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Literature summary extracted from

  • Kandeel, M.; Kitade, Y.
    The substrate binding preferences of Plasmodium thymidylate kinase (2011), Biol. Pharm. Bull., 34, 173-176.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.9 expressed in Escherichia coli Plasmodium falciparum

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.9 Plasmodium falciparum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.4.9 TALON metal affinity resin column chromatography Plasmodium falciparum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.9 ATP + dGMP dGMP is unable to displace TMP from its binding site Plasmodium falciparum ADP + dGDP
-
r
2.7.4.9 ATP + TMP TMP is able to partially displace dGMP from the binding site Plasmodium falciparum ADP + TDP
-
r

Synonyms

EC Number Synonyms Comment Organism
2.7.4.9 ATP: TMP phosphotransferase
-
Plasmodium falciparum
2.7.4.9 deoxythymidine monophosphate kinase
-
Plasmodium falciparum
2.7.4.9 dTMP kinase
-
Plasmodium falciparum
2.7.4.9 thymidylate kinase
-
Plasmodium falciparum
2.7.4.9 TMPK
-
Plasmodium falciparum

General Information

EC Number General Information Comment Organism
2.7.4.9 physiological function thymidylate kinase is a key enzyme in the control of nucleotide metabolism and synthesis of DNA Plasmodium falciparum