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Literature summary extracted from

  • Guixe, V.
    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.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.105 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

EC Number Organism UniProt Comment Textmining
2.7.1.105 Escherichia coli
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.1.105 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.105 ATP + beta-D-fructose 6-phosphate
-
 Escherichia coli ADP + beta-D-fructose 2,6-bisphosphate
-
 ?