Energetics of Leucyl-Leucine Hydrolysis in Streptococcus cremoris Wg(2).

The hydrolysis of the dipeptide leucyl-leucine by whole cells of Streptococcus cremoris Wg(2) was dependent on the presence of the energy source lactose. Incubation of cells with uncouplers or ATPase inhibitors prevented the increase of peptidase activity upon the addition of lactose. Incubation with the ionophore nigericin resulted in decreased peptide hydrolysis activity, while incubation with valinomycin led to increased hydrolysis activity. In the presence of nigericin the DeltapH component of the proton motive force was decreased, while the electrical potential was increased. With valinomycin, the electrical potential was collapsed and the DeltapH was increased. When the external pH was decreased from 8 to 5, the rate of peptide hydrolyzing activity by whole cells increased with increasing DeltapH component. In contrast, the peptide hydrolyzing activity in the cell extract decreased with decreasing external pH. These results indicate that the DeltapH component of the proton motive force determines the leucyl-leucine hydrolyzing activity in S. cremoris Wg(2).