4.5 Article

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

期刊

FEBS LETTERS
卷 583, 期 13, 页码 2301-2307

出版社

WILEY
DOI: 10.1016/j.febslet.2009.06.021

关键词

DEFECTIVE IN ANTHER DEHISCENCE1-like acylhydrolase; Phospholipase; Galactolipase; Chloroplast targeting; Alternative RNA splicing

资金

  1. Ministry of Education, Science, and Technology
  2. Korea Science and Engineering Foundation [R01-2008-00020648-0]
  3. Technology Development Program for Agriculture and Forestry [309017-5]
  4. Ministry for Agriculture, Forestry and Fisheries, Republic of Korea
  5. Brain Korea [BK21]

向作者/读者索取更多资源

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. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

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