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Plant and Cell Physiology, 1992, Vol. 33, No. 2 189-195
© 1992

Article

Diacylglycerol Acyltransferase in Microsomes and Oil Bodies of Oil Palm Mesocarp

ZhangKhaik-Cheang Oo and Yoke-Ha Chew

Department of Biochemistry, University of Malaya Kuala Lumpur, Malaysia

Specific acyltransferase activities were detected in microsomes and oil bodies from palm mesocarp in the presence of exogenous lysophosphatidic acid, diacylglycerol and glycerol-3-phosphate. These activities were 2–3 times higher per mg protein in oil bodies than in microsomes. Diacylglycerol acyltransferase in both preparations required Mg2+, dithiothreitol, gelatine and fat free bovine serum albumin for maximum activity at pH 8.5. The enzyme had an apparent Km of 0.18 mM for dipalmitin. In both preparations, the enzyme was active with myristoyl-CoA, palmitoyl-CoA, stearoyl-CoA and oleoyl-CoA. When presented with a mixture of two acyl- CoAs, microsomal enzyme showed no selectivity but oil body enzyme had a preference for oleoyl-CoA over palmitoyl-CoA.

(Received October 11, 1991; Accepted December 27, 1991)
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