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Literature summary extracted from

  • Frederiksen, H.; Berenstein, D.; Munch-Petersen, B.
    Effect of valine 106 on structure-function relation of cytosolic human thymidine kinase. Kinetic properties and oligomerization pattern of nine substitution mutants of V106 (2004), Eur. J. Biochem., 271, 2248-2256.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.21 expression of wild-type and Val106 mutants in an enzyme-deficient Escherichia coli strain as GST-fusion proteins Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.21 V106A site-directed mutagenesis, mutant is similar to the wild-type enzyme in size, conformation and polarity, unaltered activity and oligomerization pattern Homo sapiens
2.7.1.21 V106G site-directed mutagenesis, mutant differs in size, conformation and polarity from the wild-type enzyme, reduced activity, permanent tetrameric form irrespective of the presence of ATP Homo sapiens
2.7.1.21 V106H site-directed mutagenesis, mutant differs in size, conformation and polarity from the wild-type enzyme, reduced activity, permanent tetrameric form irrespective of the presence of ATP Homo sapiens
2.7.1.21 V106I site-directed mutagenesis, mutant is similar to the wild-type enzyme in size, conformation and polarity, unaltered activity and oligomerization pattern Homo sapiens
2.7.1.21 V106K site-directed mutagenesis, mutant differs in size, conformation and polarity from the wild-type enzyme, reduced activity, permanent tetrameric form irrespective of the presence of ATP Homo sapiens
2.7.1.21 V106L site-directed mutagenesis, mutant differs in size, conformation and polarity from the wild-type enzyme, reduced activity, permanent tetrameric form irrespective of the presence of ATP Homo sapiens
2.7.1.21 V106M site-directed mutagenesis, mutant differs in size, conformation and polarity from the wild-type enzyme, reduced activity, permanent tetrameric form irrespective of the presence of ATP Homo sapiens
2.7.1.21 V106Q site-directed mutagenesis, mutant differs in size, conformation and polarity from the wild-type enzyme, reduced activity, permanent tetrameric form irrespective of the presence of ATP Homo sapiens
2.7.1.21 V106T site-directed mutagenesis, mutant is similar to the wild-type enzyme in size, conformation and polarity, unaltered activity and oligomerization pattern Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.21 additional information
-
 additional information kinetics of wild-type and mutant enzymes in absence or presence of ATP, overview Homo sapiens
2.7.1.21 0.0003
-
 thymidine pH 7.5, recombinant mutant V106H, in absence of ATP Homo sapiens
2.7.1.21 0.0003
-
 thymidine pH 7.5, recombinant mutants V106A and V106G, in presence of ATP Homo sapiens
2.7.1.21 0.0004
-
 thymidine pH 7.5, recombinant mutants V106L and V106G, in absence of ATP Homo sapiens
2.7.1.21 0.0004
-
 thymidine pH 7.5, recombinant mutants V106L, V106H and V106T, in presence of ATP Homo sapiens
2.7.1.21 0.0006
-
 thymidine pH 7.5, recombinant mutant V106M, in absence or presence of ATP Homo sapiens
2.7.1.21 0.0006
-
 thymidine pH 7.5, recombinant wild-type enzyme, in presence of ATP Homo sapiens
2.7.1.21 0.0007
-
 thymidine pH 7.5, recombinant mutant V106K, in absence of ATP Homo sapiens
2.7.1.21 0.0008
-
 thymidine pH 7.5, recombinant mutant V106Q, in absence or presence of ATP Homo sapiens
2.7.1.21 0.0009
-
 thymidine pH 7.5, recombinant mutant V106I, in presence of ATP Homo sapiens
2.7.1.21 0.0012
-
 thymidine pH 7.5, recombinant mutant V106K, in presence of ATP Homo sapiens
2.7.1.21 0.0127
-
 thymidine pH 7.5, recombinant mutant V106A, in absence of ATP Homo sapiens
2.7.1.21 0.0271
-
 thymidine pH 7.5, recombinant wild-type enzyme, in absence of ATP Homo sapiens
2.7.1.21 0.0294
-
 thymidine pH 7.5, recombinant mutant V106I, in absence of ATP Homo sapiens
2.7.1.21 0.043
-
 thymidine pH 7.5, recombinant mutant V106T, in absence of ATP Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.1.21 cytosol
-
 Homo sapiens 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.21 Mg2+
-
 Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.21 24000
-
 x * 24000, about, SDS-PAGE Homo sapiens
2.7.1.21 50000
-
 approximately, dimeric enzyme form Homo sapiens
2.7.1.21 100000
-
 approximately, tetrameric enzyme form Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.21 ATP + thymidine Homo sapiens
-
 ADP + thymidine 5'-phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.21 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.21 recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli by GST affinity chromatography, cleaving of the tag Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.21 lymphocyte
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.1.21 additional information
-
 activities of recombinant wild-type and mutant enzymes in dimeric or tetrameric form, i.e. in absence or presence of ATP, overview Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.21 ATP + thymidine
-
 Homo sapiens ADP + thymidine 5'-phosphate
-
 ?
2.7.1.21 ATP + thymidine enzyme contains the putative thymidine-binding motif FQRK Homo sapiens ADP + thymidine 5'-phosphate
-
 ?
2.7.1.21 additional information Val106 has effects on structure-function relation of the enzyme Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.21 ? x * 24000, about, SDS-PAGE Homo sapiens
2.7.1.21 More oligomerization patterns of wild-type and mutant enzymes, binding of ATP induces reversible transition from a dimer with low catalytic activity to a tetramer with high catalytic activity, Val106 is involved Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.7.1.21 More the enzyme belongs to the thymidine kinase 1, i.e. TK1, family of enzymes Homo sapiens
2.7.1.21 thymidine kinase 1
-
 Homo sapiens
2.7.1.21 TK1
-
 Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.21 7.5
-
 assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.21 ATP binding of ATP induces reversible transition from a dimer with low catalytic activiy to a tetramer with high catalytic activity Homo sapiens