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Plant Acyl-ACP Thioesterases: Chain-Length Determining Enzymes in Plant Fatty Acid Biosynthesis

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Genetic Engineering

Part of the book series: Genetic Engineering ((GEPM,volume 18))

Abstract

De novo plant fatty acid biosynthesis takes place in an organelle, the plastid. Acyl chains are elongated by 6 to 7 dissociable enzymes, together constituting a so-called type II fatty acid synthase. During the extension cycles the acyl chains are covalently bound, via a thioester, to the prosthetic group of a small, soluble, acyl carrier protein (ACP; 78 amino acid residues) (1,2). Taken together, these features make the plant fatty acid synthase distinct from the cytoplasmic, multi-subunit fatty acid synthase of animals and fungi (type I), but quite similar to the one common in prokaryotes (3). This functional similarity is one of the many vestiges of the prokaryotic ancestry of the plastids, which descended from cyanobacterial endosymbionts (4).

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  1. Calgene, Inc., 1922 Fifth Street, Davis, CA, 95616, USA

    Toni Voelker

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  1. Brookhaven National Laboratory, Upton, New York, USA

    Jane K. Setlow

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Voelker, T. (1996). Plant Acyl-ACP Thioesterases: Chain-Length Determining Enzymes in Plant Fatty Acid Biosynthesis. In: Setlow, J.K. (eds) Genetic Engineering. Genetic Engineering, vol 18. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1766-9_8

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