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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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Escherichia coli K-12 substr. MG1655 Reaction: 2.7.1.21/2.7.1.145

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 2.7.1.21 , 2.7.1.145

Enzymes and Genes:
thymidine kinase Inferred from experiment : tdk

In Pathway: salvage pathways of pyrimidine deoxyribonucleotides

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 2.7.1.21: thymidine kinase

Enzyme Commission Synonyms for 2.7.1.21: thymidine kinase (phosphorylating), 2'-deoxythymidine kinase, deoxythymidine kinase (phosphorylating)

Enzyme Commission Primary Name for 2.7.1.145: deoxynucleoside kinase

Enzyme Commission Synonyms for 2.7.1.145: multispecific deoxynucleoside kinase, ms-dNK, multisubstrate deoxyribonucleoside kinase, multifunctional deoxynucleoside kinase, D. melanogaster deoxynucleoside kinase, Dm-dNK

Summary:
This reaction is part of the pyrimidine salvage pathway.

Enzyme Commission Summary for 2.7.1.21:
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 (AMPthymidine kinase), EC 2.7.1.118 (ADPthymidine kinase) and EC 2.7.4.9 (dTMP-kinase).

Enzyme Commission Summary for 2.7.1.145:
The enzyme from embryonic cells of Drosophila melanogaster differs from other deoxynucleoside kinases (EC 2.7.1.76 and EC 2.7.1.113) in its broad specificity for all four common deoxynucleosides.

Citations: [Falke82, Kizer74, Okazaki64, MunchPetersen00, MunchPetersen98]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:2.7.1.21 , BRENDA:EC:2.7.1.145 , ENZYME:EC:2.7.1.21 , ENZYME:EC:2.7.1.145 , IUBMB-ExplorEnz:EC:2.7.1.21 , IUBMB-ExplorEnz:EC:2.7.1.145


References

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

Kizer74: Kizer DE, Holman L (1974). "Purification and properties of thymidine kinase from regenerating rat liver." Biochim Biophys Acta 350(1);193-200. PMID: 4407348

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

Okazaki64: Okazaki R, Kornberg A (1964). "Deoxythymidine Kinase of Escherichia coli I. Purification and some properties of the enzyme." J Biol Chem 1964;239(1):269-274. PMID: 14114853


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Sun Dec 21, 2014, BIOCYC13B.