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JBC, Vol. 250, Issue 21, 8530-8535, Nov, 1975

sn-Glycerol-3-phosphate acyltransferase activity in particulate preparations from anaerobic, light-grown cells of Rhodopseudomonas spheroides. Involvement of acyl thiolester derivatives of acyl carrier protein in the synthesis of complex lipids

D. R. Lueking and H. Goldfine

Crude particulate preparations obtained from anaerobic, light-grown cells of Rhodopseudomonas spheroides have been shown to possess a significant level of sn-glycerol-3-phosphate acyltransferase (EC 2.3.1.15) activity. In contrast to the enzyme from Escherichia coli, the R. spheroides glycerophosphate acyltransferase has a high specificity for acyl thiolester derivatives of acyl carrier protein (ACP) as acyl donors for the reaction. Only limited , nonlinear glycerophosphate incorporation into lipid occurs when acyl coenzyme A (CoA) derivatives are employed as acyl substrate. With oleyl-ACP as substrate, maximal enzyme activity was observed at 40 degrees, over a broad pH range (6.0 to 8.5) and did not require a divalent metal cation. The presence of dithiothreitol stimulated enzyme-activity 15 to 20%. When oleyl-ACP or palmityl-ACP was employed as sole acyl group donor, the major products recoverable from the reaction mixtures were lysophosphatidic acid, phosphatidic acid, and monoglyceride. Althouh oleyl-ACP and palmityl-ACP gave comparable maximal velocities in the initial acylation of glycerophosphate, the formation of phosphatidic acid occurred preferentially with the unsaturated acyl-ACP derivative.
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