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Fructose-bisphosphatase

CHYMOTRYPSIN FRUCTOSE-2,6-BISPHOSPHATASE ILLUSTRATE COVALENT CATALYSIS... [Pg.52]

Fructose-2,6-bisphosphatase, a regulatory enzyme of gluconeogenesis (Chapter 19), catalyzes the hydrolytic release of the phosphate on carbon 2 of fructose 2,6-bisphosphate. Figure 7-8 illustrates the roles of seven active site residues. Catalysis involves a catalytic triad of one Glu and two His residues and a covalent phos-phohistidyl intermediate. [Pg.54]

Figure 19-3. Control of glycolysis and gluconeoge-nesis in the liver by fructose 2,6-bisphosphate and the bifunctional enzyme PFK-2/F-2,6-Pase (6-phospho-fructo-2-kinase/fructose-2,6-bisphosphatase). (PFK-1, phosphofructokinase-1 [6-phosphofructo-1 -kinase] ... Figure 19-3. Control of glycolysis and gluconeoge-nesis in the liver by fructose 2,6-bisphosphate and the bifunctional enzyme PFK-2/F-2,6-Pase (6-phospho-fructo-2-kinase/fructose-2,6-bisphosphatase). (PFK-1, phosphofructokinase-1 [6-phosphofructo-1 -kinase] ...
There s also a fructose 2,6-bisphosphatase that hydrolyzes fructose 2,6-bisphosphate see if you can figure out what happens to the phosphatase activity in liver and muscle when the enzyme is phosphorylated. As a check to your answer, you might recall the PFK-2 and fructose 2,6-bisphosphatase are one and the same protein. Phosphorylation-dephosphorylation actually shifts the activity of this single protein between the kinase and the phosphatase. So the answer you get should be opposite to the one we got earlier. [Pg.217]

SORBITOL DEHYDROGENASE FRUCTOSE-1,6-BISPHOSPHATASE FRUCTOSE-2,6-BISPHOSPHATASE D-Fructose 2,6-bisphosphate, 6-PHOSPHOFRUCTO-2-KINASE Fructose-1,6-bisphosphate aldolase, ALDOLASE... [Pg.744]

Phosphofructokinase-2/fructose 2,6-bisphosphatase LQRRRGSSIPQ Glycolysis/gluconeogenesis... [Pg.440]

Figure 11-2 Roles of phosphofructose kinase and fructose 1,6-bisphosphatase in the control of the breakdown and storage (—+) of glycogen in muscle. The uptake of glucose from blood and its release from tissues is also illustrated. The allosteric effector fructose 2,6-bisphosphate (Fru-2,6-P2) regulates both phosphofructokinase and fructose 2,6-bisphosphatase. These enzymes are also regulated by AMP if it accumulates. The activity of phosphofructokinase-2 (which synthesizes Fru-2,6-P2) is controlled by a cyclic AMP-dependent kinase and by dephosphorylation by a phosphatase. Figure 11-2 Roles of phosphofructose kinase and fructose 1,6-bisphosphatase in the control of the breakdown and storage (—+) of glycogen in muscle. The uptake of glucose from blood and its release from tissues is also illustrated. The allosteric effector fructose 2,6-bisphosphate (Fru-2,6-P2) regulates both phosphofructokinase and fructose 2,6-bisphosphatase. These enzymes are also regulated by AMP if it accumulates. The activity of phosphofructokinase-2 (which synthesizes Fru-2,6-P2) is controlled by a cyclic AMP-dependent kinase and by dephosphorylation by a phosphatase.
Fructose bisphosphate aldolases 699 Fructose 6-phosphate 535, 693s Fructose 6-phosphate kinase 656 Fructose-1,6-bisphosphatase 645 Fructose-2,6-bisphosphatase 646 Fruit fly. See Drosophilia melanogaster Fucose (Fuc) 165s L-Fucose isomerase 693 Fucosyltransferase 184 Fucoxanthin 22... [Pg.917]

