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

TY - JOUR

T1 - Acyl carrier protein (ACP) inhibition and other differences between b-ketoacyl synthase (KAS) I and II

AU - McGuire, Kirsten Arnvig

AU - McGuire, J.N.

AU - Wettstein-Knowles, Penny von

PY - 2000

Y1 - 2000

N2 - Escherichia coli b-ketoacyl synthases (KAS) I and II carry out the elongation steps in fatty acid synthesis. Analyses using the cross-linker BS3 [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 C14-acyl carrier protein (ACP) as well as for C14-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 µM ACP close to the physiological concentration of ACP (0.13 µM). KAS I and II also differ in carrying out the decarboxylation step of the elongation reaction.

AB - Escherichia coli b-ketoacyl synthases (KAS) I and II carry out the elongation steps in fatty acid synthesis. Analyses using the cross-linker BS3 [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 C14-acyl carrier protein (ACP) as well as for C14-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 µM ACP close to the physiological concentration of ACP (0.13 µM). KAS I and II also differ in carrying out the decarboxylation step of the elongation reaction.

M3 - Journal article

SN - 0300-5127

VL - 28 part 6

SP - 607

EP - 610

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

ER -