Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family.

@article{Chevrier1994CrystalSO,
  title={Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family.},
  author={Beno{\^i}t Chevrier and Catherine Schalk and H. D'Orchymont and J. M. Rondeau and Dino Moras and C{\'e}line Tarnus},
  journal={Structure},
  year={1994},
  volume={2 4},
  pages={283-91}
}
BACKGROUND Aminopeptidases specifically cleave the amino-terminal residue from polypeptide chains and are involved in the metabolism of biologically active peptides. The family includes zinc-dependent enzymes possessing either one or two zinc ions per active site. Structural studies providing a detailed view of the metal environment may reveal whether the one-zinc and two-zinc enzymes constitute structurally and mechanistically distinct subclasses, and what role the metal ions play in the… CONTINUE READING

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