Japan
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- Hanif Ali
- Graduate School of Technology, Industrial and Social Sciences Tokushima University Japan
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- Junji Hayashi
- Graduate School of Technology, Industrial and Social Sciences Tokushima University Japan
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- Ryushi Kawakami
- Graduate School of Technology, Industrial and Social Sciences Tokushima University Japan
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- Keizo Yuasa
- Graduate School of Science and Engineering Setsunan University Neyagawa Japan
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- Mutsumi Aihara
- Graduate School of Technology, Industrial and Social Sciences Tokushima University Japan
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- Kaori Kanemaru
- Graduate School of Technology, Industrial and Social Sciences Tokushima University Japan
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- Hiroyuki Imai
- Graduate School of Natural Science Konan University Kobe Japan
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- Tamotsu Tanaka
- Graduate School of Technology, Industrial and Social Sciences Tokushima University Japan
抄録
<jats:p>Glycosylinositol phosphoceramide (GIPC) is a major sphingolipid in the plasma membranes of plants. Previously, we found an enzyme activity that produces phytoceramide 1‐phosphate (PC1P) by hydrolysis of the D position of GIPC in cabbage and named this 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 a PLD. The recombinant NPC3 protein obtained by heterologous expression system in <jats:italic>Escherichia coli</jats:italic> produced PC1P from GIPC and showed essentially the same enzymatic properties as those we characterized as GIPC‐PLD in cabbage, radish and <jats:italic>Arabidopsis thaliana.</jats:italic> From these results, we conclude that NPC3 is one of the enzymes that degrade GIPC.</jats:p>
収録刊行物
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- FEBS Letters
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FEBS Letters 596 (23), 3024-3036, 2022-10-31
Wiley
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詳細情報 詳細情報について
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- CRID
- 1360580232375843968
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- ISSN
- 18733468
- 00145793
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- データソース種別
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- Crossref
- KAKEN