| Title : Enzymatic characterization of class I DAD1-like acylhydrolase members targeted to chloroplast in Arabidopsis - Seo_2009_FEBS.Lett_583_2301 |
| Author(s) : Seo YS , Kim EY , Kim JH , Kim WT |
| Ref : FEBS Letters , 583 :2301 , 2009 |
|
Abstract :
In Arabidopsis, there are at least seven class I acylhydrolase members, which have a putative N-terminal chloroplast-targeting signal. Here, we show that all seven class I proteins are localized to the chloroplasts and hydrolyze phosphatidylcholine at the sn-1 position. However, based on their activities toward various lipids, Arabidopsis class I enzymes could be further divided into three sub-groups by substrate specificity, one with phospholipase-specific activity, another with phospholipase and galactolipase activities, and the other with broad lipolytic activity toward phosphatidylcholine, galactolipids, and triacylglycerol. These results suggest that the three sub-groups of class I acylhydrolases have specific roles in chloroplasts. |
| PubMedSearch : Seo_2009_FEBS.Lett_583_2301 |
| PubMedID: 19527719 |
| Gene_locus related to this paper: arath-AT4G16820 , arath-PLA11 , arath-PLA12 , arath-PLA13 , arath-PLA15 , arath-PLA16 , arath-PLA17 |
| Substrate | Dioleoyllecithin |
| Gene_locus | arath-AT4G16820 arath-PLA11 arath-PLA12 arath-PLA13 arath-PLA15 arath-PLA16 arath-PLA17 |
Seo YS, Kim EY, Kim JH, Kim WT (2009)
Enzymatic characterization of class I DAD1-like acylhydrolase members targeted to chloroplast in Arabidopsis
FEBS Letters
583 :2301
Seo YS, Kim EY, Kim JH, Kim WT (2009)
FEBS Letters
583 :2301