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Literature summary extracted from

  • Cabrera, R.; Ambrosio, A.L.; Garratt, R.C.; Guixe, V.; Babul, J.
    Crystallographic Structure of Phosphofructokinase-2 from Escherichia coli in Complex with Two ATP Molecules. Implications for Substrate Inhibition (2008), J. Mol. Biol., 383, 588-602.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.105 expressed in Escherichia coli Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.105 oligomeric state observed in the crystal is tetrameric, structural elements involved in the binding of the substrate and allosteric ATPs are also participating in the dimer-dimer interface, data collection parameters and structure refinement statistics Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.105 MgATP inhibited by, structure determination reveals substrate inhibition due to sequential binding of two MgATP molecules per subunit, the first at the usual site occupied by the nucleotide in homologous enzymes and the second at the allosteric site, making a number of direct and Mg-mediated interactions with the first, two configurations observed for the second MgATP, one of which involves interactions with Tyr-23 from the adjacent subunit in the dimer and the other making an unusual non-Watson-Crick base pairing with the adenine in the substrate ATP Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.105 Mg2+ required for activity, MgATP is the active substrate Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.105 66000
-
 native protein, SDS-PAGE Escherichia coli

Organism

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.1.105 additional information
-
 monomer structure and structural features of intersubunit interactions, interactions with ligands at the active site, structure determination in its inhibited tetrameric form, with each subunit bound to two ATP molecules and two Mg ions, allosteric site reported for ATP, analogous structural features in the 6-phosphofructokinases from Escherichia coli compared Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.105 additional information mechanism of enzyme inhibition by ATP analyzed by structure determination Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.105 dimer homodimer, oligomerization state necessary for catalysis and stability, presence of MgATP favors the tetrameric form of the enzyme Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.7.1.105 Pfk-2
-
 Escherichia coli