title: Enzymatic characterization of class I DAD1-like acylhydrolase members targeted to chloroplast in Arabidopsis.
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.
authors.affiliation: Department of Biology, College of Life Science and Biotechnology, Yonsei University, Seoul, Republic of Korea.
authors.forename: Young Sam
authors.initials: YS
authors.lastname: Seo
authors.forename: Eun Yu
authors.initials: EY
authors.lastname: Kim
authors.forename: Jeong Hoe
authors.initials: JH
authors.lastname: Kim
authors.forename: Woo Taek
authors.initials: WT
authors.lastname: Kim
mesh_terms: D017360:Arabidopsis / Q000201:enzymology* / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000378:metabolism; D002736:Chloroplasts / Q000201:enzymology* / Q000378:metabolism; D006867:Hydrolases / Q000737:chemistry* / Q000378:metabolism; D054466:Phospholipases A1 / Q000737:chemistry* / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D029681:Arabidopsis Proteins; D006867:Hydrolases; C445094:DAD1 protein, Arabidopsis; D054466:Phospholipases A1