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Literature summary for 2.7.1.21 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)

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

Protein Variants

Protein Variants Comment Organism
V106A site-directed mutagenesis, mutant is similar to the wild-type enzyme in size, conformation and polarity, unaltered activity and oligomerization pattern Homo sapiens
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
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
V106I site-directed mutagenesis, mutant is similar to the wild-type enzyme in size, conformation and polarity, unaltered activity and oligomerization pattern Homo sapiens
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
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
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
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
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]

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

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Homo sapiens

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
lymphocyte
-
Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
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)

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

Subunits

Subunits Comment Organism
? x * 24000, about, SDS-PAGE Homo sapiens
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

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

pH Optimum

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

Cofactor

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