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Literature summary for 2.7.1.105 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)

Cloned (Comment) Organism
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Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
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

Inhibitors

Inhibitors Comment Organism Structure
additional information phosphorylation by cAMP-dependent protein kinase causes inactivation Escherichia coli
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

Organism UniProt Comment Textmining
Escherichia coli
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-
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Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation site: Ser-32 Rattus norvegicus
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
phosphoprotein phosphorylation by cAMP-dependent protein kinase causes inactivation Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
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
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

Source Tissue

Source Tissue Comment Organism Textmining
liver
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Rattus norvegicus
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skeletal muscle
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Rattus norvegicus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + beta-D-fructose 6-phosphate
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Escherichia coli ADP + beta-D-fructose 2,6-bisphosphate
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r
ATP + beta-D-fructose 6-phosphate
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Rattus norvegicus ADP + beta-D-fructose 2,6-bisphosphate
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r
additional information also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46) Escherichia coli ?
-
?
additional information also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46) Rattus norvegicus ?
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
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