Mechanism and inhibition of prolidase.
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.
Mock
W L
WL
Department of Chemistry, University of Illinois, Chicago 60680-4348.
Green
P C
PC
D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D002264:Carboxylic Acids / Q000737:chemistry / Q000494:pharmacology; D003517:Cyclopentanes / Q000737:chemistry / Q000494:pharmacology; D004150:Dipeptidases / Q000037:antagonists & inhibitors*; D006863:Hydrogen-Ion Concentration; D007668:Kidney / Q000201:enzymology; D046911:Macromolecular Substances; D015394:Molecular Structure; D011392:Proline / Q000031:analogs & derivatives / Q000494:pharmacology; D013329:Structure-Activity Relationship; D013552:Swine
D002264:Carboxylic Acids; D003517:Cyclopentanes; D046911:Macromolecular Substances; C066484:1,2-cyclopentanedicarboxylate; D011392:Proline; C055247:N-acetylproline; D004150:Dipeptidases; C022449:proline dipeptidase