Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase.

@article{Mochalkin2008StructuralEF,
  title={Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase.},
  author={Igor Mochalkin and J. Richard Miller and Artem Evdokimov and Sandra A Lightle and Chunhong Yan and Charles Ken Stover and Grover L. Waldrop},
  journal={Protein science : a publication of the Protein Society},
  year={2008},
  volume={17 10},
  pages={1706-18}
}
Bacterial acetyl-CoA carboxylase is a multifunctional biotin-dependent enzyme that consists of three separate proteins: biotin carboxylase (BC), biotin carboxyl carrier protein (BCCP), and carboxyltransferase (CT). Acetyl-CoA carboxylase is a potentially attractive target for novel antibiotics because it catalyzes the first committed step in fatty acid biosynthesis. In the first half-reaction, BC catalyzes the ATP-dependent carboxylation of BCCP. In the second half-reaction, the carboxyl group… CONTINUE READING