Structure of the enzyme-acyl carrier protein (ACP) substrate gatekeeper complex required for biotin synthesis.

@article{Agarwal2012StructureOT,
  title={Structure of the enzyme-acyl carrier protein (ACP) substrate gatekeeper complex required for biotin synthesis.},
  author={Vinayak A. Agarwal and Steven A. Lin and Tiit Lukk and Satish K Nair and John E. Cronan},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2012},
  volume={109 43},
  pages={17406-11}
}
Although the pimeloyl moiety was long known to be a biotin precursor, the mechanism of assembly of this C7 α,ω-dicarboxylic acid was only recently elucidated. In Escherichia coli, pimelate is made by bypassing the strict specificity of the fatty acid synthetic pathway. BioC methylates the free carboxyl of a malonyl thioester, which replaces the usual acetyl thioester primer. This atypical primer is transformed to pimeloyl-acyl carrier protein (ACP) methyl ester by two cycles of fatty acid… CONTINUE READING
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