|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name for 126.96.36.199: thymidine kinase
Enzyme Commission Synonyms for 188.8.131.52: thymidine kinase (phosphorylating), 2'-deoxythymidine kinase, deoxythymidine kinase (phosphorylating)
Enzyme Commission Primary Name for 184.108.40.206: deoxynucleoside kinase
Enzyme Commission Synonyms for 220.127.116.11: multispecific deoxynucleoside kinase, ms-dNK, multisubstrate deoxyribonucleoside kinase, multifunctional deoxynucleoside kinase, D. melanogaster deoxynucleoside kinase, Dm-dNK
This reaction is part of the pyrimidine salvage pathway.
Enzyme Commission Summary for 18.104.22.168:
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 22.214.171.124 (AMPthymidine kinase), EC 126.96.36.199 (ADPthymidine kinase) and EC 188.8.131.52 (dTMP-kinase).
Enzyme Commission Summary for 184.108.40.206:
The enzyme from embryonic cells of Drosophila melanogaster differs from other deoxynucleoside kinases (EC 220.127.116.11 and EC 18.104.22.168) in its broad specificity for all four common deoxynucleosides.
Falke82: 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. PMID: 6293576
MunchPetersen00: 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. PMID: 10692477
MunchPetersen98: 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. PMID: 9461577
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