Acyl carrier protein (ACP) inhibition and other differences between b-ketoacyl synthase (KAS) I and II
Research output: Contribution to journal › Journal article › Research › peer-review
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.
Original language | English |
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Journal | Biochemical Society Transactions |
Volume | 28 part 6 |
Pages (from-to) | 607-610 |
ISSN | 0300-5127 |
Publication status | Published - 2000 |
ID: 180327