Comparative characterization and mutational analysis of type III pantothenate kinases

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dc.contributor.advisorStrauss, Erick
dc.contributor.advisorSwart, Pieter
dc.contributor.authorBrand, Leisl Anne
dc.contributor.otherUniversity of Stellenbosch. Faculty of Science. Dept. of Biochemistry.
dc.date.accessioned2006-09-27T12:09:02Zen_ZA
dc.date.accessioned2010-06-01T08:27:33Z
dc.date.available2006-09-27T12:09:02Zen_ZA
dc.date.available2010-06-01T08:27:33Z
dc.date.issued2006-03
dc.descriptionThesis (MSc (Biochemistry))--University of Stellenbosch, 2006.
dc.description.abstractThis 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.en
dc.format.extent2030898 bytesen_ZA
dc.format.mimetypeapplication/pdfen_ZA
dc.identifier.urihttp://hdl.handle.net/10019.1/1567
dc.language.isoen
dc.publisherStellenbosch : University of Stellenbosch
dc.rights.holderUniversity of Stellenbosch
dc.subjectPantothenate kinasesen
dc.subjectDissertations -- Biochemistryen
dc.subjectTheses -- Biochemistryen
dc.subjectProtein kinasesen
dc.subjectEnzymesen
dc.subjectProteins -- Synthesisen
dc.subjectProteins -- Analysisen
dc.titleComparative characterization and mutational analysis of type III pantothenate kinasesen
dc.typeThesis
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