Enzymatic characterization of class I DAD1-like acylhydrolase members targeted to chloroplast in Arabidopsis.
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.
Seo
Young Sam
YS
Department of Biology, College of Life Science and Biotechnology, Yonsei University, Seoul, Republic of Korea.
Kim
Eun Yu
EY
Kim
Jeong Hoe
JH
Kim
Woo Taek
WT
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
D029681:Arabidopsis Proteins; D006867:Hydrolases; C445094:DAD1 protein, Arabidopsis; D054466:Phospholipases A1