The iron-sulfur cluster in the L-serine dehydratase TdcG from Escherichia coli is required for enzyme activity.

@article{Burman2004TheIC,
  title={The iron-sulfur cluster in the L-serine dehydratase TdcG from Escherichia coli is required for enzyme activity.},
  author={Julia D Burman and Roger L. Harris and Katherine A Hauton and David M. Lawson and Robert Gary Sawers},
  journal={FEBS letters},
  year={2004},
  volume={576 3},
  pages={442-4}
}
The anaerobically inducible L-serine dehydratase, TdcG, from Escherichia coli was characterized. Based on UV-visible spectroscopy, iron and labile sulfide analyses, the homodimeric enzyme is proposed to have two oxygen-labile [4Fe-4S]2+ clusters. Anaerobically isolated dimeric TdcG had a kcat of 544 s(-1) and an apparent KM for L-serine of 4.8 mM. L… CONTINUE READING