Structural and kinetic characterization of chorismate synthase; the last enzyme of the shikimate pathway.
Published: 2004
Language: eng
Number of pages: 92
Description: The shikimate pathway has immense biological significance given its existence in plants, bacteria and fungi but not animals, and is the target of the broad spectrum herbicide, Glyphosate. The three-dimensional (3D) structure of each component of the pathway has been elucidated save chorismate synthase (CS), the final enzyme. In this thesis the structure of CS from Aquifex aeolicus is reported following a proteomics-based strategy designed to yield protein crystals of CS from several different species. This 3D structure is compared and contrasted to other examples subsequently published. Using the 3D structure of CS from Streptococcus pneumoniae [MacLean and All, (2003). Structure 11; 1499] targeted mutagenesis was performed on residues conserved in CS from Arabidopsis thaliana. Each CS mutant was assayed for activity and compared to wild-type. The effect of each mutation is discussed in context of the 3D structure of the active site and mechanistically unique reaction catalyzed by CS.
Notes: Adviser:  Dinesh Christendat.

Thesis (M.Sc.)--University of Toronto, 2004.

Electronic version licensed for access by U. of T. users.

Source: Masters Abstracts International, Volume: 43-03, page: 0766.

MICR copy on microfiche (1 microfiche).