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Literature summary for 2.7.1.105 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)

Cloned (Comment) Organism
expressed in Escherichia coli Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Inhibitors Comment Organism Structure
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

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
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)

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

Subunits

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

Synonyms

Synonyms Comment Organism
Pfk-2
-
Escherichia coli