Lon contains an intrinsic ATPase activity that is stimulated by peptide or protein
substrates.
We have constructed a minimal kinetic model to account for the ATP-dependent
peptidase activity of Lon.
Although Lon cleaves peptide upon binding to ATP, maximal peptide cleavage
requires ATP hydrolysis.
Although Lon, as a homooligomer, contains an identical ATPase domain in each
subunit, the ATPase sites in Lon are functionally non-equivalent.
The functionally non-equivalent ATPase sites are distinguishable by their pre-steady
state kinetic behavior as well as by their respective affinities for ATP.
