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Literature summary for 3.1.3.46 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

Protein Variants

Protein Variants Comment Organism
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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, recombinant enzyme, liver and muscle isoform
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation by proteinkinase A at S32 results in reduced affinity for fructose-6-phosphate and stimulates bisphosphatase activity Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver isoform with proteinkinase A phosphorylation site Rattus norvegicus
-
muscle isoform lacks proteinkinase A phosphorylation site Rattus norvegicus
-