Lon protease, also known as protease La, is one of the simplest ATP-dependent proteases that plays vital roles in maintaining cellular functions by selectively eliminating misfolded, damaged and certain short-lived regulatory proteins. Although Lon is a homo-oligomer, each subunit of Lon contains both an ATPase and a protease active site. This relatively simple architecture compared to other hetero-oligomeric ATP-dependent proteases such as the proteasome makes Lon a useful paradigm for studying the mechanism of ATP-dependent proteolysis. In this article, we survey some recent developments in the mechanistic characterization of Lon with an emphasis on the utilization of pre-steady-state enzyme kinetic techniques to determine the timing of the ATPase and peptidase activities of the enzyme.
Lee, Irene; Berdis, Anthony J.; and Suzuki, Carolyn K., "Recent Developments inThe Mechanistic Enzymology of The ATP-Dependent Lon Protease from Escherichia Coli: Highlights From Kinetic Studies" (2006). Chemistry Faculty Publications. 209.