Fructose 2,6-bisphosphate in yeast

Lederer, B; Vissers, Stéphan; Schaftingen, Emile Van; Hers, Henri‐Géry

doi:10.1016/0006-291x(81)90261-8

Cited by 68 publications

(35 citation statements)

References 14 publications

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“…Sodium citrate, tested up to 10 mM; sodium acetate, ATP, ADP, AMP, glucose 6-phospahte and fructose 1,6-bisphosphate, tested up to 5 mM; and phosphoenol pyruvate, tested up to 1 raM, did not have any effect on the activities of the purified enzymes of S. cerevisiae and C. utilis. Fructose 2,6-bisphosphate was found to inhibit the enzymes competitively, but only at high concentrations (2-5 mM) which are not to be expected in vivo [20,21]. The affinity of the enzyme of both organisms for pyruvate was determined at three (Table V and Fig.…”

Section: Properties Of Pyruvate Decarboxylasementioning

confidence: 92%

Localization and kinetics of pyruvate-metabolizing enzymes in relation to aerobic alcoholic fermentation in Saccharomyces cerevisiae CBS 8066 and Candida utilis CBS 621

Urk

Schipper

Breedveld

et al. 1989

Biochimica et Biophysica Acta (BBA) - General Subjects

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Section: Properties Of Pyruvate Decarboxylasementioning

confidence: 92%

Localization and kinetics of pyruvate-metabolizing enzymes in relation to aerobic alcoholic fermentation in Saccharomyces cerevisiae CBS 8066 and Candida utilis CBS 621

Urk

Schipper

Breedveld

et al. 1989

Biochimica et Biophysica Acta (BBA) - General Subjects

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“…Models of porcine FBPase, as usual lacking electron density for residues at the N terminus, begin with Asn 9 and go to the C-terminal residue at position 337. Only residues [63][64][65][66][67][68][69][70] are not in strong electron density. These residues are part of the dynamic loop, which is in the disengaged conformation in both the Mg 2ϩ -and Zn 2ϩ -bound complexes of the porcine enzyme.…”

Section: Fru-26-p 2 -Bound Structures Of Porcine Fbpase (Protein Datmentioning

confidence: 99%

Structures of Mammalian and Bacterial Fructose-1,6-bisphosphatase Reveal the Basis for Synergism in AMP/Fructose 2,6-Bisphosphate Inhibition

Hines

Chen

Nix

et al. 2007

Journal of Biological Chemistry

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Fructose-1,6-bisphosphatase (FBPase) operates at a control point in mammalian gluconeogenesis, being inhibited synergistically by fructose 2,6-bisphosphate (Fru-2,6-P 2 ) and AMP. AMP and Fru-2,6-P 2 bind to allosteric and active sites, respectively, but the mechanism responsible for AMP/Fru-2,6-P 2 synergy is unclear. Demonstrated here for the first time is a global conformational change in porcine FBPase induced by Fru-2,6-P 2 in the absence of AMP. The Fru-2,6-P 2 complex exhibits a subunit pair rotation of 13°from the R-state (compared with the 15°rotation of the T-state AMP complex) with active site loops in the disengaged conformation. A three-state thermodynamic model in which Fru-2,6-P 2 drives a conformational change to a T-like intermediate state can account for AMP/Fru-2,6-P 2 synergism in mammalian FBPases. AMP and Fru-2,6-P 2 are not synergistic inhibitors of the Type I FBPase from Escherichia coli, and consistent with that model, the complex of E. coli FBPase with Fru-2,6-P 2 remains in the R-state with dynamic loops in the engaged conformation. Evidently in porcine FBPase, the actions of AMP at the allosteric site and Fru-2,6-P 2 at the active site displace engaged dynamic loops by distinct mechanisms, resulting in similar quaternary end-states. Conceivably, Type I FBPases from all eukaryotes may undergo similar global conformational changes in response to Fru-2,6-P 2 ligation.

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“…Yeast 6-phosphofructo-l-kinase (6PF-1-K) (EC 2.7.1.11) is activated and fructose-1,6-bisphosphatase (F-1,6-bPase) (EC 3.1.3.11) is inhibited in uitro by nanomolar concentrations of F2,6bP (Lederer et al, 1981;Bartrons et al, 1982;Noda et al, 1984;Fransois et al, 1987;Van Schaftingen, 1987). In yeast cells…”

Section: Introductionmentioning

confidence: 99%

Mutant studies of phosphofructo-2-kinases do not reveal an essential role of fructose-2, 6-bisphosphate in the regulation of carbon fluxes in yeast cells

1997

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The effect of the allosteric regulator fructose-2,6-bisphosphate (F2,6bP) on the regulation of carbohydrate metabolism was investigated in wivo with Sacchammyces cerevisiae mutants containing no, very high or unregulated 6-phosphofructo-2-kinase activity. Simultaneous overproduction of F2,6bP and 6-phosphofructo-1-kinase activity did not increase the glycolytic flux to ethanol. Overexpression of fructose-1,6-bisphosphatase during growth on glucose in a mutant strain devoid of F2,6bP did not cause pronounced effects on the cells. Moreover, high levels of F2,6bP during growth on ethanol in a strain with a highly active 6-phosphofructo-2-kinase enzyme did not affect either carbon flux to glycogen or growth rate. Site-directed mutagenesis of C-phosphofructo-2-kinase (Pfk26) revealed that serine 644 is involved in the activation of Pfk26 by protein kinase A phosphorylation, but that, additionally, the enzyme can be further activated by phosphorylation of another amino acid residue. The results demonstrate that F2,6bP is not needed to sustain an adequate glycolytic flux under fermentative conditions, but rather is concerned with the homeostasis of metabolite concentrations. Moreover, they fail to indicate a physiological significance for inhibition of fructose-1,6-bisphosphatase by F2.6bP.

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Fructose 2,6-bisphosphate in yeast

Cited by 68 publications

References 14 publications

Localization and kinetics of pyruvate-metabolizing enzymes in relation to aerobic alcoholic fermentation in Saccharomyces cerevisiae CBS 8066 and Candida utilis CBS 621

Localization and kinetics of pyruvate-metabolizing enzymes in relation to aerobic alcoholic fermentation in Saccharomyces cerevisiae CBS 8066 and Candida utilis CBS 621

Structures of Mammalian and Bacterial Fructose-1,6-bisphosphatase Reveal the Basis for Synergism in AMP/Fructose 2,6-Bisphosphate Inhibition

Mutant studies of phosphofructo-2-kinases do not reveal an essential role of fructose-2, 6-bisphosphate in the regulation of carbon fluxes in yeast cells

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