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Proc. Natl. Acad. Sci. USA Vol. 96, pp. 1100811014, September 1999
 

Summary: Proc. Natl. Acad. Sci. USA
Vol. 96, pp. 1100811014, September 1999
Colloquium Paper
This paper was presented at the National Academy of Sciences colloquium ``Proteolytic Processing and Physiological
Regulation,'' held February 2021, 1999, at the Arnold and Mabel Beckman Center in Irvine, CA.
Kinetic stability as a mechanism for protease longevity
ERIN L. CUNNINGHAM, SHEILA S. JASWAL, JULIE L. SOHL*, AND DAVID A. AGARD
Graduate Group in Biophysics, Howard Hughes Medical Institute, and Department of Biochemistry and Biophysics, University of California, San Francisco,
CA 94143-0448
ABSTRACT The folding of the extracellular serine pro-
tease, -lytic protease ( LP; EC 3.4.21.12) reveals a novel
mechanism for stability that appears to lead to a longer
functional lifetime for the protease. For LP, stability is based
not on thermodynamics, but on kinetics. Whereas this has
required the coevolution of a pro region to facilitate folding,
the result has been the optimization of native-state properties
independent of their consequences on thermodynamic stabil-
ity. Structural and mutational data lead to a model for
catalysis of folding in which the pro region binds to a
conserved -hairpin in the LP C-terminal domain, stabiliz-

  

Source: Agard, David - Department of Biochemistry and Biophysics, University of California at San Francisco

 

Collections: Biotechnology; Biology and Medicine