Molecular insights into the enzymatic diversity of flavin‐trafficking protein (Ftp; formerly ApbE) in flavoprotein biogenesis in the bacterial periplasm

@article{Deka2016MolecularII,
  title={Molecular insights into the enzymatic diversity of flavin‐trafficking protein (Ftp; formerly ApbE) in flavoprotein biogenesis in the bacterial periplasm},
  author={R. Deka and C. Brautigam and Wei Liu and D. Tomchick and M. Norgard},
  journal={MicrobiologyOpen},
  year={2016},
  volume={5},
  pages={21 - 38}
}
  • R. Deka, C. Brautigam, +2 authors M. Norgard
  • Published 2016
  • Biology, Medicine
  • MicrobiologyOpen
  • We recently reported a flavin‐trafficking protein (Ftp) in the syphilis spirochete Treponema pallidum (Ftp_Tp) as the first bacterial metal‐dependent FAD pyrophosphatase that hydrolyzes FAD into AMP and FMN in the periplasm. Orthologs of Ftp_Tp in other bacteria (formerly ApbE) appear to lack this hydrolytic activity; rather, they flavinylate the redox subunit, NqrC, via their metal‐dependent FMN transferase activity. However, nothing has been known about the nature or mechanism of metal… CONTINUE READING
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