Transient kinetic studies of fatty acid synthetase. A kinetic self-editing mechanism for the loading of acetyl and malonyl residues and the role of coenzyme A.

Abstract

A kinetic self-editing mechanism for correcting errors in the loading of thioester substrates is described for the animal fatty acid synthetase reaction. In the catalyzed reaction, these substrates load competitively on a common phosphopantetheine site, and during each of the eight loading steps the enzyme sites are partitioned between competent and… (More)

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