Acyl carrier protein (ACP) inhibition and other differences between β-ketoacyl synthase (KAS) I and II

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Abstract
Escherichia coli beta-ketoacyl synthases (KAS) I and II carry out the elongation steps in fatty acid synthesis. Analyses using the cross-linker BS(3) [bis(sulphosuccinimidyl) suberate] and surface-enhanced laser desorption/ionization-time-of-flight MS disclosed only monomeric and dimeric forms of KAS II, whereas KAS I also forms higher multimers. The binding affinities for KAS I and KAS II to C(14)-acyl carrier protein (ACP) as well as for C(14)-ACP to KAS I and KAS II were determined. KAS I is sensitive to the ACP released during the transfer reaction, with 50% inhibition at 0.17 microM ACP close to the physiological concentration of ACP (0.13 microM). KAS I and II also differ in carrying out the decarboxylation step of the elongation reaction.

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