Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2'-deoxyadenosine substrates

Steven L. Cobb, Hai Deng, Andrew R McEwan, James H. Naismith, David O'hagan (Corresponding Author), David A. Robinson

Research output: Contribution to journalArticle

26 Citations (Scopus)

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 languageEnglish
Pages (from-to)1458-1460
Number of pages3
JournalOrganic & Biomolecular Chemistry
Issue number8
DOIs
Publication statusPublished - 2006

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Fluorination
fluorination
Halogenation
Substrate Specificity
enzymes
Substrates
Enzymes
Biocatalysis
ribose
adenosines
Ribose
Hydrogen Bonding
Adenosine
Conformations
Hydrogen bonds
hydrogen
fluorinase
2'-deoxyadenosine

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Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2'-deoxyadenosine substrates. / Cobb, Steven L. ; Deng, Hai; McEwan, Andrew R; Naismith, James H.; O'hagan, David (Corresponding Author); Robinson, David A.

In: Organic & Biomolecular Chemistry, No. 8, 2006, p. 1458-1460.

Research output: Contribution to journalArticle

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