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Literature summary for 2.7.3.5 extracted from
- The structure of lombricine kinase: implications for phosphagen kinase conformational changes (2011), J. Biol. Chem., 286, 9338-9350.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli | Urechis caupo |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| substrate-free enzyme or in complex with ADP, vapor diffusion method, using 15 mM bis-Tris, 0.2 M NaNO3, 1 mM dithiothreitol, and 20% (w/v) PEG 3350MME, pH 6.8 | Urechis caupo |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Urechis caupo | Q8T6T7 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| DEAE column chromatography, ADP-agarose column chromatography, and Superdex 200 gel filtration | Urechis caupo |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + lombricine | - |
Urechis caupo | ADP + N-phospholombricine | - |
? |  |
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Release 2023.1 (January 2023)
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