Any feedback?
Literature summary for 2.7.1.105 extracted from
- Chemical modification of SH groups of E. coli phosphofructokinase-2 induces subunit dissociation: monomers are inactive but preserve ligand binding properties (2000), Arch. Biochem. Biophys., 376, 313-319.
Inhibitors
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Posttranslational Modification
| 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 and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + beta-D-fructose 6-phosphate | - |
Escherichia coli | ADP + beta-D-fructose 2,6-bisphosphate | - |
? | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
