Projects per year
Abstract
The fluorinase enzyme from Streptomyces cattleya displays an unusual ability in biocatalysis in that it forms a C - F bond. We now report that the enzyme will accept 2'-deoxyadenosine in place of adenosine substrates, and structural evidence reveals a reorganisation in hydrogen bonding to accommodate this substrate series. It emerges from this study that the enzyme does not require a planar ribose conformation of the substrate to catalyse C - F bond formation.
| Original language | English |
|---|---|
| Pages (from-to) | 1458-1460 |
| Number of pages | 3 |
| Journal | Organic & Biomolecular Chemistry |
| Volume | 4 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - Apr 2006 |
Keywords
- BOND FORMATION
- CONVENIENT PREPARATION
- BIOSYNTHESIS
- REFINEMENT
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Dive into the research topics of 'Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2'-deoxyadenosine substrates'. Together they form a unique fingerprint.Projects
- 4 Finished
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bb/c000080/1: The pyrrolnitrin biosynthetic pathway
Naismith, J. (PI)
Biotechnology and Biological Sciences Research Council
1/01/05 → 1/05/10
Project: Standard
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BBSRC BBS/B/14426: SPORT
Naismith, J. (PI)
Biotechnology and Biological Sciences Research Council
18/10/04 → 30/04/12
Project: Standard
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GR/S97491/01: Extending the substratespecificity of enzymatic fluorination. An entirely novel biocatalysis
O'Hagan, D. (PI)
1/10/04 → 30/09/07
Project: Standard
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