Computer‐assisted simulations of phosphofructokinase‐1 kinetics using simplified velocity equations [PDF]
AbstractEquations useful for simulating the kinetic behavior of phosphofructokinase are presented. The equations, which are based on the concerted transition (symmetry) model for allosteric enzymes, account for substrate inhibition by MgATP, cooperative binding by F‐6‐P, activation by F‐2, 6‐P2, and deinhibition by AMP.
Harry Roy+3 more
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EGFR-Phosphorylated Platelet Isoform of Phosphofructokinase 1 Promotes PI3K Activation. [PDF]
EGFR activates phosphatidylinositide 3-kinase (PI3K), but the mechanism underlying this activation is not completely understood. We demonstrated here that EGFR activation resulted in lysine acetyltransferase 5 (KAT5)-mediated K395 acetylation of the platelet isoform of phosphofructokinase 1 (PFKP) and subsequent translocation of PFKP to the plasma ...
Lee JH+18 more
europepmc +5 more sources
Phosphofructokinase-1 subunit composition and activity in the skeletal muscle, liver, and brain of dogs. [PDF]
Phosphofructokinase-1 (EC:2.7.1.11, PFK-1) catalyzes the phosphorylation of fructose 6-phosphate to fructose 1,6-bisphosphate using adenosine triphosphate and is a key regulatory enzyme of glycolysis. Mammalian PFK-1 isozymes are composed of three kinds of subunits (PFK-M, -L, and -P), with different properties.
Kanai S+3 more
europepmc +5 more sources
Reversible High Affinity Inhibition of Phosphofructokinase-1 by Acyl-CoA [PDF]
The enzyme phosphofructokinase-1 (PFK-1) catalyzes the first committed step of glycolysis and is regulated by a complex array of allosteric effectors that integrate glycolytic flux with cellular bioenergetics. Here, we demonstrate the direct, potent, and reversible inhibition of purified rabbit muscle PFK-1 by low micromolar concentrations of long ...
Christopher M. Jenkins+3 more
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Effect of ammonium, sodium, and potassium ions on rabbit muscle phosphofructokinase-1 and adenylate kinase activities [PDF]
This report shows that 30 nM PFK-1 and 30 nM AK were both affected by the presence of NH(4)(+), Na(+), and K(+) salts but with opposite consequences. Low concentrations of PFK-1 lose about half of its activity as a result of dilution and become susceptible to further activity losses owing to the presence of monovalent salts.
Percy J. Russell+7 more
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Fructose utilization in Corynebacterium glutamicum starts with its uptake and concomitant phosphorylation via the phosphotransferase system (PTS) to yield intracellular fructose 1-phosphate, which enters glycolysis upon ATP-dependent phosphorylation to ...
Irene Krahn+11 more
doaj +1 more source
Structures of Human Phosphofructokinase-1 and Atomic Basis of Cancer-Associated Mutations [PDF]
Phosphofructokinase-1 (PFK1), the 'gatekeeper' of glycolysis, catalyses the committed step of the glycolytic pathway by converting fructose-6-phosphate to fructose-1,6-bisphosphate. Allosteric activation and inhibition of PFK1 by over ten metabolites and in response to hormonal signalling fine-tune glycolytic flux to meet energy requirements. Mutations
Bradley A. Webb+5 more
openalex +7 more sources
Key glycolytic enzyme activities of skeletal muscle are decreased under fed and fasted states in mice with knocked down levels of Shc proteins. [PDF]
Shc proteins interact with the insulin receptor, indicating a role in regulating glycolysis. To investigate this idea, the activities of key glycolytic regulatory enzymes and metabolites levels were measured in skeletal muscle from mice with low levels ...
Kevork Hagopian+4 more
doaj +1 more source
Role of the C‐terminal region in the allosteric properties of Escherichia coli phosphofructokinase‐1 [PDF]
In order to investigate the role of the carboxy‐terminal segment in the catalytic, regulatory, and structural properties of the major allosteric phosphofructokinase (ATP: D‐fructose‐6‐phosphate‐1‐phosphotransferase: EC 2.7.1.11) from Escherichia coli, the corresponding gene has been modified at either of two sites using oligonucleotide‐directed ...
Marie-Claude Serre, Jean‐Renaud Garel
openalex +5 more sources
Premature neonates are submitted to an early-life oxidative stress from parenteral nutrition, which is vitamin C (VC) deficient and induces low endogenous levels of glutathione.
Vitor Teixeira+2 more
doaj +1 more source