| EC |
2.7.1.145 |
| Accepted name: |
deoxynucleoside kinase |
| Reaction: |
ATP + a 2′-deoxyribonucleoside = ADP + a 2′-deoxyribonucleoside 5′-phosphate |
| Other name(s): |
multispecific deoxynucleoside kinase; ms-dNK; multisubstrate deoxyribonucleoside kinase; multifunctional deoxynucleoside kinase; D. melanogaster deoxynucleoside kinase; Dm-dNK; ATP:deoxynucleoside 5′-phosphotransferase |
| Systematic name: |
ATP:deoxyribonucleoside 5′-phosphotransferase |
| Comments: |
The enzyme from embryonic cells of the fruit fly Drosophila melanogaster differs from other 2′-deoxyribonucleoside kinases [EC 2.7.1.76 (deoxyadenosine kinase) and EC 2.7.1.113 (deoxyguanosine kinase)] in its broad specificity for all four common 2′-deoxyribonucleosides. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 52227-81-3 |
| References: |
| 1. |
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] |
| 2. |
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] |
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| [EC 2.7.1.145 created 2001] |
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