Literature DB >> 27198176

Enzymatic characterization of recombinant rat DDHD2: a soluble diacylglycerol lipase.

Mari Araki1,2, Noriyasu Ohshima3, Chizu Aso4, Akimitsu Konishi1, Hideru Obinata1, Kazuaki Tatei1, Takashi Izumi1.   

Abstract

DDHD2 has been reported to exhibit phospholipase A1, triacylglycerol (TG) lipase and diacylglycerol (DG) lipase activities. However, the detailed enzymatic properties of DDHD2 have not yet been elucidated. In the current study, the substrate specificity of DDHD2 towards DG, TG and phosphatidic acid (PA) has been examined using highly purified recombinant rat DDHD2 (rDDHD2) with a liquid chromatography mass spectrometer. The k cat/Km value for DG (18:0/20:4) was much higher than those for TG (18:1/18:1/18:1), and PA (18:0/20:4) in the presence of sodium deoxycholate. The enzyme activity of rDDHD2 towards DG (18:0/20:4) was highest among all of the substrates tested. In addition, rDDHD2 was highly specific to DG substrates with a polyunsaturated fatty acid at their sn-2 position. The levels of 2-arachidonoylglycerol (2-AG) in CHO cells were quantified by gas chromatography-tandem mass spectrometry, showing that CHO cells expressing recombinant rDDHD2 contained higher levels of 2-AG when cells were treated with a monoacylglycerol lipase inhibitor, URB602. These results therefore support the idea that DDHD2 functions as a DG lipase in vivo and produces 2-AG.
© The Authors 2016. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Entities:  

Keywords:  2-arachidonoylglycerol; DDHD2; diacylglycerol; lipase; phospholipase

Mesh：

Substances：

Year:  2016        PMID： 27198176     DOI： 10.1093/jb/mvw034

Source DB:  PubMed          Journal:  J Biochem        ISSN： 0021-924X            Impact factor:   3.387


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