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Literature summary for 2.7.4.8 extracted from
- Binding dynamics and energetic insight into the molecular forces driving nucleotide binding by guanylate kinase (2011), J. Mol. Recognit., 24, 322-332.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli JM109 cells | Plasmodium falciparum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Plasmodium falciparum | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| TALON metal affinity resin column chromatography | Plasmodium falciparum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | - |
? |  |
| ATP + GMP | - |
Plasmodium falciparum | ADP + GDP | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ATP: GMP phosphotransferase | - |
Plasmodium falciparum |
| guanosine monophosphate kinase | - |
Plasmodium falciparum |
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Release 2023.1 (January 2023)
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