Purification and characterization of YfkN, a trifunctional nucleotide phosphoesterase secreted by Bacillus subtilis.

@article{Chambert2003PurificationAC,
  title={Purification and characterization of YfkN, a trifunctional nucleotide phosphoesterase secreted by Bacillus subtilis.},
  author={R{\'e}gis Chambert and Yannick Pereira and Marie-Françoise Petit-Glatron},
  journal={Journal of biochemistry},
  year={2003},
  volume={134 5},
  pages={655-60}
}
YfkN isolated from the culture supernatant of Bacillus subtilis in the exponential phase of growth is a protein of 143.5 kDa that derives from a putative large precursor of 159.6 kDa processed at both the N- and C-terminal ends. Pulse-chase experiments indicated that the release occurs slowly with a half-time longer than 30 min, suggesting that the event is coupled with wall turnover. YfkN exhibits 2',3' cyclic nucleotide phosphodiesterase, 2' (or 3') nucleotidase and 5' nucleotidase activities… CONTINUE READING

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