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Copper-Dependent Hydroxylation Catalyzed by the DUF3328 Enzyme CctR.

Kaushik Seshadri1, Chen-Yu Chiang1, Kyle K Nagasawa2

  • 1Department of Chemical and Biomolecular Engineering, University of California, Los Angeles, California 90095, United States.

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Summary

This study characterizes CctR, a novel enzyme in the domain of unknown function (DUF) 3328 family. CctR catalyzes a copper- and oxygen-dependent hydroxylation reaction, expanding the known functions of DUF3328 enzymes in fungal natural product biosynthesis.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Fungal Natural Product Biosynthesis

Background:

  • Domain of unknown function (DUF) 3328 enzymes are implicated in diverse fungal natural product biosynthesis pathways.
  • Previously, only two DUF3328 enzymes, ApnU (halogenase) and AprY (macrocyclase), had been biochemically characterized.
  • The catalytic capabilities of the DUF3328 enzyme family remain largely unexplored.

Purpose of the Study:

  • To biochemically characterize CctR, a novel enzyme belonging to the DUF3328 family.
  • To elucidate the specific catalytic activity of CctR in hydroxycyclochlorotine biosynthesis.
  • To expand the known enzymatic repertoire of DUF3328 proteins.

Main Methods:

  • Biochemical assays were employed to determine the enzymatic activity of CctR.
  • Copper and oxygen dependency for the catalytic reaction were investigated.
  • The role of CctR in the biosynthesis of hydroxycyclochlorotine was analyzed.

Main Results:

  • CctR was identified as a DUF3328 enzyme.
  • CctR catalyzes a copper- and oxygen-dependent C(sp3)-H hydroxylation reaction.
  • This hydroxylation is a key step in the biosynthesis of hydroxycyclochlorotine.

Conclusions:

  • The catalytic repertoire of DUF3328 enzymes is broader than previously known.
  • CctR represents a new class of hydroxylases within the DUF3328 family.
  • This finding contributes to understanding fungal natural product biosynthesis and enzyme evolution.