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Literature summary extracted from

  • Zhu, Z.; Ling, S.; Yang, Q.H.; Li, L.
    Involvement of the chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase sequence His444-Arg-Glu-Arg in modulation of the bisphosphatase activity by its kinase domain (2001), Biochem. J., 357, 513-520.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.1.105 ATP the binding of ATP to the fructose 2,6-bisphosphatase domain of chicken liver 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase leads to activation of enzyme, but no activation of rat liver enzyme Gallus gallus
2.7.1.105 ATP the binding of ATP to the fructose 2,6-bisphosphatase domain of chicken liver 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase leads to activation of enzyme, but no activation of rat liver enzyme Rattus norvegicus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.105 expression in Escherichia coli Gallus gallus
2.7.1.105 expression in Escherichia coli Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.105 additional information
-
 Rattus norvegicus
2.7.1.105 additional information the chicken enzyme in which the C-termini tail were replaced with that of rat enzyme is not activated by ATP Gallus gallus
2.7.1.105 additional information a series of C-terminal deletion mutants are generated: 15, 20, 25 and 30 amino acids, the deletion of the C-terminal 25 or 30 residues of enzyme increases Km of beta-D-fructose 6-phosphate by approximately 2fold. The mutations E446A, H444A, H444K, H444E, R445E, R445L prove the importance of His444 and Arg445.The C-terminal region I involves in the activation of enzyme by ATP. Gallus gallus
2.7.1.105 R279A mutation eliminates both the binding of ATP to the bisphosphatase domain of the bifunctional enzyme and the activation of enzyme by ATP Gallus gallus
2.7.1.105 R359A mutation eliminates both the binding of ATP to the bisphosphatase domain of the bifunctional enzyme and the activation of enzyme by ATP Gallus gallus
3.1.3.46 H444A/R445A/R447A enhances catalytic rate of bisphosphatase activity and abrogates inhibition by kinase domain Gallus gallus
3.1.3.46 additional information truncation of the C-terminus by 25, but not by 20 amino acids enhances catalytic rate of bisphosphatase activity and abrogates inhibition by kinase domain Gallus gallus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.105 additional information phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme Gallus gallus
2.7.1.105 additional information phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.105 additional information
-
 additional information comparison of Km of wild-type and mutant enzyme Gallus gallus
2.7.1.105 additional information
-
 additional information comparison of Km of wild-type and mutant enzyme Rattus norvegicus
2.7.1.105 0.022
-
 beta-D-fructose 6-phosphate pH 7.5, 30°C, comparison of Km of wild-type, mutant and mutant phosphorylated enzyme Gallus gallus
2.7.1.105 0.11
-
 ATP pH 7.5, 30°C Gallus gallus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.105 Mg2+
-
 Rattus norvegicus
2.7.1.105 Mg2+ inhibition of enzyme at 2 mM, but no effect on activation by ATP Gallus gallus

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 Gallus gallus
-
 ADP + beta-D-fructose 2,6-bisphosphate
-
 ?
2.7.1.105 ATP + beta-D-fructose 6-phosphate Rattus norvegicus responsible for regulation of fructose 2,6-bisphosphate-concentration ADP + beta-D-fructose 2,6-bisphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.105 Gallus gallus
-
-
-
2.7.1.105 Rattus norvegicus
-
-
-
3.1.3.46 Gallus gallus
-
 bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.1.105 phosphoprotein phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme Gallus gallus
2.7.1.105 phosphoprotein phosphorylation by cAMP-dependent protein kinase causes inactivation of liver enzyme Rattus norvegicus
3.1.3.46 phosphoprotein phosphorylation by proteinkinase A activates bisphosphatase activity or abolishes inhibitory effect of kinase domain Gallus gallus

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 Rattus norvegicus
a
3.1.3.46 beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate mechanism, regulation Gallus gallus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.105 liver
-
 Gallus gallus
-
2.7.1.105 liver
-
 Rattus norvegicus
-
3.1.3.46 liver
-
 Gallus gallus
-

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
-
 Gallus gallus ADP + beta-D-fructose 2,6-bisphosphate
-
 ?
2.7.1.105 ATP + beta-D-fructose 6-phosphate
-
 Gallus gallus 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 ATP + beta-D-fructose 6-phosphate responsible for regulation of fructose 2,6-bisphosphate-concentration Rattus norvegicus ADP + beta-D-fructose 2,6-bisphosphate
-
 ?
2.7.1.105 additional information also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46) Gallus gallus ?
-
 ?
2.7.1.105 additional information also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46) Rattus norvegicus ?
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.105 30
-
 assay at Gallus gallus
2.7.1.105 30
-
 assay at Rattus norvegicus