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Literature summary extracted from

  • Baez, M.; Rodriguez, P.H.; Babul, J.; Guixe, V.
    Structural and functional roles of Cys-238 and Cys-295 in Escherichia coli phosphofructokinase-2 (2003), Biochem. J., 376, 277-283.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.105 pyrene maleimide incorporation of 2 mol per mol of enzyme subunit, modifiying Cys-238 and Cys-295, leads to rapid inactivation, MgATP2- protects Cys295, modification of Cys238 does not abolish activity Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.105 additional information
-
 additional information kinetics of native and pyrene maleimide modified enzyme Escherichia coli
2.7.1.105 0.042
-
 MgATP2- native enzyme Escherichia coli
2.7.1.105 0.044
-
 MgATP2- C238-pyrene maleimide modified enzyme Escherichia coli
2.7.1.105 0.058
-
 beta-D-fructose 6-phosphate native enzyme Escherichia coli
2.7.1.105 0.063
-
 beta-D-fructose 6-phosphate C238-pyrene maleimide modified enzyme Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.105 Mg2+ as MgATP2- 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
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.105 ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate ordered bi bi mechanism, structural and functional roles of Cys-238 and Cys-295 Escherichia coli
a

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 MgATP2- + beta-D-fructose 6-phosphate
-
 Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.105 dimer wild-type enzyme in presence of MgATP2-, and C238-pyrene maleimide modified enzyme in presence of beta-D-fructose 6-phosphate and ATP4- Escherichia coli
2.7.1.105 monomer C238-pyrene maleimide modified enzyme in absence of MgATP2- Escherichia coli
2.7.1.105 tetramer wild-type enzyme in absence of ligands, and C238-pyrene maleimide modified enzyme in presence of MgATP2- Escherichia coli

Synonyms

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.1.105 9240
-
 MgATP2- native enzyme Escherichia coli
2.7.1.105 9240
-
 beta-D-fructose 6-phosphate native enzyme Escherichia coli
2.7.1.105 9320
-
 MgATP2- C238-pyrene maleimide modified enzyme Escherichia coli
2.7.1.105 9320
-
 beta-D-fructose 6-phosphate C238-pyrene maleimide modified enzyme Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.105 ATP as MgATP2- Escherichia coli