Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

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 Fri Dec 19, 2014, BIOCYC13B.