Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2'-deoxyadenosine substrates.
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.
Cobb
Steven L
SL
School of Chemistry, Centre for Biomolecular Sciences, University of St Andrews, Purdie Building, North Haugh, St Andrews, KY16 9ST, UK.
Deng
Hai
H
McEwan
Andrew R
AR
Naismith
James H
JH
O'Hagan
David
D
Robinson
David A
DA
D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D002712:Chlorides / Q000737:chemistry; D018360:Crystallography, X-Ray; D003839:Deoxyadenosines / Q000737:chemistry*; D005459:Fluorides / Q000737:chemistry; D006860:Hydrogen Bonding; D008958:Models, Molecular; D015394:Molecular Structure; D010088:Oxidoreductases / Q000737:chemistry*; D013302:Streptomyces / Q000145:classification / Q000201:enzymology*; D013379:Substrate Specificity
D001426:Bacterial Proteins; D002712:Chlorides; D003839:Deoxyadenosines; D010088:Oxidoreductases; C495766:fluorinase; C058118:2'-deoxyadenosine; D005459:Fluorides