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Literature summary for 2.7.1.105 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
Search for more literature for 2.7.1.105

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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
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
L148N inactive mutant enzyme Rattus norvegicus
L168A inactive mutant enzyme Rattus norvegicus
L168R mutant enzyme shows 0.2% of wild-type activity Rattus norvegicus

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
testis
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

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

Turnover Number [1/s]

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