ADP—thymidine kinase
| ADP-thymidine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.118 | ||||||||
| CAS no. | 82114-39-4 | ||||||||
| 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, an ADP—thymidine kinase (EC 2.7.1.118) is an enzyme that catalyzes the chemical reaction
- ADP + thymidine AMP + thymidine 5'-phosphate
Thus, the two substrates of this enzyme are ADP and thymidine, whereas its two products are AMP and thymidine 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 ADP:thymidine 5'-phosphotransferase. Other names in common use include ADP:dThd phosphotransferase, and adenosine diphosphate-thymidine phosphotransferase.
References
[edit]- Falke D, Labenz J, Brauer D, Muller WE (1982). "Adenosine diphosphate: thymidine 5'-phosphotransferase, a new enzyme activity, associated with the Herpes simplex virus-induced deoxypyrimidine kinase". Biochim. Biophys. Acta. 708 (1): 99–103. doi:10.1016/0167-4838(82)90207-2. PMID 6293576.