The effects of ATP, AMP, and fructose 2,6-bisphos-phate on phosphofructokinase have been discussed in Chapter 11, Section C. Fructose 2,6-P2 is a potent allosteric activator of phosphofructokinase and a strong competitive inhibitor of fructose 1,6-bisphosphatase (Fig. 11-2). It is formed from fructose 6-P and ATP by the 90-kDa bifunctional phosphofructo-2-kinase/ fructose 2,6-bisphosphatase. Thus, the same protein forms and destroys this allosteric effector. Since the bifunctional enzyme is present in very small amounts, the rate of ATP destruction from the substrate cycling is small. [Pg.999]

Shin DJ and McGrane MM (1997) Vitamin A regulates genes involved in hepatic gluconeogenesis in mice phosphoenolpyruvate carboxykinase, fructose-l,6-bis-phosphatase and 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase./owmaZ of Nutrition 127, 1274-8. [Pg.452]

The crystal structure of the entire 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, a key bifunctional regulator of both glycolysis and gluconeogenesis, has been solved at 2.0 A resolution. The entire enzyme is a homodimer of 55kDa subunits arranged in a head-to-head fashion, with each monomer consisting of an independent kinase and phosphatase domain. The location of y-5 -ATP and inorganic phosphate in the kinase and phosphatase domains,... [Pg.2417]

Kitamura, K., Kangawa, K., Matsuo, H., Uyeda, K. (1988). Phosphorylation of myocardial fructose-6-phosphate,2-kinase fructose-2,6-bisphosphatase by cAMP-dependent protein kinase and protein kinase C. J. Biol. Chem. 263, 16796-16801. [Pg.168]

Pilkis, S. J., T. H. Claus, 1. J. Kurland, and A. J. Lange. 1995. 6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase a metabolic signaling enzyme. Arm. Rev. Biochem. 64 799-835. [Pg.349]

Phosphofructo-2-kinase-Fructose-2,6-bisphosphatase (PFK2-FBPase2)... [Pg.163]

When phosphorylated, PFK2, effectively is a fructose-2,6-bisphosphatase. Thus, it will carry out the reaction offructose-2,6-bisphosphate fructose-6-phosphate + inorganic phosphate. This will decrease the level of fructose-2,6-bisphosphate, removing the activation of PFK and the inhibition of FBPase, and al-... [Pg.384]


See other pages where Fructose-bisphosphatase is mentioned: [Pg.752]    [Pg.54]    [Pg.55]    [Pg.158]    [Pg.159]    [Pg.80]    [Pg.302]    [Pg.581]    [Pg.582]    [Pg.646]    [Pg.524]    [Pg.316]    [Pg.245]    [Pg.149]    [Pg.189]    [Pg.373]    [Pg.369]    [Pg.646]    [Pg.281]    [Pg.496]    [Pg.353]    [Pg.237]    [Pg.311]   
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See also in sourсe #XX -- [ Pg.204 ]

See also in sourсe #XX -- [ Pg.646 , Pg.1320 ]

See also in sourсe #XX -- [ Pg.646 ]

See also in sourсe #XX -- [ Pg.281 ]

See also in sourсe #XX -- [ Pg.239 ]

See also in sourсe #XX -- [ Pg.646 ]

See also in sourсe #XX -- [ Pg.646 ]

See also in sourсe #XX -- [ Pg.335 , Pg.395 ]




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Citrate fructose-1,6-bisphosphatase

Cytosolic fructose 1,6-bisphosphatase

Fructose 1,6-bisphosphatase , inhibition

Fructose 1,6-bisphosphatase gluconeogenesis

Fructose 1,6-bisphosphatase substrate cycle

Fructose 1,6-bisphosphatase, function

Fructose- 1,6-bisphosphatase regulation

Fructose-1,6-bisphosphatase control

Fructose-1,6-bisphosphatase deficiency

Fructose-1,6-bisphosphatase gene

Fructose-1,6-bisphosphatase-phosphofructokinase cycle

Fructose-l,6-bisphosphatase

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