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Characterization of Phosphatidylcholine-Hydrolyzing Phospholipase D in the Scuticociliate Parasite, Uronema marinum  

Seo, Jung-Soo (Patholgy Division, National Fisheries Research and Development Institute)
Kim, Moo-Sang (Department of Aquatic Life Medicine, Pukyong National University)
Kim, Na-Young (Department of Aquatic Life Medicine, Pukyong National University)
Ahn, Sang-Jung (Faculty of Food Science and Biotechnology, Pukyong National University)
Jee, Bo-Young (Patholgy Division, National Fisheries Research and Development Institute)
Jung, Sung-Hee (Patholgy Division, National Fisheries Research and Development Institute)
Kim, Jin-Woo (Patholgy Division, National Fisheries Research and Development Institute)
Kim, Ki-Hong (Department of Aquatic Life Medicine, Pukyong National University)
Lee, Hyung-Ho (Faculty of Food Science and Biotechnology, Pukyong National University)
Chung, Joon-Ki (Department of Aquatic Life Medicine, Pukyong National University)
Publication Information
Journal of fish pathology / v.21, no.1, 2008 , pp. 1-11 More about this Journal
Abstract
We report the existence of new type of phosphatidylcholine-hydrolyzing phospholipase D (PLD), which has been characterized and partially purified in the scuticociliate, Uronema marinum. The enzyme from partial purification showed that it was existed in membrane fraction and was a neutral PLD, which catalyzed both transphosphatidylation and hydrolysis reaction. The activity of partially purified membrane-bound PLD was also found to be optimal at pH 7.0-7.5 for 2 hours at 37℃ and depended strictly on the presence of Ca2+ (2.5 mM) and Mg2+ (1.6 mM). Immunoblot analysis indicated that the enzyme was distinct from hPLD1 (human PLD1) and hPLD2 (human PLD2) because it was not recognized by a polyclonal antibody raised to the 12 terminal amino acid of these enzymes. We also found that the membrane-bound PLD is a PIP2-dependent PLD and that GTP-binding proteins are not implicated in the regulation of this enzyme: This enzyme activity is markedly stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) but not by the small G-protein Arf and GTPrS. In addition, this enzyme was capable of hydrolyzing phosphatidylcholine (PC) but not phosphatidylethanolamine (PE), implying that PC was a preferred substrate.
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