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Enzymatic characterization of class I DAD1‐like acylhydrolase members targeted to chloroplast in Arabidopsis
Author(s) -
Seo Young Sam,
Kim Eun Yu,
Kim Jeong Hoe,
Kim Woo Taek
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.06.021
Subject(s) - arabidopsis , chloroplast , enzyme , chemistry , class (philosophy) , biochemistry , gene , computer science , mutant , artificial intelligence
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.