Enzymatic characterization of class I DAD1-like acylhydrolase members targeted to chloroplast in Arabidopsis

Young Sam Seo, Eun Yu Kim, Jeong Hoe Kim, Woo Taek Kim

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35 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)2301-2307
Number of pages7
JournalFEBS Letters
Issue number13
Publication statusPublished - 2009 Jul 7


All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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