Search results for "Phosphofructokinases"

showing 2 items of 2 documents

Fructose-1,6-Bisphosphate Protects Hippocampal Rat Slices from NMDA Excitotoxicity

2019

Effects of fructose 1,6-bisphosphate (F-1,6-P2) towards N-methyl-d-aspartate NMDA excitotoxicity were evaluated in rat organotypic hippocampal brain slice cultures (OHSC) challenged for 3 h with 30 &mu

Fructose 16-bisphosphateExcitotoxicityFructose-bisphosphate aldolaseorganotypic hippocampal brainslice culturesmedicine.disease_causeHippocampuslcsh:Chemistrychemistry.chemical_compoundenergymetabolismFructose-Bisphosphate Aldolaseenergy metabolismfructose-16-bisphosphatelcsh:QH301-705.5Spectroscopy<i>N</i>-methyl-<span style="font-variant: small-caps">d</span>-aspartatebiologyChemistryorganotypic hippocampal brain slice culturesGlyceraldehyde-3-Phosphate DehydrogenasesGeneral MedicineComputer Science ApplicationsFructose-BisphosphataseNeuroprotective AgentsNMDA receptorexcitotoxicityPhosphofructokinaseN-methyl-d-aspartatemedicine.medical_specialtyN-MethylaspartateFructose 16-bisphosphataseCatalysisArticleInorganic ChemistryNecrosisInternal medicinemitochondrial dysfunctionmedicineAnimalsPhysical and Theoretical ChemistryRats WistarMolecular BiologySettore BIO/10 - BIOCHIMICAOrganic ChemistryAldolase AMetabolismPurine NucleosidesRatsEndocrinologylcsh:Biology (General)lcsh:QD1-999Phosphofructokinases6-bisphosphatebiology.proteinfructose-1; 6-bisphosphate; N-methyl-d-aspartate; excitotoxicity; energymetabolism; mitochondrial dysfunction; organotypic hippocampal brainslice culturesfructose-1
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Studying the phosphoryl transfer mechanism of the E. coli phosphofructokinase-2: from X-ray structure to quantum mechanics/molecular mechanics simula…

2019

Phosphofructokinases (Pfks) catalyze the ATP-dependent phosphorylation of fructose-6-phosphate (F6P) and they are regulated in a wide variety of organisms. Although numerous aspects of the kinetics and regulation have been characterized for Pfks, the knowledge about the mechanism of the phosphoryl transfer reaction and the transition state lags behind. In this work, we describe the X-ray crystal structure of the homodimeric Pfk-2 from E. coli, which contains products in one site and reactants in the other, as well as an additional ATP molecule in the inhibitory allosteric site adjacent to the reactants. This complex was previously predicted when studying the kinetic mechanism of ATP inhibit…

Reaction mechanism010405 organic chemistryChemistryMetaphosphateKineticsAllosteric regulationGeneral Chemistry010402 general chemistry01 natural sciencesMolecular mechanics0104 chemical sciencesMolecular dynamicschemistry.chemical_compoundBACTÉRIAS GRAM-NEGATIVASQuantum mechanicsMoleculePhosphofructokinasesChemical Science
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