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Literature summary extracted from

  • Baez, M.; Merino, F.; Astorga, G.; Babul, J.
    Uncoupling the MgATP-induced inhibition and aggregation of Escherichia coli phosphofructokinase-2 by C-terminal mutations (2008), FEBS Lett., 582, 1907-1912.
    View publication on PubMed

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.105 L307A site-directed mutagenesis, C-terminal point mutant, further mutants analyzed that reveal successive deletions of up to 10 residues at the C-terminal end Escherichia coli
2.7.1.105 Y306A site-directed mutagenesis, C-terminal point mutant, no dimer-tetramer conversion in presence of MgATP, inhibition pattern almost undistinguishable from the wild-type, conformational changes leading to allosteric inhibition can be uncoupled from tetramer formation at least in the Y306A mutant Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.105 MgATP2- allosteric inhibition Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.105 0.01
-
 MgATP2- C-terminal deletion mutant L307, 1 mM co-substrate Escherichia coli
2.7.1.105 0.0137
-
 MgATP2- Y306A, C-terminal point mutant, 1 mM co-substrate Escherichia coli
2.7.1.105 0.015
-
 MgATP2- wild-type, 1 mM co-substrate Escherichia coli
2.7.1.105 0.02
-
 beta-D-fructose 6-phosphate C-terminal deletion mutant D299, 1 mM co-substrate Escherichia coli
2.7.1.105 0.029
-
 beta-D-fructose 6-phosphate L307A, C-terminal point mutant, 1 mM co-substrate Escherichia coli
2.7.1.105 0.036
-
 beta-D-fructose 6-phosphate C-terminal deletion mutant A305, 1 mM co-substrate Escherichia coli
2.7.1.105 0.057
-
 beta-D-fructose 6-phosphate wild-type, 1 mM co-substrate, chosen in order avoid the effect of MgATP binding at the allosteric site to the binding of fructose-6-P to the catalytic site, that is observed above 1 mM MgATP Escherichia coli
2.7.1.105 0.06
-
 beta-D-fructose 6-phosphate C-terminal deletion mutant L307, 1 mM co-substrate Escherichia coli
2.7.1.105 0.062
-
 beta-D-fructose 6-phosphate Y306A, C-terminal point mutant, 1 mM co-substrate Escherichia coli
2.7.1.105 0.8
-
 MgATP2- C-terminal deletion mutant A305, 1 mM co-substrate Escherichia coli
2.7.1.105 0.88
-
 MgATP2- C-terminal deletion mutant Y306, 1 mM co-substrate Escherichia coli
2.7.1.105 0.954
-
 MgATP2- L307A, C-terminal point mutant, 1 mM co-substrate Escherichia coli
2.7.1.105 2
-
 MgATP2- C-terminal deletion mutant D299, 1 mM co-substrate Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.105 Mg2+ required for activity Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.105 gel filtration 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
-
 binding of MgATP to an allosteric site provokes inhibition and a dimer-tetramer conversion of the enzyme, mutant generation by successive deletions of up to 10 residues and point mutations at the C-terminal end, elevated KM values for MgATP that fails to show the dimer-tetramer conversion, Y306 required for the quaternary packing involved in the dimer-tetramer conversion, the following residue L307 is crucial for the ternary packing necessary for the catalytic MgATP-binding site, dimer-tetramer conversion can be uncoupled from the conformational changes that lead to the MgATP-induced allosteric inhibition 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
-
 ?
2.7.1.105 ATP + beta-D-fructose 6-phosphate activity determined spectrophotometrically by coupling the fructose-1,6-bisphosphate production to the oxidation of NADH Escherichia coli ADP + beta-D-fructose 2,6-bisphosphate
-
 ?
2.7.1.105 MgATP2- + beta-D-fructose 6-phosphate analysis of MgATP-induced tetramer formation Escherichia coli ?
-
 ?

Synonyms

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