Thesis (MSc (Biochemistry))--University of Stellenbosch, 2005. / This study describes:
1. The cloning of baboon cytochrome P450 side-chain cleavage (CYP11A1) cDNA by in
vitro site-directed mutagenesis.
2. The identification and sequencing of three baboon CYP11A1 mutants: CYP11A1a,
CYP11A1b and CYP11A1c.
3. The expression and characterisation of baboon and human CYP11A1 cDNA,
CYP11A1a, CYP11A1b and CYP11A1c in nonsteroidogenic COS-1 cells. The Km and
V-values for the metabolism of 25-hydroxycholesterol were determined.
4. The construction of the first homology model of CYP11A1, using both mammalian
(CYP2C5) and bacterial (CYP102) cytochromes P450 crystal structures as templates.
5. A structure/function study into the role of the amino acid residues Ile98, Lys103 and
Thr291 in substrate binding and enzymatic activity.
6. The proposal of a topological model of the CYP11A1 active pocket as determined by
substrate docking studies.
| Identifer | oai:union.ndltd.org:netd.ac.za/oai:union.ndltd.org:sun/oai:scholar.sun.ac.za:10019.1/3113 |
| Date | 12 1900 |
| Creators | Storbeck, Karl-Heinz |
| Contributors | Swart, A. C., Swart, P., University of Stellenbosch. Faculty of Science. Dept. of Biochemistry. |
| Publisher | Stellenbosch : University of Stellenbosch |
| Source Sets | South African National ETD Portal |
| Language | English |
| Detected Language | English |
| Type | Thesis |
| Format | 7447068 bytes, application/pdf |
| Rights | University of Stellenbosch |
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