Study of the Enantioselectivity of Enzymes Involved in Nucleoside Analogue Metabolism: Deoxycytidine Kinase
- 1 July 1997
- journal article
- research article
- Published by Taylor & Francis in Nucleosides and Nucleotides
- Vol. 16 (7-9) , 1767-1770
- https://doi.org/10.1080/07328319708006274
Abstract
The substrate properties of recombinant human deoxycytidine kinase (dCK) with regard to a series of D- or L-enantiomers of cytidine, 2′-deoxycytidine, and 2′,3′-dideoxycytidine analogues were studied using HPLC analysis. Our results suggest that dCK has a remarkably relaxed enantioselectivity with respect to a large number of cytidine derivatives in the β configuration.Keywords
This publication has 7 references indexed in Scilit:
- The Effect of Absolute Configuration on the Anti-HIV and Anti-HBV Activity of Nucleoside AnaloguesAntiviral Chemistry and Chemotherapy, 1995
- 2 cloning and expression of mouse deoxycytidine kinase. Pure recombinant mouse and human enzymes show differences in substrate specificity.Journal of Biological Chemistry, 1994
- Influence of stereochemistry on antiviral activities and resistance profiles of dideoxycytidine nucleosidesAntimicrobial Agents and Chemotherapy, 1994
- Affinity of the antiviral enantiomers of oxathiolane cytosine nucleosides for human 2′-deoxycytidine kinaseBiochemical Pharmacology, 1993
- Beta-L-thymidine 5'-triphosphate analogs as DNA polymerase substrates.Journal of Biological Chemistry, 1992
- Cloning and expression of human deoxycytidine kinase cDNA.Proceedings of the National Academy of Sciences, 1991
- Deoxycytidine kinase from calf thymus. Substrate and inhibitor specificity.Journal of Biological Chemistry, 1976