244183-90-2Relevant academic research and scientific papers
Study of human deoxycytidine kinase binding properties using intrinsic fluorescence or new fluorescent ligands
Shafiee, Manijeh,Gosselin, Gilles,Imbach, Jean-Louis,Divita, Gilles,Eriksson, Staffan,Maury, Georges
, p. 423 - 431 (2007/10/03)
A series of D- and L-enantiomers of cytidine or adenosine analogues and fluorescent N-methylanthraniloyl (MeNHBz) cytidine derivatives regiospecifically synthesized from cytidine or deoxycytidine were used to quantify the enantioselectivity of human deoxycytidine kinase (dCK) and to characterize its binding states. Both D- and L-enantiomers of these compounds induced significant bimodal quenchings of the intrinsic fluorescence of the enzyme. The ratios of dissociation constants Kd(D)/Kd(L) for the high affinity binding of non fluorescent cytidine derivatives were remarkably similar. β-D- and β-L-ATP gave monophasic titration curves and the enzyme displayed a preference for the natural enantiomer. This demonstrates the lack of enantioselectivity of dCK in the substrate binding steps of its mechanism. The results of other fluorescence experiments with MeNHBz-cytidine derivatives were consistent with an enzyme mechanism in which nucleotide binding precedes nucleoside binding.
Synthesis of new fluorescent nucleoside analogues and application to the study of human deoxycytidine kinase
Shafiee,Gosselin,Imbach,Eriksson,Maury
, p. 717 - 719 (2007/10/03)
We have determined the affinity of human deoxycytidine kinase with respect to new fluorescent N-methylanthraniloyl cytidine derivatives or non fluorescent enantiomeric cytidine analogues. New results regarding the enantioselectivity and the mechanism of the enzyme are presented.
