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Showing 1–2 of 2 results
Advanced filters: Author: "Steven D. Bruner" Clear advanced filters
  • Enzymes that selectively oxidize unactivated C–H bonds are capable of constructing complex molecules with high efficiency. A new member of this enzyme family is RedG, a Reiske-type oxygenase that catalyses chemically challenging cyclizations in the biosynthesis of prodiginine natural products.

    • Steven D. Bruner
    News & Views
    Nature Chemistry
    Volume: 3, P: 342-343
  • The final steps in the biosynthetic pathway to the morphine alkaloids have been revealed with the characterization of two key enzymes. In addition to the widely exploited parent compound, these new O-demethylases control metabolic flux to pharmaceutically useful opioid precursors.

    • Eric J Dimise
    • Steven D Bruner
    News & Views
    Nature Chemical Biology
    Volume: 6, P: 251-252