Document Type
Article
Publication Date
2006
Publication Title
Molecular Biosystems
Abstract
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.
Recommended Citation
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.
https://engagedscholarship.csuohio.edu/scichem_facpub/209
DOI
10.1039/B609936J
Version
Postprint
Volume
2
Issue
10
Comments
The work described in the authors’ lab was supported by the National Institutes of Health (R01GM61095), the Basil O’Connor Scholars Award–March of Dimes and the American Heart Association To C. K. Suzuki; The National Institutes Of Health (R01GM067172) to I. Lee; and the Ohio Board of Regent as the PRI award to A. J. Berdis and I. Lee.