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Studies on the Mechanism of Fatty Acid Synthesis

XVI. PREPARATION AND GENERAL PROPERTIES OF ACYL-MALONYL ACYL CARRIER PROTEIN-CONDENSING ENZYME FROM ESCHERICHIA COLI

Richard E. Toomey 1 and Salih J. Wakil 1

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

Acyl-malonyl acyl carrier protein (ACP)-condensing enzyme, prepared from extracts of Escherichia coli, catalyzes the condensation of acetyl-ACP and malonyl-ACP to form acetoacetyl-ACP. It also catalyzes the condensation of various longer chain saturated acyl-ACP derivatives with malonyl-ACP to form the ß-ketoacyl-ACP of the longer homologues. The enzyme is specific for the acyl-ACP derivatives and does not act on acyl coenzyme A derivatives (acetyl-CoA or malonyl-CoA).

The enzyme has a functional —SH group and can be readily inhibited by —SH-binding reagents such as N-ethylmaleimide and iodoacetamide. Acetyl-ACP protects the enzyme against thiol-binding reagents, which indicates that an acetyl—S—enzyme complex may be an intermediate in the condensation of acyl-ACP and malonyl-ACP to form ß-ketoacyl-ACP.

Submitted on September 1, 1965


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