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.
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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.
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| skos:exactMatch | |
| uniprot:name |
Org. Biomol. Chem.
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| uniprot:author |
Cobb S.L.,
Deng H.,
McEwan A.R.,
Naismith J.H.,
O'Hagan D.,
Robinson D.A.
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| uniprot:date |
2006
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| uniprot:pages |
1458-1460
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| uniprot:title |
Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2'-deoxyadenosine substrates.
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| uniprot:volume |
4
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| dc-term:identifier |
doi:10.1039/b600574h
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