Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Sus scrofa |
Crystallization (Comment) | Organism |
---|---|
In presence of AMP, the enzyme crystallizes in the T-state and AMP displaces loop 52-72 from its engaged conformation and abolishes metal association with sites 2 and 3. In the absence of AMP, enzyme is in the R-state and loop 52-72 associates with the active site. Three metal-binding sites are occupied by Zn2+ and two of three metal sites by Mg2+. | Sus scrofa |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
AMP | allosteric inhibitor | Sus scrofa |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Sus scrofa | |
Zn2+ | - |
Sus scrofa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-fructose 1,6-diphosphate + H2O | Sus scrofa | enzyme is usually regarded as a regulatory enzyme of gluconeogenesis | D-fructose 6-phosphate + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sus scrofa | P00636 | - |
- |
Purification (Comment) | Organism |
---|---|
the recombinant enzyme | Sus scrofa |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-fructose 1,6-diphosphate + H2O | - |
Sus scrofa | D-fructose 6-phosphate + phosphate | - |
? | |
D-fructose 1,6-diphosphate + H2O | enzyme is usually regarded as a regulatory enzyme of gluconeogenesis | Sus scrofa | D-fructose 6-phosphate + phosphate | - |
? |