Characterization of phosphofructokinase II and regulation of fructose 2,6-bisphosphate levels in Trichoderma reesei

Neto, José Abrahão

doi:10.1099/00221287-139-6-1363

Cited by 3 publications

(1 citation statement)

References 34 publications

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“…However, no evidence of the role of hexokinase or glucokinase in glucose control in Trichoderma has been established. Phosphofructokinase 2, another enzyme in the glycolytic pathway important for regulation, has been purified from T. reesei and studied (Abrahao Neto, 1993). Data suggest that the enzyme is not regulated by cyclic-AMP-dependent phosphorylation but only by substrate availability, unlike in yeasts.…”

Section: Energy Metabolismmentioning

confidence: 96%

Metabolic Diversity of Trichoderma

Silva

Steindorff

Monteiro

2014

Biotechnology and Biology of Trichoderma

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Section: Energy Metabolismmentioning

confidence: 96%

Metabolic Diversity of Trichoderma

Silva

Steindorff

Monteiro

2014

Biotechnology and Biology of Trichoderma

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Fungal metabolic diversity

Steindorff

Persinoti

Monteiro

et al. 2015

Fungal Biomolecules

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Fructose 2,6-bisphosphate biosynthesis and regulation of carbohydrate metabolism inAspergillus oryzae

Rádis‐Baptista¹,

Valdivia²,

Abrahão-Neto³

1998

Can. J. Microbiol.

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The biosynthesis and role of fructose 2,6-bisphosphate (Fru-2,6-P 2 ) in carbohydrate metabolism during induction of an amylolytic system in Aspergillus oryzae was studied. Fluctuations in Fru-2,6-P 2 were not dependent on the external glucose concentration during induction, whereas the level of Fru-2,6-P 2 increased significantly when the oxygen concentration was diminished. Phosphofructokinase II (PFK II) of A. oryzae was sensitive to phosphorylation in vitro by the catalytic subunit of cyclic AMP dependent protein kinase, which increased the V max (twofold), although the K m (0.7 mM) remained unchanged. Phosphofructokinase I was neither activated by micromolar Fru-2,6-P 2 nor inhibited by high ATP concentrations. The activity of fructose-1,6-bisphosphatase (FBPase) was subject to strong inhibition by Fru-2,6-P 2 . Addition of glucose to cultures under gluconeogenic conditions caused a decrease of approximately 40% in the FBPase activity within 4 min. These results indicate that the effect of Fru-2,6-P 2 in A. oryzae could preferentially control gluconeogenesis. The addition of 0.1 M glucose under gluconeogenic culture conditions also showed that Fru-2,6-P 2 fluctuations appeared to be, at least in short term, more closely related to temporal changes in the hexose-6-phosphate concentration.Résumé : Nous avons étudié la biosynthèse et le rôle du fructose-2,6-diphosphate (Fru-2,6-P 2 ) sur le métabolisme des hydrates de carbone lors de l'induction d'un système amylolytique chez l'Aspergillus oryzae. Les fluctuations du Fru-2,6-P 2 ne dépendaient pas de la concentration externe de glucose durant l'induction mais le niveau du Fru-2,6-P 2 augmentait significativement lorsque la concentration d'oxygène était diminuée. La phosphofructokinase II (PFK II) d'A. oryzae était sensible à la phosphorylation in vitro par la sous-unité catalytique de la protéine kinase AMP cyclique dépendante qui augmentait la V max (deux fois) même si le K m (0,7 mM) demeurait inchangé. La phosphofructokinase I n'était pas inactivée par des concentrations micromolaires de Fru-2,6-P 2 ni inhibée par des concentrations élevées d'ATP. L'activité de la fructose-l,6-diphosphatase (FBPase) pouvait être fortement inhibée par le Fru-2,6-P 2 . L'addition de glucose dans des cultures en condition de gluconéogénèse a provoqué une diminution d'environ 40% de l'activité de la FBPase en moins de 4 min. Les résultats obtenus suggèrent que chez l'A. oryzae l'effet du Fru-2,6-P 2 pourrait contrôler la gluconéogénèse de façon préférentielle. L'addition de 0.1 M de glucose dans des conditions de gluconéogénèse a aussi révélé que les fluctuations du Fru-2,6-P 2 semblaient étroitement reliées, du moins à court terme, à la variation dans le temps de la concentration de l'hexose-6-phosphate.Mots clés : Aspergillus oryzae, fructose-2,6-diphosphate, phosphofructokinase II (PFK II), AMP cyclique, contrôle de la gluconéogénèse.[Traduit par la rédaction]

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Characterization of phosphofructokinase II and regulation of fructose 2,6-bisphosphate levels in Trichoderma reesei

Abstract: These results provide evidence that the fructose 2,6-bisphosphate level in T. reesei is independent of cAMP concentrations and not related to a CAMP-dependent mechanism, but to the availability of substrate fructose 6-phosphate.

Cited by 3 publications

References 34 publications

Metabolic Diversity of Trichoderma

Metabolic Diversity of Trichoderma

Fungal metabolic diversity

Fructose 2,6-bisphosphate biosynthesis and regulation of carbohydrate metabolism inAspergillus oryzae

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