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Studies on the Mechanism of Fatty Acid Synthesis

XIX. PREPARATION AND GENERAL PROPERTIES OF PALMITYL THIOESTERASE

From the ¹ From the Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27706

Palmityl thioesterase of Escherichia coli has been purified 260-fold. Its molecular weight is estimated at 22,000 by sedimentation velocity. The enzyme catalyzes the hydrolysis of long chain fatty acyl thioesters of acyl carrier protein or coenzyme A to form free fatty acid and the respective thiol. The enzyme is readily inhibited by diisopropyl fluorophosphate. Palmityl thioesterase was found to exhibit specificity for fatty acyl thioesters of chain length greater than C₁₀ and palmityl, palmitoleyl, and cis-vaccenyl thioesters are the preferred substrates. The enzyme was shown to be capable of mediating the synthesis of free fatty acids by preparations of the E. coli fatty acid-synthesizing system.

Palmityl thioesterase activity is also present in highly purified preparations of pigeon liver fatty acid synthetase. The pigeon liver thioesterase was shown to be specific for fatty acyl-coenzyme A thioesters of C₁₆ and C₁₈ chain length.

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