Purification, characterization, and inhibition of peptide deformylase from Escherichia coli.

@article{Rajagopalan1997PurificationCA,
  title={Purification, characterization, and inhibition of peptide deformylase from Escherichia coli.},
  author={P T Ravi Rajagopalan and Anindya Datta and Dehua Pei},
  journal={Biochemistry},
  year={1997},
  volume={36 45},
  pages={13910-8}
}
Peptide deformylase (EC 3.5.1.31) catalyzes the removal of a formyl group from the N-termini of nascent ribosome-synthesized polypeptides, an obligatory step during protein maturation in eubacteria. Since its discovery in crude Escherichia coli extracts 3 decades ago, the deformylase has resisted all attempts of purification or characterization due to its extraordinary lability. By placing the coding sequence (def gene) of Escherichia coli deformylase behind a bacteriophage T7 promoter, we have… CONTINUE READING