Date of Award:

2012

Document Type:

Thesis

Degree Name:

Master of Science (MS)

Department:

Chemistry and Biochemistry

Advisor/Chair:

Alvan C. Hengge

Abstract

The phosphothreonine lyase class of enzymes represents a recently discovered set of enzymes that catalyze a dephosphorylation reaction. The catalysis is carried out using a unique elimination mechanism without any involvement of cofactors. Crystallographic studies of SpvC, a phosphothreonine lyase, and its mutant show that the mutation of the general catalytic acid does not result in any significant perturbations to the tertiary and the secondary structure of the protein. Using results from the structural studies and a deuterium isotope exchange experiment, we conclude that the reaction catalyzed by SpvC may not involve formation of a carbanion at the active site.

Comments

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