ライフサイエンスコーパス: fructose-2,6-bisphosphate

1 ence and presence of the allosteric effector fructose 2,6-bisphosphate.

2 evented binding and allosteric activation by fructose 2,6-bisphosphate.

3 ut is with both ATP and fructose-6-P or with fructose-2,6-bisphosphate.

4 bited the IGF-1-induced increase in cellular fructose-2,6-bisphosphate.

5 atase, catalyzes synthesis and hydrolysis of fructose 2, 6-bisphosphate.

6 tase, catalyzes synthesis and degradation of fructose 2, 6-bisphosphate.

7 ng reaction with the physiological substrate fructose-2, 6-bisphosphate.

8 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)

9 Raising the cellular concentration of fructose-2,6-bisphosphate, a potent effector of the dire

10 Binding of fructose-2,6-bisphosphate also significantly increased t

11 ts glycolysis by reducing cellular levels of fructose-2,6-bisphosphate, an activator of glycolysis an

12 By controlling the level of fructose-2,6-bisphosphate, an allosteric activator of th

13 4 6-fold decreases in Ki values for fructose 2,6-bisphosphate and 5-9-fold decreases in the

14 The two sites for activators, fructose 2,6-bisphosphate and AMP or ADP, have evolved f

15 dent and was enhanced by forced elevation of fructose 2,6-bisphosphate and by additional xylitol-deri

16 te, and that inhibition could be reversed by fructose 2,6-bisphosphate and cyclic AMP, a high-affinit

17 filled by the O2 phosphate of the substrate, fructose-2,6-bisphosphate, and subsequently, the phospho

18 e absent in FBPases of organisms that employ fructose 2,6-bisphosphate as a regulator.

19 inant human and zebra fish enzymes hydrolyze fructose-2,6-bisphosphate as well as fructose-1,6-bispho

20 [2-32P]Fructose 2,6-bisphosphate binding experiments also sugge

21 Increasing the fructose-2,6-bisphosphate concentration over a 15-fold r

22 ux, consistent with the observed decrease in fructose-2,6-bisphosphate concentration.

23 Also, the effects of fructose-2, 6-bisphosphate concentrations on fructose-1,

24 d) a normal ATP/ADP ratio, and (e) unchanged fructose 2,6 bisphosphate content.

25 apo and holo tetramers show that binding of fructose 2,6-bisphosphate cools the enzyme and reduces d

26 te and the Ki for the competitive inhibitor, fructose 2,6-bisphosphate, decreased by as much as 4- an

27 c flux is the relatively recently discovered fructose-2,6-bisphosphate (F-2,6-P2), an allosteric acti

28 iated L6 rat myotubes increased synthesis of fructose 2,6-bisphosphate (F2,6BP), a positive allosteri

29 FKFB3 and increased synthesis of its product fructose 2,6-bisphosphate (F2,6P2).

30 tion of the allosteric glycolytic activator, fructose-2,6-bisphosphate (F2,6BP).

31 ) control glycolytic flux via their product, fructose-2,6-bisphosphate (F26BP), which activates 6-pho

32 l-product complexes of the Trp57 mutant with fructose 2,6-bisphosphate (F26P(2)) causes similar decre

33 The addition of fructose 2,6-bisphosphate (F26P(2)) has no effect on the

34 rating amounts of the heterotropic activator fructose 2, 6-bisphosphate (F26P2) gives no change in th

35 Fructose 2,6-bisphosphate (Fru-2,6-BP) is an allosteric

36 ogenesis, being inhibited synergistically by fructose 2,6-bisphosphate (Fru-2,6-P(2)) and AMP.

37 PFK-2 controls the level of fructose 2,6-bisphosphate (Fru-2,6-P(2)), an important r

38 Here we examine the physiological role of fructose 2,6-bisphosphate (Fru-2,6-P2 ) during photosynt

39 this study, we investigated (a) the roles of fructose 2,6-bisphosphate (Fru-2,6-P2) and ribose 1,5-bi

40 he generally accepted metabolic concept that fructose 2,6-bisphosphate (Fru-2,6-P2) inhibits gluconeo

41 Fructose 2,6-bisphosphate (fru-2,6-P2) is a signalling m

42 The effects of AMP and fructose 2,6-bisphosphate (Fru-2,6-P2) on porcine fructo

43 Fructose 2,6-bisphosphate (Fru-2,6-P2) plays an importan

44 ase), catalyzes synthesis and degradation of fructose 2,6-bisphosphate (Fru-2,6-P2).

45 beta-D-Fructose-2,6-bisphosphate (Fru-2,6-P(2)) is an important

46 rease in its catalytic ability to synthesize fructose-2,6-bisphosphate (Fru-2,6-P(2)), the key glycol

47 f beta-D-fructose- 6-phosphate (Fru-6-P) and fructose-2,6-bisphosphate (Fru-2,6-P2) at distinct activ

48 is, we analyzed the effect of amino acids on fructose-2,6-bisphosphate (Fru-2,6-P2) metabolism.

49 roperties support the view that the level of fructose 2,6-bisphosphate in leaves is determined by the

50 The steady state concentration of fructose 2,6-bisphosphate in turn depends on the activit

51 e 6-phosphofructo-2-kinase and production of fructose 2,6-bisphosphate, in the hearts of mPDK1(-/-) m

52 The Ki for the competitive inhibitor fructose 2,6-bisphosphate increased 3- and 5-fold in Arg

53 The K(i) for fructose 2,6-bisphosphate increases approximately 20- an

54 s a possible evolutionary predecessor to AMP/fructose 2,6-bisphosphate inhibition in mammalian FBPase

55 Fructose 2,6-bisphosphate is a powerful allosteric regul

56 A in the liver and demonstrate that elevated fructose 2,6-bisphosphate is essential for recruitment o

57 increased levels of the allosteric regulator fructose-2,6-bisphosphate, leading to increased glycolyt

58 se in hepatic fat oxidation, increased liver fructose 2,6-bisphosphate level, and reductions in lacta

59 crease in mRNA level over a 15-fold range in fructose-2,6-bisphosphate level.

60 e mRNA were unchanged by the manipulation of fructose-2,6-bisphosphate level.

61 TIGAR expression lowered fructose-2,6-bisphosphate levels in cells, resulting in

62 Seven days after virus injection, hepatic fructose-2,6-bisphosphate levels increased significantly

63 rmal lung fibroblasts showed that iPFK-2 and fructose-2,6-bisphosphate levels increased specifically

64 ucokinase mRNA and protein levels as well as fructose-2,6-bisphosphate levels were increased in aLivG

65 ficient of 2), synergistic with both AMP and fructose 2,6-bisphosphate, noncompetitive with respect t

66 ve identified the origins of the citrate and fructose 2,6-bisphosphate sites.

67 -2), regulator of the glycolysis-stimulating fructose-2,6-bisphosphate, was among human HeLa cell pro

68 Km for fructose 1,6-bisphosphate, and Ki for fructose 2,6-bisphosphate were comparable for the mutant

69 lites, such as fructose 1,6-bisphosphate and fructose 2,6-bisphosphate, which are known allosteric ac

70 element in its mRNA and functions to produce fructose-2,6-bisphosphate, which is a powerful allosteri

71 iation constants of fructose-6-phosphate and fructose-2,6-bisphosphate, which were 29 +/- 3 and 2.1 +

72 t was counteracted by selective depletion of fructose 2,6-bisphosphate with a bisphosphatase-active k