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Positional Specificity and Fatty Acid Selectivity of Purified sn-Glycerol 3-Phosphate Acyltransferases from Chloroplasts ¹

Botanisches Institut der Universität zu Köln, Gyrhofstr. 15, 5000 Köln 41, Federal Republic of Germany

Soluble acyl-CoA:sn-glycerol 3-phosphate acyltransferases (EC 2.3.1.15) which are localized in chloroplasts were purified from leaves of Pisum sativum and Spinacia oleracea and obtained free from interfering activities. The purification raised the specific activities by factors of about 1,000 for pea and 200 for spinach preparations. In pea chloroplasts, acyltransferase activity occurs in two soluble forms with apparent isoelectric points of 6.3 and 6.6. For both forms, the same molecular weight of about 42,000 was determined. The enzyme from spinach chloroplasts showed a slightly higher molecular weight and a lower isoelectric point of 5.2.

The enriched enzyme fractions possessed a specificity for glycerol 3-phosphate as acyl acceptor and did not use dihydroxyacetone phosphate. Besides acyl-CoA, acyl-acyl carrier protein also can function as acyl donor. With acyl-CoA as acyl donor, the enzyme shows a high positional specificity, since the predominant product is 1-acylglycerol 3-phosphate.

Different acyl-CoAs, when offered separately, were all accepted as substrates, whereas incubations with mixtures of palmitoyl-, stearoyl-, and oleoyl-CoA demonstrated a preference for oleic acid. The acyltransferase from spinach displays higher selectivity than does the enzyme from pea and, therefore, may be responsible for the preferred esterification of oleic acid at the C—1 position in chloroplast lipids and the exclusion of palmitic acid from this position as observed during in vivo labeling experiments.

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