Abstract
The enzymatic conversion of isothiazolo[4,3-d]pyrimidine-based adenosine ((tz) A) and 2-aminoadenosine ((tz) 2-AA) analogues to the corresponding isothiazolo[4,3-d]pyrimidine-based inosine ((tz) I) and guanosine ((tz) G) derivatives is evaluated and compared to the conversion of native adenosine to inosine. Henri-Michaelis-Menten analyses provides the foundation for a high-throughput screening assay, and the efficacy of the assay is showcased by fluorescence-based analysis of (tz) A conversion to (tz) I in the presence of known and newly synthesized inhibitors.