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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Investigating beta-hydroxyenduracididine formation in the biosynthesis of the mannopeptimycins.

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.[1]

References

  1. Investigating beta-hydroxyenduracididine formation in the biosynthesis of the mannopeptimycins. Haltli, B., Tan, Y., Magarvey, N.A., Wagenaar, M., Yin, X., Greenstein, M., Hucul, J.A., Zabriskie, T.M. Chem. Biol. (2005) [Pubmed]
 
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