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Literature summary extracted from

  • Kurland, I.J.; Chapman, B.; El-Maghrabi, M.R.
    N- and C-termini modulate the effects of pH and phosphorylation on hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (2000), Biochem. J., 347, 459-467.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.105
-
 Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.105 additional information effects of N- and C-terminal deletions of skeletal muscle and liver enzyme, e.g. ND4, ND7, ND12, ND23, CD30, comparison of the kinetic properties of deletion mutants Rattus norvegicus
3.1.3.46 additional information deletion of N- and C-terminal amino acids to define the catalytic core and the phosphorylation site of protein kinase A Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.105 additional information phosphorylation by cAMP-dependent protein kinase causes inactivation Escherichia coli
2.7.1.105 additional information loss of phosphorylation-dependent reduction of enzyme by deletion of the N-terminal residues of enzyme. The deletion of 7 N-terminal amino acids causes a 75% decrease in activity; phosphorylation site: Ser-32 Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.105 Escherichia coli
-
-
-
2.7.1.105 Rattus norvegicus
-
-
-
3.1.3.46 Rattus norvegicus
-
 bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, recombinant enzyme, liver and muscle isoform
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.1.105 phosphoprotein phosphorylation site: Ser-32 Rattus norvegicus
2.7.1.105 phosphoprotein loss of phosphorylation-dependent reduction of enzyme by deletion of the N-terminal residues of enzyme, The deletion of 7 N-terminal amino acids causes a 75% decrease in activity Rattus norvegicus
2.7.1.105 phosphoprotein phosphorylation by cAMP-dependent protein kinase causes inactivation Escherichia coli
3.1.3.46 phosphoprotein phosphorylation by proteinkinase A at S32 results in reduced affinity for fructose-6-phosphate and stimulates bisphosphatase activity Rattus norvegicus

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 bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46 Escherichia coli
a
2.7.1.105 ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46 Rattus norvegicus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.105 liver
-
 Rattus norvegicus
-
2.7.1.105 skeletal muscle
-
 Rattus norvegicus
-
3.1.3.46 liver isoform with proteinkinase A phosphorylation site Rattus norvegicus
-
3.1.3.46 muscle isoform lacks proteinkinase A phosphorylation site 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
-
 Escherichia coli ADP + beta-D-fructose 2,6-bisphosphate
-
 r
2.7.1.105 ATP + beta-D-fructose 6-phosphate
-
 Rattus norvegicus ADP + beta-D-fructose 2,6-bisphosphate
-
 r
2.7.1.105 additional information also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46) Escherichia coli ?
-
 ?
2.7.1.105 additional information also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46) Rattus norvegicus ?
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.105 additional information
-
 biphasic pH profile with two optima at pH 6.8 and 10.00 and a minimum at 8.5, comparison of pH optima of N- and C-deletion mutants of enzyme, comparison of kinetic properties of wild-type and deletion mutants at pH 6.8 and pH 8.2 Rattus norvegicus