Structurally distinct active sites in the copper(II)-substituted aminopeptidases from Aeromonas proteolytica and Escherichia coli.

@article{Bennett2002StructurallyDA,
  title={Structurally distinct active sites in the copper(II)-substituted aminopeptidases from Aeromonas proteolytica and Escherichia coli.},
  author={Brian Bennett and William E. Antholine and Ventris M D'souza and Guanjing Chen and Leila Ustinyuk and Richard C Holz},
  journal={Journal of the American Chemical Society},
  year={2002},
  volume={124 44},
  pages={13025-34}
}
The aminopeptidase from Aeromonas proteolytica (AAP) was titrated with copper, which bound sequentially at two distinct sites. Both the mono- and disubstituted forms of AAP exhibited catalytic hyperactivity relative to the native dizinc enzyme. Monosubstituted AAP exhibited an axial Cu(II) EPR spectrum with slight pH dependence: at pH 6.0 g(parallel) = 2.249, g( perpendicular ) = 2.055, and A(parallel)((63/65)Cu) = 1.77 x 10(-)(2) cm(-)(1), whereas at pH 9.65 g(parallel) = 2.245, g… CONTINUE READING

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