A novel adenylate binding site confers phosphopantetheine adenylyltransferase interactions with coenzyme A.

@article{Izard2003ANA,
  title={A novel adenylate binding site confers phosphopantetheine adenylyltransferase interactions with coenzyme A.},
  author={Tina Izard},
  journal={Journal of bacteriology},
  year={2003},
  volume={185 14},
  pages={4074-80}
}
  • Tina Izard
  • Published 2003 in Journal of bacteriology
Phosphopantetheine adenylyltransferase (PPAT) regulates the key penultimate step in the essential coenzyme A (CoA) biosynthetic pathway. PPAT catalyzes the reversible transfer of an adenylyl group from Mg(2+):ATP to 4'-phosphopantetheine to form 3'-dephospho-CoA (dPCoA) and pyrophosphate. The high-resolution crystal structure of PPAT complexed with CoA has been determined. Remarkably, CoA and the product dPCoA bind to the active site in distinct ways. Although the phosphate moiety within the… CONTINUE READING

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