Comparative characterization and mutational analysis of type III pantothenate kinases
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.