The enzyme from embryonic cells of the fruit fly Drosophila melanogaster differs from other 2′-deoxyribonucleoside kinases [EC 188.8.131.52 (deoxyadenosine kinase) and EC 184.108.40.206 (deoxyguanosine kinase)] in its broad specificity for all four common 2′-deoxyribonucleosides.
Munch-Petersen, B., Piskur, J. and Søndergaard, L. Four deoxynucleoside kinase activities from Drosophila melanogaster are contained within a single monomeric enzyme, a new multifunctional deoxynucleoside kinase. J. Biol. Chem.273 (1998) 3926–3931. [DOI] [PMID: 9461577]
Munch-Petersen, B., Knecht, W., Lenz, C., Søndergaard, L. and Piskur, J. Functional expression of a multisubstrate deoxyribonculeoside kinase from Drosophila melanogaster and its C-terminal deletion. J. Biol. Chem.275 (2000) 6673–6679. [DOI] [PMID: 10692477]