Investigating β-Hydroxyenduracididine Formation in the Biosynthesis of the Mannopeptimycins Academic Article uri icon

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  • The mannopeptimycins (MPPs) are potent glycopeptide antibiotics that contain both D and L forms of the unique, arginine-derived amino acid beta-hydroxyenduracididine (betahEnd). The product of the mppO gene in the MPP biosynthetic cluster resembles several non-heme iron, alpha-ketoglutarate-dependent oxygenases, such as VioC and clavaminate synthase. The role of MppO in betahEnd biosynthesis was confirmed through inactivation of mppO, which yielded a strain that produced dideoxy-MPPs, indicating that mppO is essential for generating the beta-hydroxy functionality for both betahEnd residues. Characterization in vitro of recombinant His6-MppO expressed in E. coli revealed that MppO selectively hydroxylates the beta carbon of free L-enduracididine.


  • Haltli, Brad
  • Tan, Ying
  • Magarvey, Nathan
  • Wagenaar, Melissa
  • Yin, Xihou
  • Greenstein, Michael
  • Hucul, John A
  • Zabriskie, T Mark

publication date

  • November 2005