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Comparative characterization and mutational analysis of type III pantothenate kinases
Thesis (MSc (Biochemistry))--University of Stellenbosch, 2006.
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| Format: | Thesis |
| Language: | English |
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Stellenbosch : University of Stellenbosch
2006
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| _version_ | 1867613948454371328 |
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| access_status_str | Open Access |
| author | Brand, Leisl Anne |
| author2 | Strauss, Erick |
| author_browse | Brand, Leisl Anne Strauss, Erick |
| author_facet | Strauss, Erick Brand, Leisl Anne |
| author_sort | Brand, Leisl Anne |
| collection | Thesis |
| dc_rights_str_mv | University of Stellenbosch |
| description | Thesis (MSc (Biochemistry))--University of Stellenbosch, 2006. |
| format | Thesis |
| id | oai:scholar.sun.ac.za:10019.1/1567 |
| institution | Stellenbosch University (South Africa) |
| language | English |
| last_indexed | 2026-06-10T12:44:15.221Z |
| license_str | Other — see source repository |
| provenance_str_mv | Harvested via OAI-PMH from SUNScholar — Stellenbosch University Repository |
| publishDate | 2006 |
| publishDateRange | 2006 |
| publishDateSort | 2006 |
| publisher | Stellenbosch : University of Stellenbosch |
| publisherStr | Stellenbosch : University of Stellenbosch |
| record_format | dspace |
| source_str | SUNScholar — Stellenbosch University Repository |
| spelling | oai:scholar.sun.ac.za:10019.1/1567 Comparative characterization and mutational analysis of type III pantothenate kinases Brand, Leisl Anne Strauss, Erick Swart, Pieter University of Stellenbosch. Faculty of Science. Dept. of Biochemistry. Pantothenate kinases Dissertations -- Biochemistry Theses -- Biochemistry Protein kinases Enzymes Proteins -- Synthesis Proteins -- Analysis Thesis (MSc (Biochemistry))--University of Stellenbosch, 2006. 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. 2006-09-27T12:09:02Z 2010-06-01T08:27:33Z 2006-09-27T12:09:02Z 2010-06-01T08:27:33Z 2006-03 Thesis http://hdl.handle.net/10019.1/1567 en University of Stellenbosch 2030898 bytes application/pdf application/pdf Stellenbosch : University of Stellenbosch |
| spellingShingle | Pantothenate kinases Dissertations -- Biochemistry Theses -- Biochemistry Protein kinases Enzymes Proteins -- Synthesis Proteins -- Analysis Brand, Leisl Anne Comparative characterization and mutational analysis of type III pantothenate kinases |
| title | Comparative characterization and mutational analysis of type III pantothenate kinases |
| title_full | Comparative characterization and mutational analysis of type III pantothenate kinases |
| title_fullStr | Comparative characterization and mutational analysis of type III pantothenate kinases |
| title_full_unstemmed | Comparative characterization and mutational analysis of type III pantothenate kinases |
| title_short | Comparative characterization and mutational analysis of type III pantothenate kinases |
| title_sort | comparative characterization and mutational analysis of type iii pantothenate kinases |
| topic | Pantothenate kinases Dissertations -- Biochemistry Theses -- Biochemistry Protein kinases Enzymes Proteins -- Synthesis Proteins -- Analysis |
| url | http://hdl.handle.net/10019.1/1567 |
| work_keys_str_mv | AT brandleislanne comparativecharacterizationandmutationalanalysisoftypeiiipantothenatekinases |