Mechanism and inhibition of prolidase.

  title={Mechanism and inhibition of prolidase.},
  author={William L Mock and Phil Green},
  journal={The Journal of biological chemistry},
  volume={265 32},
The pH dependence of Ki for inhibition of prolidase by acetylproline, proline, and trans-1,2-cyclopentanedicarboxylate follows a different pattern in each case, although deprotonation of an enzymic functional group with a pKa value of 6.6 perturbs ligand binding in every instance. Results are most easily explained with prolidase active as a metalloenzyme dimer exhibiting selective cooperative interactions. 

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