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Literature summary extracted from

  • Kim, S.G.; Cavalier, M.; El-Magrabi, M.R.; Lee, Y.M.
    A direct substratesubstrate interaction found in the kinase domain of the bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (2007), J. Biol. Chem., 370, 14-26.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.105 sitting-drop, vapor-diffusion method, crystal structures of PFKFB3/beta,gamma-methylene-adenosine 5'-triphosphate/fructose-6-phosphate and PFKFB3/ADP/phosphoenolpyruvate complexes are determined to 2.7 A and 2.25 A resolution Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.105 A44G the Km values for ATP and fructose-6-phosphate of the mutant enzyme are decreased by approximately 20fold compared to wilde-type values Rattus norvegicus
2.7.1.105 A44V the Km values for ATP and fructose-6-phosphate of the mutant enzyme are decreased by 8fold and 20fold compared to wilde-type values Rattus norvegicus
2.7.1.105 L148N inactive mutant enzyme Rattus norvegicus
2.7.1.105 L168A inactive mutant enzyme Rattus norvegicus
2.7.1.105 L168R mutant enzyme shows 0.2% of wild-type activity Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.105 0.00087
-
 ATP mutant enzyme A44G Rattus norvegicus
2.7.1.105 0.0038
-
 beta-D-fructose 6-phosphate mutant enzyme A44G Rattus norvegicus
2.7.1.105 0.0102
-
 beta-D-fructose 6-phosphate wild-type enzyme Rattus norvegicus
2.7.1.105 0.0169
-
 ATP wild-type enzyme Rattus norvegicus
2.7.1.105 0.14
-
 ATP mutant enzyme A44V Rattus norvegicus
2.7.1.105 0.204
-
 beta-D-fructose 6-phosphate mutant enzyme A44V Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.105 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.105 testis
-
 Rattus norvegicus
-

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 site-directed mutant study and inhibition kinetics suggest that the reaction will be catalyzed most efficiently by the protein when the substrates bind to the active pocket in an ordered manner in which ATP binds first Rattus norvegicus ADP + beta-D-fructose 2,6-bisphosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.1.105 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase bifunctional enzyme Rattus norvegicus
2.7.1.105 PFKFB3
-
 Rattus norvegicus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.1.105 0.14
-
 ATP wild-type enzyme Rattus norvegicus
2.7.1.105 0.14
-
 beta-D-fructose 6-phosphate wild-type enzyme Rattus norvegicus
2.7.1.105 0.17
-
 ATP mutant enzyme A44V Rattus norvegicus
2.7.1.105 0.17
-
 beta-D-fructose 6-phosphate mutant enzyme A44V Rattus norvegicus
2.7.1.105 0.19
-
 ATP mutant enzyme A44G Rattus norvegicus
2.7.1.105 0.19
-
 beta-D-fructose 6-phosphate mutant enzyme A44G Rattus norvegicus