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

Department of Biology, College of Life Science and Biotechnology, Yonsei University, Seoul, Republic of Korea.

FEBS letters 2009 Jul 7

filter terms:

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.

Citation

Young Sam Seo, Eun Yu Kim, Jeong Hoe Kim, Woo Taek Kim. Enzymatic characterization of class I DAD1-like acylhydrolase members targeted to chloroplast in Arabidopsis. FEBS letters. 2009 Jul 7;583(13):2301-7