Investigating β-hydroxyenduracididine formation in the biosynthesis of the mannopeptimycins

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

Research output: Contribution to journalArticlepeer-review

41 Scopus citations


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

Original languageEnglish (US)
Pages (from-to)1163-1168
Number of pages6
JournalChemistry and Biology
Issue number11
StatePublished - Nov 2005
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Clinical Biochemistry


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