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Huomiao Ran1, Viola Wohlgemuth1, Xiulan Xie2

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|September 19, 2018
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Summary

A novel enzyme from Neosartorya fischeri hydroxylates tryprostatin B, a precursor to fumitremorgin mycotoxins. This enzyme, identified as a nonheme FeII/2-oxoglutarate-dependent oxygenase, catalyzes a unique double bond migration and hydroxylation reaction.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Mycology

Background:

  • Prenylation of cyclodipeptides diversifies structure and biological activity.
  • Metabolism of prenylated products involves hydroxylation by enzymes like cytochrome P450 and nonheme FeII/2-oxoglutarate-dependent oxygenases.
  • Fumitremorgin-type mycotoxins are produced by Aspergillus fumigatus, involving enzymes like FtmOx1Af.

Purpose of the Study:

  • To clone and overexpress NFIA_045530 from Neosartorya fischeri.
  • To characterize the enzymatic activity of the recombinant protein EAW25734.
  • To elucidate the role of this enzyme in the metabolism of fumitremorgin/verruculogen pathway intermediates.

Main Methods:

  • Cloning and overexpression of NFIA_045530.
  • Purification of the recombinant protein EAW25734.
  • Enzymatic assays using fumitremorgin biosynthetic pathway intermediates, FeII, and 2-oxoglutarate.
  • Liquid chromatography-mass spectrometry (LC-MS) analysis for product identification.
  • Structure elucidation of enzyme products.
  • Incubation with 18O2-enriched atmosphere to trace oxygen origin.
  • Analysis of Neosartorya fischeri extracts.

Main Results:

  • The recombinant protein EAW25734 showed no consumption of fumitremorgin B but good conversion of tryprostatin B.
  • 22-hydroxylisotryprostatin B and 14α, 22-dihydroxylisotryprostatin B were identified as major products.
  • The enzyme catalyzes a novel double bond migration within the dimethylallyl moiety of tryprostatin B with concomitant hydroxylation.
  • Oxygen (O2) was confirmed as the major source of hydroxyl groups.
  • Solvent exchange was observed at C22.
  • 22-hydroxylisotryprostatin B was detected in Neosartorya fischeri extracts.

Conclusions:

  • A novel nonheme FeII/2-oxoglutarate-dependent oxygenase from Neosartorya fischeri was identified.
  • This enzyme plays a role in the metabolism of fumitremorgin/verruculogen pathway intermediates by hydroxylating tryprostatin B.
  • The enzyme exhibits a unique catalytic mechanism involving double bond migration and hydroxylation.
  • A plausible reaction mechanism involving radical rearrangement is proposed.