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Eukaryotic TYW1 Is a Radical SAM Flavoenzyme.

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Summary
This summary is machine-generated.

The TYW1 enzyme, crucial for tRNA synthesis, was studied in yeast. This radical S-adenosyl-l-methionine flavoenzyme shows unique activity with NAD(P)H, offering new insights into its biological function.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • TYW1 is a radical S-adenosyl-l-methionine (SAM) enzyme involved in tRNA biosynthesis.
  • Eukaryal TYW1 enzymes possess both a radical SAM domain and a flavin binding domain, unlike archaeal counterparts.

Purpose of the Study:

  • To characterize the Saccharomyces cerevisiae TYW1 (ScTYW1) enzyme.
  • To investigate the cofactor requirements and activity of ScTYW1.

Main Methods:

  • Heterologous expression of ScTYW1 in Escherichia coli.
  • Protein purification and homogeneity assessment.
  • Enzyme activity assays with various nucleotide and flavin cofactor combinations.

Main Results:

  • Purified ScTYW1 contained flavin mononucleotide (FMN) and iron, indicating partial saturation with Fe-S clusters and FMN.
  • ScTYW1 demonstrated activity with both NADPH and NADH.
  • Maximal product formation was observed when NAD(P)H was used in conjunction with flavin nucleotides.

Conclusions:

  • ScTYW1 is the first identified radical SAM flavoenzyme active with NAD(P)H alone.
  • This finding provides novel insights into the catalytic mechanism and cofactor utilization of TYW1 enzymes.