EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.1.3.11 | AMP | study of allosteric inhibition, two classes of binding sites with two distinct affinities for AMP are possible | Sus scrofa |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.3.11 | additional information | - |
additional information | comparison of KM of wild-type and hybrid enzymes | Sus scrofa |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.3.11 | D-fructose 1,6-bisphosphate + H2O | Sus scrofa | enzyme is usually regarded as a regulatory enzyme of gluconeogenesis | D-fructose 6-phosphate + phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.3.11 | Sus scrofa | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.1.3.11 | additional information | construction of hybrids in which subunits have either their active or regulatory sited rendered non-functional by specific mutations | Sus scrofa |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.1.3.11 | kidney | - |
Sus scrofa | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.3.11 | D-fructose 1,6-bisphosphate + H2O | - |
Sus scrofa | D-fructose 6-phosphate + phosphate | - |
? | |
3.1.3.11 | D-fructose 1,6-bisphosphate + H2O | enzyme is usually regarded as a regulatory enzyme of gluconeogenesis | Sus scrofa | D-fructose 6-phosphate + phosphate | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.3.11 | additional information | - |
additional information | comparison of kcat of wild-type and hybrid enzymes | Sus scrofa |