Iron center, substrate recognition and mechanism of peptide deformylase

@article{Becker1998IronCS,
  title={Iron center, substrate recognition and mechanism of peptide deformylase},
  author={Andreas Becker and Ilme Schlichting and Wolfgang Kabsch and Dieter Groche and Sabine Schultz and A. F. Volker Wagner},
  journal={Nature Structural Biology},
  year={1998},
  volume={5},
  pages={1053-1058}
}
Eubacterial proteins are synthesized with a formyl group at the N-terminus which is hydrolytically removed from the nascent chain by the mononuclear iron enzyme peptide deformylase. Catalytic efficiency strongly depends on the identity of the bound metal. We have determined by X-ray crystallography the Fe2+, Ni2+ and Zn2+ forms of the Escherichia coli enzyme and a structure in complex with the reaction product Met-Ala-Ser. The structure of the complex, with the tripeptide bound at the active… CONTINUE READING

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thesis , Universität Heidelberg . Charakterisierung des Eisenzentrums und des Katalysemechanismus von Peptid - Deformylase aus Escherichia coli ( 1995 ) . 8 .

  • D. Ph. D. Groche
  • Biochem . Biophys . Res . Commun .
  • 1998

Charakterisierung des Eisenzentrums und des Katalysemechanismus von Peptid-Deformylase aus Escherichia coli

  • Groche, D. Ph.D. thesis, Universität Heidelberg
  • 1995

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