Fatty acid synthetase from Brevibacterium ammoniagenes: formation of monounsaturated fatty acids by a multienzyme complex.

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Abstract
A multienzyme fatty acid synthetase complex isolated from B. ammoniagenes was purified to a specific activity of 1440 nmol of malonyl-CoA incorporated/min per mg. The enzyme is homogeneous, as judged by gel electrophoresis on agarose gels, and has a MW of 1.2 .times. 106. NADPH and NADH are required for activity. Unlike other fatty acid synthetase complexes, the enzyme catalyzes the synthesis of long-chain saturated and monounsaturated fatty acids from malonyl-CoA and acetyl-CoA. The formation of unsaturated fatty acids is O2-independent and sharply reduced by 3-decynoyl-N-acetylcysteamine, a known inhibitor of Escherichia coli .beta.-hydroxydecanoyl thioester dehydrase (EC 4.2.1.60).