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Binding of manganese to phosphofructokinase from yeast. Paper-3295263.
Binding of fructose 2,6-bisphosphate to yeast phosphofructokinase. Paper-6010568.
Rapid purification and crystallization of yeast phosphofructokinase. Paper-3948872.
Kinetic effects of fructose-1,6-bisphosphate on yeast phosphofructokinase. Paper-5150603.
Stimulation of yeast phosphofructokinase activity by fructose 2,6-bisphosphate. Paper-3950497.
The significance of phosphofructokinase to the regulation of carbohydrate metabolism. Paper-2447932.
Binding of Fru-2,6-P2 to yeast phosphofructokinase was investigated by ultrafiltration technique. Paper-6010568.
Yeast phosphofructokinase is known to be effectively activated by fructose-2,6-bisphosphate and AMP. Paper-5150603.
Small-angle x-ray scattering studies on the quaternary structure of phosphofructokinase from baker's yeast. Paper-3041476.
Allosteric regulation of yeast phosphofructokinase. Correlation between equilibrium binding, spectroscopic and kinetic data. Paper-3294158.
Since the molecular weight of phosphofructokinase does not change, these findings must reflect conformational changes in the enzyme molecule. Paper-3388359.
Biochemical and small-angle X-ray scattering (SAXS) studies had indicated that Pfk1 underwent a large conformational change upon Mg-ATP binding. Paper-13287917.
Plasmids containing the information of one or the other gene were identified by back-transformation into pfk single mutants ( pfk1 PFK2, PFK1 pfk2). Paper-5405835.
The two types of subunits alpha and beta constitutive of yeast phosphofructokinase have been separated by ion-exchange chromatography under denaturating conditions. Paper-4239356.
Inorganic phosphate augments the sensitivity of phosphofructokinase to the activators AMP and fructose 2,6-bisphosphate and increases the respective maximum activities. Paper-4765927.
The glycolytic oscillator, mainly studied in yeast, is described with respect to its overall dynamic and biochemical properties and the kinetics of its master enzyme phosphofructokinase. Paper-3417761.
Mammalian studies revealed complete loss of binding between the COOH terminus of a4 containing the G-to-R mutant and PFK-1, without affecting PFK-1's catalytic activity. Paper-13029008.
With the exception of phosphofructokinase and pyruvate decarboxylase in the industrial strain, no clear-cut correlation between the activities of glycolytic enzymes and the fermentative capacity was found. Paper-15011421.
In the absence of positive effectors, the maximum activity of the cross-linked enzyme corresponds to the respective values of native phosphofructokinase when activated by AMP or by fructose 2,6-bisphosphate. Paper-70588.
AMP deaminase reaction as a control system of glycolysis in yeast. Role of ammonium ion in the interaction of phosphofructokinase and pyruvate kinase activity with the adenylate energy charge. Paper-4827211.
The results agree with the predictions of an allosteric model for phosphofructokinase (EC 2.7.1.11; ATP:D-fructose-6-phosphate 1-phosphotransferase), which is the enzyme responsible for periodic operation of glycolysis. Paper-2320356.
Two strictly conserved residues belonging to an acidic surface loop of class II aldolases, are a potential site for electrostatic interaction with the positively charged regions close to the active site in phosphofructokinase. Paper-8765221.
However, severe (78%) loss of proton transport but less decrease in ATPase activity (36%) were observed in mutant vacuoles, suggesting a requirement for the a-subunit/ PFK-1 binding to couple these two functions. Paper-13029008.
The system was evaluated by testing known interacting proteins: labelling of the phosphofructokinase subunits, Pfk1p and Pfk2p, with N- and C-terminal EGFP fragments, respectively, resulted in green fluorescence in the cytoplasm. Paper-14307973.
The role of ammonium ion and AMP deaminase (EC 3.5.4.6) reaction in the activation of phosphofructokinase (EC 2.7.1.11) and pyruvate kinase (EC 2.7.1.40) by the decrease in the adenylate energy charge was investigated using permeabilized yeast cells. Paper-4827211.
At saturating levels of AMP and of fructose 2,6-bisphosphate, nearly identical affinities with respect to fructose 6-phosphate are found, ranging between the Km values of native phosphofructokinase activated by AMP and by fructose 2,6-bisphosphate. Paper-70588.
The results suggest that the allosteric regulation of yeast phosphofructokinase is mainly related to conformational changes controlled by fructose 6-phosphate while the ATP affinity at the catalytic site of the enzyme remains essentially unaffected. Paper-70588.
A third control regime in which phosphofructokinase exerted dominant glycolytic flux control was also found, but it appeared to be physiologically unreachable by this model, and all realistically obtainable flux control regimes featured hexose transport as a step involving high flux control. Paper-9534618.
These accession numbers are used for gene PFK1: .
PFK1 is a homologue of phosphofructokinase (hypothetical protein) from Caenorhabditis elegans.
PFK1 is a homologue of PFKP (phosphofructokinase, platelet) from Homo sapiens.
PFK1 is a homologue of PFKP (phosphofructokinase, platelet) from Pan troglodytes.
PFK1 is a homologue of PFKP (phosphofructokinase, platelet) from Canis lupus familiaris.
PFK1 is a homologue of PFKP (phosphofructokinase, platelet) from Bos taurus.
PFK1 is a homologue of Pfkp (phosphofructokinase, platelet) from Mus musculus.
PFK1 is a homologue of Pfkp (phosphofructokinase, platelet) from Rattus norvegicus.
PFK1 is a homologue of Pfk (Phosphofructokinase) from Drosophila melanogaster.
PFK1 is a homologue of LOC561416 (6-phosphofructokinase type C-like) from Danio rerio.
PFK1 is a homologue of LOC560944 (6-phosphofructokinase type C-like) from Danio rerio.
PFK1 is a homologue of KLLA0A05544g (hypothetical protein) from Kluyveromyces lactis NRRL Y-1140.
PFK1 is a homologue of AGOS_AEL208W (AEL208Wp) from Ashbya gossypii ATCC 10895.
PFK1 is a homologue of AgaP_AGAP007642 (AGAP007642-PA) from Anopheles gambiae str. PEST.
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iHOP - Information Hyperlinked over Proteins .
Concept & Implementation by Robert Hoffmann.