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Literature summary extracted from
- Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography (1995), Biochemistry, 34, 4307-4315.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.1.3.11 | crystal structure of the enzyme complexed with AMP, the substrate analogue 2,5-anhydro-D-glucitol 1,6-diphosphosphate and Mn2+ | Sus scrofa |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.3.11 | AMP | structural aspects of the allosteric inhibition | Sus scrofa |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.3.11 | Sus scrofa | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.1.3.11 | kidney | - |
Sus scrofa | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.11 | D-fructose 1,6-diphosphate + H2O | - |
Sus scrofa | D-fructose 6-phosphate + phosphate | - |
? | |
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