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Originally published In Press as doi:10.1074/jbc.M100005200 on January 18, 2001

J. Biol. Chem., Vol. 276, Issue 14, 10847-10852, April 6, 2001
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Identification, Purification, and Characterization of Monoacylglycerol Acyltransferase from Developing Peanut Cotyledons*

Ajay W. Tumaney, Sunil Shekar, and Ram RajasekharanDagger

From the Department of Biochemistry, Indian Institute of Science, Bangalore 560 012, India

Biosynthesis of diacylglycerols in plants occurs mainly through the acylation of lysophosphatidic acid in the microsomal membranes. Here we describe the first identification of diacylglycerol biosynthetic activity in the soluble fraction of developing oilseeds. This activity was NaF-insensitive and acyl-CoA-dependent. Diacylglycerol formation was catalyzed by monoacylglycerol (MAG) acyltransferase (EC 2.3.1.22) that transferred an acyl moiety from acyl-CoA to MAG. The enzyme was purified by successive chromatographic separations on octyl-Sepharose, blue-Sepharose, Superdex-75, and palmitoyl-CoA-agarose to apparent homogeneity from developing peanut (Arachis hypogaea) cotyledons. The enzyme was purified to 6,608-fold with the final specific activity of 15.86 nmol min-1 mg-1. The purified enzyme was electrophoretically homogeneous, and its molecular mass was 43,000 daltons. The purified MAG acyltransferase was specific for MAG and did not utilize any other acyl acceptor such as glycerol, glycerol-3-phosphate, lysophosphatidic acid, and lysophosphatidylcholine. The Km values for 1-palmitoylglycerol and 1-oleoylglycerol were 16.39 and 5.65 µM, respectively. The Km values for 2-monoacylglycerols were 2- to 4-fold higher than that of the corresponding 1-monoacylglycerol. The apparent Km values for palmitoyl-, stearoyl-, and oleoyl-CoAs were 17.54, 25.66, and 9.35 µM, respectively. Fatty acids, phospholipids, and sphingosine at low concentrations stimulated the enzyme activity. The identification of MAG acyltransferase in oilseeds suggests the presence of a regulatory link between signal transduction and synthesis of complex lipids in plants.

* This research was supported by the Dept. of Science and Technology, and the Dept. of Biotechnology, New Delhi, India.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Tel.: 91-80-3092881; Fax: 91-80-3602627; E-mail: lipid@biochem.iisc.ernet.in.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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