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|Title:||Creation of a zymogen|
Stephen M. Fuchs
Ronald T. Raines
University of Wisconsin Madison
|Keywords:||Biochemistry, Genetics and Molecular Biology|
|Citation:||Nature Structural Biology. Vol.10, No.2 (2003), 115-119|
|Abstract:||Cells produce proteases as inactive zymogens. Here, we demonstrate that this tactic can extend beyond proteases. By linking the N and C termini of ribonuclease A, we obstruct the active site with the amino acid sequence recognized by plasmepsin II, a highly specific protease from Plasmodium falciparum. We generate new N and C termini by circular permutation. In the presence of plasmepsin II, a ribonuclease zymogen gains ∼103-fold in catalytic activity and maintains high conformational stability. We conclude that zymogen creation provides a new and versatile strategy for the control of enzymatic activity, as well as the potential development of chemotherapeutic agents.|
|Appears in Collections:||Scopus 2001-2005|
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