QM/MM and QM calculations have been applied to investigate and refine modelled features of the substrate binding characteristics and catalysed rearrangement of chorismate to prephenate in Bacillus Suhtilis chorismate mutase. The structural details of the modelled active site and enzyme-substrate binding interactions in a range of QM/MM simulations are investigated and compared with results from detailed analysis of the available crystal structure data. This has helped to identify significant variations between experimental and modelled details of key enzyme-substrate interactions. Detailed structure-activity relationship studies of multiple high level reaction profiles previously run in the group have demonstrated that such variations in the substrate binding interactions have a dramatic on the modelled barrier height and reaction energy.
| Identifer | oai:union.ndltd.org:bl.uk/oai:ethos.bl.uk:495642 |
| Date | January 2008 |
| Creators | Macrae, Stephen J. |
| Publisher | University of Bristol |
| Source Sets | Ethos UK |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
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