| EPSRC Reference: |
GR/S97491/01 |
| Title: |
Extending the substrate specificity of enzymatic flourination. An entriely novel biocatalysis |
| Principal Investigator: |
O'Hagan, Professor D |
| Other Investigators: |
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| Researcher Co-Investigators: |
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| Project Partners: |
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| Department: |
Chemistry |
| Organisation: |
University of St Andrews |
| Scheme: |
Standard Research (Pre-FEC) |
| Starts: |
01 October 2004 |
Ends: |
30 September 2007 |
Value (£): |
181,982
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| EPSRC Research Topic Classifications: |
| Biological & Medicinal Chem. |
Bioprocess Engineering |
| Chemical Synthetic Methodology |
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| EPSRC Industrial Sector Classifications: |
| Food and Drink |
Pharmaceuticals and Biotechnology |
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| Related Grants: |
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| Panel History: |
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Summary on Grant Application Form |
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The study will explore the substrate specificity of an entirely new class of biotransformation. C-F bond formation. A fluorination enzyme has recently been isolated, cloned and overexpressed from the bacterium Streptomyces cattleya. The enzyme combines inorganic fluoride with S-adenosyl-Lmethionine to generate an organic fluorine metabolite, 5'-fluorodeoxyadenoise. This is the first native enzyme which has been isolated with the capability to generate C-F bonds. Of course organo fluorine compounds are of huge commercial importance so it is attractive now to consider the prospects of using this enzyme in biotransformations. The enzyme is immediately attractive as a catalyst for the synthesis of F-18 labelled organic fluorine biochemicals (nucleosides, riboses etc). This has already been demonstrated. There are prospects too of placing the gene for the fluorinaytion enzyme into other hosts for scale up biotransformations. The purpose of this research is now to explore the substrate specificity of the enzyme. This is being pursued with a background that the enzyme shows some substrate specificity (eg 2'-deoxy series) and that there is a very recent X-ray structure of the enzyme bound to SAM and to the product 5'-FDA.A range of candidate substrates are identified for synthesis and enzymatic assay.
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Key Findings |
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This information can now be found on Gateway to Research (GtR) http://gtr.rcuk.ac.uk
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Potential use in non-academic contexts |
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This information can now be found on Gateway to Research (GtR) http://gtr.rcuk.ac.uk
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Impacts |
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| Description |
This information can now be found on Gateway to Research (GtR) http://gtr.rcuk.ac.uk |
| Summary |
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| Date Materialised |
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Sectors submitted by the Researcher |
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This information can now be found on Gateway to Research (GtR) http://gtr.rcuk.ac.uk
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| Project URL: |
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| Further Information: |
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| Organisation Website: |
http://www.st-and.ac.uk |