The use of the key enzyme involved in carbon–fluorine bond formation in Streptomyces cattleya catalysing the formation of 5′‐fluoro‐5′‐deoxyadenosine (5′‐FDA) from fluoride ion and S‐adenosyl‐l‐methionine (SAM) was explored for its potential application in fluorine‐18 labelling of the adenosine derivative. Enzymatic radiolabelling of [18F]‐5′‐FDA was successfully carried out starting from SAM and [18F]HF when the concentration of the enzyme preparation was increased from sub‐mg/ml values to mg/ml values. The purity of the enzyme had no measurable effect on the radiochemical yield of the reaction and the radiochemical purity of [18F]‐5′‐FDA. Copyright © 2003 John Wiley & Sons, Ltd.
|Number of pages||9|
|Journal||Journal of Labelled Compounds and Radiopharmaceuticals|
|Early online date||8 Oct 2003|
|Publication status||Published - Nov 2003|
Martarello, L., Schaffrath, C., Deng, H., Gee, A. D., Lockhart, A., & O’Hagan, D. (2003). The first enzymatic method for C–18F bond formation: the synthesis of 5′‐[18F]‐fluoro‐5′‐deoxyadenosine for imaging with PET. Journal of Labelled Compounds and Radiopharmaceuticals, 46(13), 1181-1189. https://doi.org/10.1002/jlcr.779