The enzymes involved in hydrolysis of nucleoside triphosphates are a major focus of biochemical research, targeting the understanding and treatment of cellular processes involved in diseases such as cancer, viral infections, cardiovascular and motional disorders. To elucidate the mechanisms of action of these enzymes, it is often desirable to trap the enzymes in their triphosphate-bound state.
Since natural nucleotides are hydrolyzed at rates usually preventing such studies, nucleotide analogs are used that are hydrolyzed at much smaller rates or that are even completely resistant to hydrolysis. The position of the modification within the triphosphate exerts influence on its binding affinity to a certain enzyme and its hydrolysis rate.
