Fructose 1 6 Bisphosphate
Mostrando 1-12 de 210 artigos, teses e dissertações.
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1. Molecular And 3D-Structural Characterization Of Fructose-1,6-Bisphosphate Aldolase Derived From Metroxylon Sagu
ABSTRACT Fructose-1,6-bisphosphate aldolase (FBAld) is an enzyme that catalyzes the cleavage of D-fructose-1,6-phosphate (FBP) to D-glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP), and plays vital role in glycolysis and gluconeogenesis. However, molecular characterization and functional roles of FBAld remain unknown in sago palm. Here
Braz. arch. biol. technol.. Publicado em: 22/06/2017
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2. Investigation of adenosine endogenous increase decurrent of D-Frutose-1,6-difosfato administration, a glycolytic intermediate. / Investigação do aumento endógeno de adenosina decorrente da administração do intermediário glicolítico D-Frutose-1,6-difosfato
D-Fructose-1,6-bisphosphate (F1,6BP), a high-energy glycolytic pathway intermediate, is reported to have a many pharmacologically effect, but its underlying mechanism of action in inflammation is incompletely understood. In this study, the aim was to examine the function of F1,6BP on cytokines and adenosine. Then, the possible F1,6BP anti-inflammatory activi
Publicado em: 2009
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3. Utilização da frutose-1, 6-Bisfosfato como um protetor celular na preservação de fígados para transplante / Use of fructose-1,6-bisphosphate in cold storage solution for liver preservation
A solução de preservação da Universidade de Wisconsin (UW) é considerada a solução padrão para preservação de fígados, rins e pâncreas. A frutose-1,6-bisfosfato (FBP) é uma substância que apresenta efeito protetor do fígado contra injúrias provocadas por agentes químicos e ocorridas durante o período de isquemia-reperfusão. O objetivo dest
Publicado em: 2007
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4. Fructose 2,6-Bisphosphate Inhibition of Phosphoglucomutase 1
Fructose 2,6-bisphosphate inhibits phosphoglucomutase noncompetitively with respect to the cofactor glucose 1,6-bisphosphate. Previous studies from our laboratory had shown that phosphoglucomutase was activated by fructose 2,6-bisphosphate in the absence of added glucose 1,6-bisphosphate. The fructose 2,6-bisphosphate activation previously reported was due t
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5. Effects of Fructose 2,6-Bisphosphate on Phosphoglucomutase from Plants 1
Fructose 2,6-bisphosphate affects phosphoglucomutase from plant and animal sources in a similar way. As previously found with rabbit muscle phosphoglucomutase, fructose 2,6-bisphosphate cannot substitute for glucose 1,6-bisphosphate as a cofactor in the reaction catalyzed by phosphoglucomutase from potato tubers, pea seeds, and string-beans. In the presence
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6. Control of liver 6-phosphofructokinase by fructose 2,6-bisphosphate and other effectors.
Rat liver 6-phosphofructokinase (ATP-D-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) was partially purified free of interfering enzymes by a rapid procedure. Fructose 2,6-bisphosphate, at micromolar concentrations, greatly stimulated the enzyme by increasing its affinity for fructose 6-phosphate and relieving the inhibition by ATP. Its action was s
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7. Fructose 1,6-bisphosphate aldolase activity is essential for synthesis of alginate from glucose by Pseudomonas aeruginosa.
We have isolated a mutant of Pseudomonas aeruginosa deficient in fructose 1,6-bisphosphate aldolase activity. This mutant, similar to the mutants deficient in any of the Entner-Doudoroff pathway enzymes, does not allow appreciable alginate formation from glucose and gluconate, but allows alginate synthesis from mannitol and fructose. This suggests that gluco
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8. Assessment of a futile cycle involving reconversion of fructose 6-phosphate to fructose 1,6-bisphosphate during gluconeogenic growth of Escherichia coli.
In gluconeogenesis, fructose 6-phosphate is formed from fructose 1,6-bisphosphate, and if fructose 1,6-bisphosphate were reformed by the phosphofructokinase reaction there would be a "gluconeogenic futile cycle." We assessed the extent of this cycling in Escherichia coli growing on glycerol 3-phosphate, using a medium containing 32Pi. Fructose 1,6-bisphospha
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9. Elucidating the biosynthesis of 2-carboxyarabinitol 1-phosphate through reduced expression of chloroplastic fructose 1,6-bisphosphate phosphatase and radiotracer studies with 14CO2
2-Carboxyarabinitol 1-phosphate limits photosynthetic CO2 assimilation at low light because it is a potent, naturally occurring inhibitor of ribulose 1,5-bisphosphate carboxylase/oxygenase. Evidence is presented that this inhibitor is derived from chloroplastic fructose 1,6-bisphosphate. First, transgenic plants containing decreased amounts of chloroplastic
The National Academy of Sciences.
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10. Unequivocal demonstration of fructose-1,6-bisphosphatase in mammalian brain.
Fructose-1,6-bisphosphatase (D-fructose-1,6-bisphosphate 1-phosphohydrolase; EC 3.1.3.11) has been found in rat brain and identified unequivocally. The enzyme has been purified to 95% homogeneity by standard procedures, including adsorption to a phosphocellulose column followed by elution with substrate. The purified enzyme exhibits a broad optimum above pH
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11. Uridine diphosphate glucose breakdown is mediated by a unique enzyme activated by fructose 2,6-bisphosphate in Solanum tuberosum
In the presence of inorganic phosphate, uridine 5′-diphosphate glucose (UDPG) is specifically hydrolyzed to glucose 1-phosphate and UDP by a unique enzyme, UDPG phosphorylase. The activity of the enzyme was maximally stimulated by fructose 2,6-bisphosphate, a regulatory metabolite recently discovered in both plants and animals, and by 2-phosphoglyceric aci
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12. Activities synthesizing and degrading fructose 2,6-bisphosphate in spinach leaves reside on different proteins
Activities catalyzing the synthesis and degradation of fructose 2,6-bisphosphate—6-phosphofructo-2-kinase (ATP:D-fructose-6-phosphate-2-phosphotransferase, EC 2.7.1.105) and fructose-2,6-bisphosphatase (D-fructose-2,6-bisphosphate 2-phosphohydrolase, EC 3.1.3.46)—were isolated from spinach leaves by an improved procedure and separated on the basis of bot