Abstract
Cell-free homogenates of spinach leaves incorporated glycerophosphate-32P into phosphatides when supplied with adenosine triphosphate, Mg++and coenzyme A (CoA). Most of the activity of the homogenate was associated with the microsome fraction sedimented at 104,000 × g, but some activity was also present in the chloroplast fraction. In all systems, most of the32P incorporated appeared in phosphatide acid (+ lysophosphatidic acid), with small to trace amounts in phosphatidyl glycerol and phosphatidyl inositol. Coenzyme A and adenosine triphosphate + Mg++were obligatory cofactors for the incorporation of α-glycerophosphate-32P but acetate + bicarbonate, cytidine triphosphate, or light were not essential. The results demonstrate the presence of acyl-CoA:L-glycerol-3-phosphate O-acyltransferase in the microsome fraction of spinach leaves and also indicate the existence of enzyme systems catalyzing the conversion of phosphatidic acid to phosphatidyl inositol and phosphatidyl glycerol.