Characterization of the formation of the pyrrole moiety during clorobiocin and coumermycin A1 biosynthesis.

@article{Garneau2005CharacterizationOT,
  title={Characterization of the formation of the pyrrole moiety during clorobiocin and coumermycin A1 biosynthesis.},
  author={Sylvie Garneau and Pieter C. Dorrestein and Neil L. Kelleher and Christopher T Walsh},
  journal={Biochemistry},
  year={2005},
  volume={44 8},
  pages={2770-80}
}
The aminocoumarin antibiotics clorobiocin and coumermycin A(1) target the B subunit of DNA gyrase by presentation of the 5-methyl-pyrrolyl-2-carboxy ester moiety in the ATP-binding site of the enzyme. The pyrrolyl pharmacophore is derived by a four electron oxidation of a prolyl unit while tethered in phosphopantetheinyl thioester linkage to a peptidyl carrier protein (PCP) subunit. l-Proline is selected and activated as l-prolyl-AMP by adenylation domain enzymes (CloN4 and CouN4) and then… CONTINUE READING
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