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Structural Characterization of Two Short Unspecific Peroxygenases: Two Different Dimeric Arrangements.

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Unspecific peroxygenases (UPOs) are fungal enzymes valuable for industry. This study reveals the crystal structures of two UPOs, uncovering their dimeric arrangements and enabling a variant with enhanced fatty acid diepoxide production.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Unspecific peroxygenases (UPOs) are fungal enzymes with biotechnological potential, serving as stable alternatives to cytochrome P450 monooxygenases.
  • Limited structural information exists for UPOs, hindering the exploitation of their vast genetic diversity for industrial applications.
  • Only 19 Protein Data Bank entries represent UPOs, with published structures from just two species prior to this study.

Purpose of the Study:

  • To determine the crystal structures of two novel UPOs, rMroUPO and rCviUPO, from *Marasmius rotula* and *Collariella virescens*, respectively.
  • To elucidate the structural basis for the dimeric nature of these UPOs.
  • To engineer a UPO variant with enhanced capabilities for producing valuable compounds.

Main Methods:

  • Sequence optimization and expression of rMroUPO and rCviUPO in *Escherichia coli*.
  • Crystallization of the enzymes and collection of diffraction data at high resolution.
  • Structure determination by molecular replacement and analysis of dimer interfaces using biophysical and molecular biology techniques.

Main Results:

  • High-resolution crystal structures (1.45 Å for rMroUPO, 1.95 Å for rCviUPO) of the two UPOs were solved, revealing dimeric arrangements.
  • Diverse structural interactions, including disulfide bridges and alpha-helix associations, were identified at the dimer interfaces.
  • A modified rCviUPO variant lacking the C-terminal tail demonstrated an enhanced ability to produce fatty acid diepoxides.

Conclusions:

  • The study provides novel structural insights into two distinct UPO enzymes, highlighting varied dimeric arrangements.
  • The findings contribute to understanding UPO structure-function relationships and open avenues for protein engineering.
  • The engineered rCviUPO variant shows potential for industrial applications in producing cross-linking agents.