EC 2.7.1.21 - Thymidine kinase

  IntEnz view ENZYME view
XML

IntEnz Enzyme Nomenclature
EC 2.7.1.21

Names

Accepted name:
thymidine kinase
Other names:
2'-deoxythymidine kinase
deoxythymidine kinase (phosphorylating)
thymidine kinase (phosphorylating)
Systematic name:
ATP:thymidine 5'-phosphotransferase

Reaction

Comments:

Deoxyuridine can also act as acceptor, and dGTP can act as a donor. The deoxypyrimidine kinase complex induced by Herpes simplex virus catalyses this reaction as well as those of EC 2.7.1.114 (AMP-thymidine kinase), EC 2.7.1.118 (ADP-thymidine kinase) and EC 2.7.4.9 (dTMP-kinase).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00524
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004797
CAS Registry Number: 9002-06-6
UniProtKB/Swiss-Prot: (261) [show] [UniProt]

References

  1. Falke, D., Labenz, J., Brauer, D. and Muller, W.E.G.
    Adenosine diphosphate: thymidine 5'-phosphotransferase, a new enzyme activity, associated with the Herpes simplex virus-induced deoxypyrimidine kinase.
    Biochim. Biophys. Acta 708 : 99-103 (1982). [PMID: 6293576]
  2. Kizer, D.E. and Holman, L.
    Purification and properties of thymidine kinase from regenerating rat liver.
    Biochim. Biophys. Acta 350 : 193-200 (1974). [PMID: 4407348]
  3. Okazaki, R. and Kornberg, A.
    Deoxythymidine kinase of Escherichia coli. I. Purification and some properties of the enzyme.
    J. Biol. Chem. 239 : 269-274 (1964). [PMID: 14114853]

[EC 2.7.1.21 created 1961, deleted 1972, reinstated 1976 (EC 2.7.1.75 created 1972, incorporated 1976)]