Self-assembly of the binuclear metal center of phosphotriesterase.

@article{Shim2000SelfassemblyOT,
  title={Self-assembly of the binuclear metal center of phosphotriesterase.},
  author={H Shim and Frank M Raushel},
  journal={Biochemistry},
  year={2000},
  volume={39 25},
  pages={7357-64}
}
The active site of the bacterial phosphotriesterase (PTE) from Pseudomonas diminuta contains two divalent metal ions and a carboxylated lysine residue. The native enzyme contains two Zn(2+) ions, which can be replaced with Co(2+), Cd(2+), Ni(2+), or Mn(2+) without loss of catalytic activity. Carbon dioxide reacts with the side chain of lysine-169 to form a carbamate functional group within the active site, which then serves as a bridging ligand to the two metal ions. The activation of apo-PTE… CONTINUE READING