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Literature summary extracted from

  • Kandeel, M.; Kitade, Y.
    Binding dynamics and energetic insight into the molecular forces driving nucleotide binding by guanylate kinase (2011), J. Mol. Recognit., 24, 322-332.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.8 expressed in Escherichia coli JM109 cells Plasmodium falciparum

Organism

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

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.8 ATP + dGMP dGMP is a poor substrate, the Kcat for dGMP is about 22fold lower than that observed for GMP. The value of kcat/Km for dGMP is at least 70fold lower than that of GMP Plasmodium falciparum ADP + dGDP
-
?
2.7.4.8 ATP + GMP
-
Plasmodium falciparum ADP + GDP
-
?

Synonyms

EC Number Synonyms Comment Organism
2.7.4.8 ATP: GMP phosphotransferase
-
Plasmodium falciparum
2.7.4.8 guanosine monophosphate kinase
-
Plasmodium falciparum