Literature summary extracted from
Kotaka, M.; Dhaliwal, B.; Ren, J.; Nichols, C.E.; Angell, R.; Lockyer, M.; Hawkins, A.R.; Stammers, D.K.
Structures of S. aureus thymidylate kinase reveal an atypical active site configuration and an intermediate conformational state upon substrate binding (2006), Protein Sci., 15, 774-784.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.7.4.9 |
expression in Escherichia coli |
Staphylococcus aureus |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.7.4.9 |
For the His-tagged SaTMK crystals, data is collected on beamline ID 14.1 at the ESRF (Grenoble, France). |
Staphylococcus aureus |
2.7.4.9 |
The data for the untagged SaTMK crystals is collected using Cu Ka radiation from a Rigaku MicroMax 007 generator equipped with aMAR345 image plate. |
Staphylococcus aureus |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.7.4.9 |
thymidine monophosphate + ATP |
Staphylococcus aureus |
Thymidylate kinase (TMK) (E.C. 2.7.4.9) is a member of the NMP kinase family and catalyzes the phosphoryl transfer from the preferred phosphoryl donor, ATP, to thymidine monophosphate (TMP), yielding thymidine diphosphate (TDP). The TMK reaction is positioned at the junction of the de novo and salvage pathway of thymidine triphosphate (dTTP) synthesis, with TMK being the last specific enzyme for dTTP synthesis. |
thymidine diphosphate + ADP |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.4.9 |
Staphylococcus aureus |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.7.4.9 |
Zn2+ charched sepharose column, hydroxyapalite column |
Staphylococcus aureus |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.7.4.9 |
thymidine monophosphate + ATP |
Thymidylate kinase (TMK) (E.C. 2.7.4.9) is a member of the NMP kinase family and catalyzes the phosphoryl transfer from the preferred phosphoryl donor, ATP, to thymidine monophosphate (TMP), yielding thymidine diphosphate (TDP). The TMK reaction is positioned at the junction of the de novo and salvage pathway of thymidine triphosphate (dTTP) synthesis, with TMK being the last specific enzyme for dTTP synthesis. |
Staphylococcus aureus |
thymidine diphosphate + ADP |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.7.4.9 |
S. aureus thymidylate kinase |
- |
Staphylococcus aureus |