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Literature summary for 2.7.1.105 extracted from

  • Langer, S.; Okar, D.A.; Schultz, J.; Lenzen, S.; Baltrusch, S.
    Dimer interface rearrangement of the 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase rat liver isoenzyme by cAMP-dependent Ser-32 phosphorylation (2012), FEBS Lett., 586, 1419-1425.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
S32A/H258A mutant unable to be phosphorylated Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P07953 bifunctional 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein forskolin induces a 40% increase in phosphorylation at residue Ser32. The enzyme dimer favors binding of monomers in the same Ser32 phosphorylation state in living cells. Phosphorylation at Ser32 may tighten the liver enzyme dimer complex Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
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Rattus norvegicus
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Subunits

Subunits Comment Organism
More the enzyme dimer favors binding of monomers in the same Ser32 phosphorylation state in living cells. Phosphorylation at Ser32 may tighten the liver enzyme dimer complex Rattus norvegicus

Synonyms

Synonyms Comment Organism
PFKFB1
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Rattus norvegicus