Abstract:
This thesis reports the cloning, overexpression and characterization of the
coaX gene product from Bacillus subtilis and its homologue from Helicobacter
pylori. It demonstrates that these proteins have pantothenate kinase activity.
Compared to the two pantothenate kinase analogues classified to date, these
two enzymes exhibit distinctly different characteristics, suggesting that they
are the first characterized examples of a third pantothenate kinase analogue.
In addition, mutational studies are presented that probe the importance of
conserved aspartate residues within the active sites of these newly
characterized analogues. The results show that these residues are important
for the activity of the protein.
