Identification of a monooxygenase from Streptomyces coelicolor A3(2) involved in biosynthesis of actinorhodin: purification and characterization of the recombinant enzyme.

@article{Kendrew1997IdentificationOA,
  title={Identification of a monooxygenase from Streptomyces coelicolor A3(2) involved in biosynthesis of actinorhodin: purification and characterization of the recombinant enzyme.},
  author={S. Kendrew and D. Hopwood and E. Marsh},
  journal={Journal of bacteriology},
  year={1997},
  volume={179 13},
  pages={
          4305-10
        }
}
The oxidation of phenols to quinones is an important reaction in the oxidative tailoring of many aromatic polyketides from bacterial and fungal systems. Sequence similarity between ActVA-Orf6 protein from the actinorhodin biosynthetic cluster and the previously characterized TcmH protein that is involved in tetracenomycin biosynthesis suggested that ActVA-Orf6 might catalyze this transformation as a step in actinorhodin biosynthesis. To investigate the role of ActVA-Orf6 in this oxidation, we… Expand
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References

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Enzymatic synthesis of a bacterial polyketide from acetyl and malonyl coenzyme A.
Genetics of actinorhodin biosynthesis by Streptomyces coelicolor A3(2).
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