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Literature summary extracted from

  • Okazaki, R.; Kornerg, A.
    Deoxythymidine kinase of Escherichia coli. II. Kinetics and feedback control (1964), J. Biol. Chem., 239, 275-284.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.21 bromo-dUTP
-
Escherichia coli
2.7.1.21 dTTP 50-90% inhibition at 0.2-0.8 mM; competitive to thymidine Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.21 additional information
-
additional information
-
Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.21 Mg2+
-
Escherichia coli
2.7.1.21 Mn2+
-
Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.21 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.21 ATP + thymidine ATP can be substituted by GTP Escherichia coli ADP + dTMP
-
?
2.7.1.21 ATP + thymidine ATP can be substituted by dGTP Escherichia coli ADP + dTMP
-
?
2.7.1.21 ATP + thymidine requirement for high levels of ATP Escherichia coli ADP + dTMP
-
?
2.7.1.21 ATP + thymidine ATP can be substituted by dATP Escherichia coli ADP + dTMP
-
?
2.7.1.21 ATP + thymidine ATP can be substituted by CTP Escherichia coli ADP + dTMP
-
?
2.7.1.21 ATP + thymidine ATP can be substituted by ITP Escherichia coli ADP + dTMP
-
?