Date of Award:

5-2012

Document Type:

Thesis

Degree Name:

Master of Science (MS)

Department:

Chemistry and Biochemistry

Committee Chair(s)

Alvan C. Hengge

Committee

Alvan C. Hengge

Committee

Sean J. Johnson

Committee

Cheng Wei Tom Chang

Abstract

Phosphorylation and dephosphorylation are a highly pervasive mechanism in biology that is used by the cell to modulate enzymes and proteins. The presence of a phosphate group can activate or deactivate an enzyme. The phosphate group is linked to a protein by a phosphoester bond that is known to be highly stable in cytoplasmic pH range. Thus the breaking and formation of these bonds need to be effected by enzymes.

Recent discovery of the activity carried out by certain virulence related proteins (OspF released by Shigella and SpvC released by Salmonella) have resulted in a necessity to create a new class of dephosphorylating enzymes – phosphothreonine lyases.

This class of proteins forms an important drug target against salmonella and shigella. The objective of our work has been to decipher the mechanism by which these effector proteins catalyze the dephosphorylation. Elimination reactions can be carried out by several mechanisms, namely E1, E2, and E1cB. Identification of the mechanism will aid in drug design. This report presents the results of analytical and crystallographic techniques used to study the mechanism of the elimination catalyzed by SpvC.

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Comments

This work made publicly available electronically on December 21, 2012.

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