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1 ted levels of the PFK-1 allosteric activator fructose 2,6-bisphosphate.
2 evented binding and allosteric activation by fructose 2,6-bisphosphate.
3 ence and presence of the allosteric effector fructose 2,6-bisphosphate.
4 ut is with both ATP and fructose-6-P or with fructose-2,6-bisphosphate.
5 bited the IGF-1-induced increase in cellular fructose-2,6-bisphosphate.
6 atase, catalyzes synthesis and hydrolysis of fructose 2, 6-bisphosphate.
7 tase, catalyzes synthesis and degradation of fructose 2, 6-bisphosphate.
8 ng reaction with the physiological substrate fructose-2, 6-bisphosphate.
9 rom; K(a) for Mg(2+), 0.34-0.76 mm; K(i) for fructose-2,6-bisphosphate, 0.11-0.61 microm; and IC(50)
11 FKFB3), the pro-glycolytic enzyme that forms fructose-2,6-bisphosphate, a powerful allosteric activat
13 ts glycolysis by reducing cellular levels of fructose-2,6-bisphosphate, an activator of glycolysis an
17 dent and was enhanced by forced elevation of fructose 2,6-bisphosphate and by additional xylitol-deri
18 te, and that inhibition could be reversed by fructose 2,6-bisphosphate and cyclic AMP, a high-affinit
19 filled by the O2 phosphate of the substrate, fructose-2,6-bisphosphate, and subsequently, the phospho
21 inant human and zebra fish enzymes hydrolyze fructose-2,6-bisphosphate as well as fructose-1,6-bispho
27 apo and holo tetramers show that binding of fructose 2,6-bisphosphate cools the enzyme and reduces d
28 te and the Ki for the competitive inhibitor, fructose 2,6-bisphosphate, decreased by as much as 4- an
29 c flux is the relatively recently discovered fructose-2,6-bisphosphate (F-2,6-P2), an allosteric acti
30 iated L6 rat myotubes increased synthesis of fructose 2,6-bisphosphate (F2,6BP), a positive allosteri
32 y, the levels of both PFKFB3 and its product fructose-2,6 bisphosphate (F2,6BP), an allosteric modula
34 ) control glycolytic flux via their product, fructose-2,6-bisphosphate (F26BP), which activates 6-pho
35 l-product complexes of the Trp57 mutant with fructose 2,6-bisphosphate (F26P(2)) causes similar decre
37 rating amounts of the heterotropic activator fructose 2, 6-bisphosphate (F26P2) gives no change in th
41 Here we examine the physiological role of fructose 2,6-bisphosphate (Fru-2,6-P2 ) during photosynt
42 this study, we investigated (a) the roles of fructose 2,6-bisphosphate (Fru-2,6-P2) and ribose 1,5-bi
43 he generally accepted metabolic concept that fructose 2,6-bisphosphate (Fru-2,6-P2) inhibits gluconeo
49 rease in its catalytic ability to synthesize fructose-2,6-bisphosphate (Fru-2,6-P(2)), the key glycol
50 f beta-D-fructose- 6-phosphate (Fru-6-P) and fructose-2,6-bisphosphate (Fru-2,6-P2) at distinct activ
52 roperties support the view that the level of fructose 2,6-bisphosphate in leaves is determined by the
54 e 6-phosphofructo-2-kinase and production of fructose 2,6-bisphosphate, in the hearts of mPDK1(-/-) m
57 s a possible evolutionary predecessor to AMP/fructose 2,6-bisphosphate inhibition in mammalian FBPase
59 A in the liver and demonstrate that elevated fructose 2,6-bisphosphate is essential for recruitment o
60 increased levels of the allosteric regulator fructose-2,6-bisphosphate, leading to increased glycolyt
61 se in hepatic fat oxidation, increased liver fructose 2,6-bisphosphate level, and reductions in lacta
65 Seven days after virus injection, hepatic fructose-2,6-bisphosphate levels increased significantly
66 rmal lung fibroblasts showed that iPFK-2 and fructose-2,6-bisphosphate levels increased specifically
67 ucokinase mRNA and protein levels as well as fructose-2,6-bisphosphate levels were increased in aLivG
68 ficient of 2), synergistic with both AMP and fructose 2,6-bisphosphate, noncompetitive with respect t
69 y identified mechanism whereby the levels of fructose 2,6-bisphosphate promote mitochondrial PDK4 lev
71 lycolysis in adipocytes via the synthesis of fructose-2,6-bisphosphate that was significantly downreg
72 -2), regulator of the glycolysis-stimulating fructose-2,6-bisphosphate, was among human HeLa cell pro
73 Km for fructose 1,6-bisphosphate, and Ki for fructose 2,6-bisphosphate were comparable for the mutant
74 lites, such as fructose 1,6-bisphosphate and fructose 2,6-bisphosphate, which are known allosteric ac
76 element in its mRNA and functions to produce fructose-2,6-bisphosphate, which is a powerful allosteri
77 iation constants of fructose-6-phosphate and fructose-2,6-bisphosphate, which were 29 +/- 3 and 2.1 +
78 t was counteracted by selective depletion of fructose 2,6-bisphosphate with a bisphosphatase-active k