Inhibitors | Comment | Organism | Structure |
---|---|---|---|
N-(1-pyrenil)maleimide | complete loss of catalytic activity, but modified enzyme is able to bind beta-D-fructose 6-phosphate, the presence of MgATP2- completely protects the enzyme activity, the modified enzyme elutes as a monomer | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
side-chain modification | specific modification by N-(1-pyrenyl)maleimide, the results demonstrate the presence of SH residue in the interface of enzyme subunits critical for interactions between them and that conformational changes occurring through dimers are essential for catalytic activity | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + beta-D-fructose 6-phosphate | - |
Escherichia coli | ADP + beta-D-fructose 2,6-bisphosphate | - |
? |