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Literature summary for 2.7.1.21 extracted from

  • Barroso, J.F.; Elholm, M.; Flatmark, T.
    Tight binding of deoxyribonucleotide triphosphates to human thymidine kinase 2 expressed in Escherichia coli. Purification and partial characterization of its dimeric and tetrameric forms (2003), Biochemistry, 42, 15158-15169.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination, expression in Escherichia coli as maltose binding fusion protein in inclusion bodies, coexpression of GroEL/ES molecular chaperone system improves enzyme solubility only marginally, but ethanol supplementation contributes to enzyme recovery due to activation of heat shock response Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics Homo sapiens
0.0047
-
ATP dimeric enzyme, pH 7.5, 25°C Homo sapiens
0.0109
-
ATP tetrameric enzyme, pH 7.5, 25°C Homo sapiens
0.018
-
2'-deoxycytidine tetrameric enzyme, pH 7.5, 25°C Homo sapiens
0.025
-
2'-deoxycytidine dimeric enzyme, pH 7.5, 25°C Homo sapiens
0.05
-
2'-deoxythymidine tetrameric enzyme, pH 7.5, 25°C Homo sapiens
0.054
-
2'-deoxythymidine dimeric enzyme, pH 7.5, 25°C Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Homo sapiens 5829
-
mitochondrion
-
Homo sapiens 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
oligomeric states have MWs of 152200 and 95900, as determined by gel filtration Homo sapiens
48800
-
recombinant enzyme, gel filtration Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + 2'-deoxycytidine Homo sapiens
-
ADP + 2'-deoxycytidine 5'-phosphate
-
ir
ATP + 2'-deoxythymidine Homo sapiens
-
ADP + 2'-deoxythymidine 5'-phosphate
-
ir
ATP + 2'-deoxyuridine Homo sapiens
-
ADP + 2'-deoxyuridine 5'-phosphate
-
ir

Organism

Organism UniProt Comment Textmining
Homo sapiens O00142
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme as maltose binding fusion protein from Escherichia coli Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
ATP + thymidine = ADP + dTMP molecular docking of substrates and inhibitors, active site structure modeling Homo sapiens

Renatured (Commentary)

Renatured (Comment) Organism
coexpression of GroEL/ES molecular chaperone system improves recombinant enzyme solubility from inclusion bodies only marginally, but ethanol supplementation contributes to enzyme recovery due to activation of heat shock response Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
additional information expression in nonproliferating tissue Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 2'-deoxycytidine
-
Homo sapiens ADP + 2'-deoxycytidine 5'-phosphate
-
ir
ATP + 2'-deoxythymidine
-
Homo sapiens ADP + 2'-deoxythymidine 5'-phosphate
-
ir
ATP + 2'-deoxyuridine
-
Homo sapiens ADP + 2'-deoxyuridine 5'-phosphate
-
ir

Subunits

Subunits Comment Organism
dimer enzyme appears as dimer and tetramer Homo sapiens
More structure modeling Homo sapiens
tetramer enzyme appears as dimer and tetramer Homo sapiens

Synonyms

Synonyms Comment Organism
2'-deoxythymidine kinase
-
Homo sapiens
More the enzyme belongs to the thymidine kinase 2, i.e. TK2, family of enzymes Homo sapiens
thymidine kinase 2
-
Homo sapiens
TK2
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Homo sapiens

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 37 highest activity within this temperature range at 37°C Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
Homo sapiens