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homodimer
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determined by circular dichroismand gel filtration, subunits consist of a large domain and an additional beta-sheet that provides the interfacial contacts between the subunits, creating a beta-barrel flattened-like structure with the adjacent subunits beta-sheet, Pfk-2 undergoes a cooperative unfolding/dissociation process with the accumulation of an expanded and unstructured monomeric intermediate with a marginal stability and a large solvent accessibility with respect to the native dimer
monomer
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C238-pyrene maleimide modified enzyme in absence of MgATP2-
?
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x * 61000, SDS-PAGE
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x * 58000, long isozyme variants H1-PFK2, H2-PFK2, and H4-PFK2, x * 54000, short isozyme variant H3-PFK2
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x * 72000, isozyme Tb2, about, sequence calculation, x * 54000, isozyme Tb3, about, sequence calculation, x * 79000, isozyme Tb4, about, sequence calculation
dimer
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dimer
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2 * 49000, SDS-PAGE
dimer
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2 * 120000, SDS-PAGE
dimer
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2 * 52000, SDS-PAGE
dimer
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2 * 53000, SDS-PAGE, with a minor constituent of MW 54000
dimer
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wild-type enzyme in presence of MgATP2-, and C238-pyrene maleimide modified enzyme in presence of beta-D-fructose 6-phosphate and ATP4-
dimer
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the unfolding pathways of the dimeric (free or fructose-6-phosphate-bound) and tetrameric (MgATP-bound) forms of Pfk-2 are characterized through changes in enzymatic activity and structural properties by intrinsic fluorescence, circular dichroism, 8-anilino-1-naphthalene sulfonic acid binding, gel filtration, and dynamic light scattering measurements
dimer
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homodimer, oligomerization state necessary for catalysis and stability, presence of MgATP favors the tetrameric form of the enzyme
dimer
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2 * 54000, SDS-PAGE
dimer
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2 * 58000, SDS-PAGE
dimer
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2 * 53000, SDS-PAGE
dimer
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2 * 55800, liver isoenzyme, SDS-PAGE
dimer
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2 * 53900, muscle-type isozyme, SDS-PAGE
dimer
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2 * 58000, SDS-PAGE
dimer
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2 * 55000, SDS-PAGE
dimer
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2 * 54760, calculated from amino acid sequence
dimer
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2 * 55000, high speed sedimentation equilibrium in 6 M guanidinium chloride, amino acid sequence
dimer
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2 * 54000, SDS-PAGE, amino acid sequence
dimer
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2 * 54000, SDS-PAGE
dimer
2 * 60000, recombinant Tb1, SDS-PAGE, 2 * 111000, isozyme Tb1, about, sequence calculation
tetramer
4 * 83000
tetramer
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wild-type enzyme in absence of ligands, and C238-pyrene maleimide modified enzyme in presence of MgATP2-
tetramer
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the unfolding pathways of the dimeric (free or fructose-6-ühosphate-bound) and tetrameric (MgATP-bound) forms of Pfk-2 are characterized through changes in enzymatic activity and structural properties by intrinsic fluorescence, circular dichroism, 8-anilino-1-naphthalene sulfonic acid binding, gel filtration, and dynamic light scattering measurements
tetramer
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4 * 90000, H-form, SDS-PAGE
tetramer
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4 * 90000, H-form, SDS-PAGE
tetramer
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4 * 90000, H-form, SDS-PAGE
tetramer
4 * 90800, SDS-PAGE
additional information
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two isozymes: 58000 Da and 54000 Da, SDS-Page
additional information
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two isozymes: 58000 Da and 54000 Da, SDS-Page
additional information
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two isozymes: 58000 Da and 54000 Da, SDS-Page
additional information
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oligomeric state of the enzyme plays a role in enzyme activity and regulation, alterations occur via binding of MgATP2- which mediates dimer-dimer interactions, the dimeric state of the enzyme is critical for stability and activity of the enzyme, Cys-295 plays a role in subunit interactions, overview
additional information
domain organization of isozyme PFKFB1 tissue variants, overview
additional information
domain organization of isozyme PFKFB1 tissue variants, overview
additional information
domain organization of isozyme PFKFB1 tissue variants, overview
additional information
domain organization of isozyme PFKFB1 tissue variants, overview
additional information
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additional information
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additional information
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two isozymes: 55000 Da and 52000 Da
additional information
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
additional information
bifunctional enzyme domain structure, the bifunctional enzyme possesses a 6-phosphofructo-2-kinase and a fructose-2,6-bisphosphatase domain, as well as ankyrin-motif repeats, overview
additional information
bifunctional enzyme domain structure, the bifunctional enzyme possesses a 6-phosphofructo-2-kinase and a fructose-2,6-bisphosphatase domain, as well as ankyrin-motif repeats, overview
additional information
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bifunctional enzyme domain structure, the bifunctional enzyme possesses a 6-phosphofructo-2-kinase and a fructose-2,6-bisphosphatase domain, as well as ankyrin-motif repeats, overview