Structural highlights
Function
NK_THEAC Nucleoside kinase with broad substrate specificity. Catalyzes the phosphorylation of a variety of nucleosides to the corresponding nucleoside 5'-mono-phosphate in the presence of phosphate donors and divalent cations. Displays the most efficient activity with guanosine, followed by inosine, cytidine, and adenosine. Negligible enzymatic activity is detected with thymidine, uridine, and 2-deoxyadenosine. ATP is the most efficient phosphate donor, but can also use GTP and ITP. Shows no sugar kinase activity, since it is unable to phosphorylate ribose, fructose-1-phosphate, or fructose-6-phosphate.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Elkin SR, Kumar A, Price CW, Columbus L. A broad specificity nucleoside kinase from Thermoplasma acidophilum. Proteins. 2013 Apr;81(4):568-82. doi: 10.1002/prot.24212. Epub 2013 Jan 17. PMID:23161756 doi:http://dx.doi.org/10.1002/prot.24212
