Eriksson, Staffan
- Institutionen för molekylär biovetenskap, Sveriges lantbruksuniversitet
Sammanfattning
Deoxycytidine kinase (dCK), is responsible for the phosphorylation of deoxynucleosides to the corresponding monophosphates using ATP or UTP as phosphate donors. Steady-state intrinsic fluorescence measurements were used to study interaction of dCK with substrates in the absence and presence of phosphate donors. Enzyme fluorescence quenching by its substrates exhibited unimodal quenching when excited at 295 nm. Binding of substrates induced conformational changes in the protein, suggesting that dCK can assume different conformational states with different substrates and may account for the observed differences in their specificity. dCK bound the substrates more tightly in the presence of phosphate donors and UTP is the preferred phosphate donor. Among the substrates tested, the antitumour drugs gemcitabine and cladribine were bound very tightly by dCK, yielding Kd values of 0.75 and 0.8 muM, respectively, in the presence of UTP.
Nyckelord
deoxycytidine kinase; gemcitabine; fluorescence spectroscopy
Publicerad i
Nucleosides, Nucleotides and Nucleic Acids
2004, volym: 23, nummer: 45878, sidor: 1343-1346
Utgivare: MARCEL DEKKER INC
SLU författare
Publikationens identifierare
- DOI: https://doi.org/10.1081/NCN-200027609
Permanent länk till denna sida (URI)
https://res.slu.se/id/publ/3551