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Mechanism and inhibition of prolidase.

The Journal of biological chemistry (1990-11-15)
W L Mock, P C Green
RÉSUMÉ

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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Sigma-Aldrich
N-Acetyl-L-proline