| deoxynucleoside kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.145 | ||||||||
| CAS no. | 52227-81-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a deoxynucleoside kinase (EC 2.7.1.145) is an enzyme that catalyzes the chemical reaction
- ATP + 2'-deoxynucleoside ADP + 2'-deoxynucleoside 5'-phosphate
Thus, the two substrates of this enzyme are ATP and 2'-deoxynucleoside, whereas its two products are ADP and 2'-deoxynucleoside 5'-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:deoxynucleoside 5'-phosphotransferase. Other names in common use include multispecific deoxynucleoside kinase, ms-dNK, multisubstrate deoxyribonucleoside kinase, multifunctional deoxynucleoside kinase, D. melanogaster deoxynucleoside kinase, and Dm-dNK.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1OE0, 1OT3, 1ZM7, 1ZMX, and 2JCS.
References
- Munch-Petersen B, Piskur J, Sondergaard L (1998). "Four deoxynucleoside kinase activities from Drosophila melanogaster are contained within a single monomeric enzyme, a new multifunctional deoxynucleoside kinase". J. Biol. Chem. 273 (7): 3926–31. doi:10.1074/jbc.273.7.3926. PMID 9461577.
- Munch-Petersen B, Knecht W, Lenz C, Sondergaard L, Piskur J (2000). "Functional expression of a multisubstrate deoxyribonucleoside kinase from Drosophila melanogaster and its C-terminal deletion mutants". J. Biol. Chem. 275 (9): 6673–9. doi:10.1074/jbc.275.9.6673. PMID 10692477.