Physics Commons^™

Inhibition Of The Aminopeptidase From Aeromonas Proteolytica By L-Leucinethiol: Kinetic And Spectroscopic Characterization Of A Slow, Tight-Binding Inhibitor–Enzyme Complex, David Bienvenue, Brian Bennett, Richard Holz

Richard C. Holz

The peptide inhibitor l-leucinethiol (LeuSH) was found to be a potent, slow-binding inhibitor of the aminopeptidase from Aeromonas proteolytica (AAP). The overall potency (KI*) of LeuSH was 7 nM while the corresponding alcohol l-leucinol (LeuOH) was a simple competitive inhibitor of much lower potency (KI=17 μM). These data suggest that the free thiol is likely involved in the formation of the E·I and E·I* complexes, presumably providing a metal ligand. In order to probe the nature of the interaction of LeuSH and LeuOH with the dinuclear active site of AAP, we have recorded both the electronic absorption and EPR spectra …