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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry*
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Binding Sites
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Chlorides / chemistry
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Crystallography, X-Ray
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Deoxyadenosines / chemistry*
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Fluorides / chemistry
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Hydrogen Bonding
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Models, Molecular
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Molecular Structure
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Oxidoreductases / chemistry*
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Streptomyces / classification
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Streptomyces / enzymology*
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Substrate Specificity
Substances
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Bacterial Proteins
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Chlorides
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Deoxyadenosines
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Oxidoreductases
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fluorinase
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2'-deoxyadenosine
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Fluorides