A new regulatory principle for in vivo biochemistry: Pleiotropic low affinity regulation by the adenine nucleotides – Illustrated for the glycolytic enzymes of <i>Saccharomyces cerevisiae</i>

Mensonides, F.I.C.; Bakker, Barbara M.; Crémazy, Frédéric; Messiha, Hanan L.; Mendes, Pedro; Boogerd, Fred C.; Westerhoff, Hans V.

doi:10.1016/j.febslet.2013.07.013

Cited by 14 publications

(14 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…If ATP demand dictates glycolytic flux to a significant extent, an energetic surplus should lead to the inhibition of glycolysis and ATP supply. This interpretation is supported by demonstrations that, in vitro, ATP inhibits most glycolytic enzymes . Of the many identified inhibition targets of ATP, PFK stands out as a key control point in this demand‐driven framework.…”

Section: Bioenergetics: How Is the Atp Generating Activity Of Glycolymentioning

confidence: 86%

“…This should serve to highlight some of the conceptual challenges inherent in thinking about glycolysis, but also underscore the usefulness of frameworks that facilitate the simplification of biological complexities to basic principles. inhibits most glycolytic enzymes [51,52]. Of the many identified inhibition targets of ATP, PFK stands out as a key control point in this demand-driven framework.…”

Section: Atp Demand Regulates the Glycolytic Fluxmentioning

confidence: 99%

See 1 more Smart Citation

Multi‐tasking of biosynthetic and energetic functions of glycolysis explained by supply and demand logic

Heerden

Bruggeman²,

Teusink³

2014

BioEssays

View full text Add to dashboard Cite

After more than a century of research on glycolysis, we have detailed descriptions of its molecular organization, but despite this wealth of knowledge, linking the enzyme properties to metabolic pathway behavior remains challenging. These challenges arise from multi-layered regulation and the context and time dependence of component functions. However, when viewed as a system that functions according to the principles of supply and demand, a simplifying theoretical framework can be applied to study its regulation logic and to assess the coherence of experimental interpretations. These principles are universally applicable, as they emphasize the common metabolic tasks of glycolysis: the provision of free-energy carriers, and precursors for biosynthesis and stress-related compounds. Here we will review the regulation of multi-tasking by glycolysis and consider how an understanding of this central metabolic pathway can be pursued using general principles, rather than focusing on the biochemical details of constituent components.

show abstract

Section: Bioenergetics: How Is the Atp Generating Activity Of Glycolymentioning

confidence: 86%

Section: Atp Demand Regulates the Glycolytic Fluxmentioning

confidence: 99%

Multi‐tasking of biosynthetic and energetic functions of glycolysis explained by supply and demand logic

Heerden

Bruggeman²,

Teusink³

2014

BioEssays

View full text Add to dashboard Cite

show abstract

“…This is known as 'aerobic fermentation' or 'Warburg effect' in cancer cells (Diaz-Ruiz et al, 2011). In addition to being an important indicator of cell energy, ATP itself is a common regulator of multiple glycolytic enzymes (Larsson et al, 2000;Mensonides et al, 2013). Therefore, to elucidate the cellular dynamics of ATP is essential also in order to decipher the regulation of glycolytic flux, but remained unaddressed for aforementioned reasons.…”

Section: Introductionmentioning

confidence: 99%

Reliable imaging of ATP in living budding and fission yeast

Takaine

Ueno

Kitamura

et al. 2019

Journal of Cell Science

View full text Add to dashboard Cite

Adenosine triphosphate (ATP) is a main metabolite essential for all living organisms. However, our understanding of ATP dynamics within a single living cell is very limited. Here, we optimized the ATP-biosensor QUEEN and monitored the dynamics of ATP with good spatial and temporal resolution in living yeasts. We found stable maintenance of ATP concentration in wild-type yeasts, regardless of carbon sources or cell cycle stages, suggesting that mechanism exists to maintain ATP at a specific concentration. We further found that ATP concentration is not necessarily an indicator of metabolic activity, as there is no clear correlation between ATP level and growth rates. During fission yeast meiosis, we found a reduction in ATP levels, suggesting that ATP homeostasis is controlled by differentiation. The use of QUEEN in yeasts offers an easy and reliable assay for ATP dynamicity and will answer several unaddressed questions about cellular metabolism in eukaryotes.

show abstract

“…0.21 mM for PGK from Pseudomonas sp . and 0.31 mM for yeast PGK [33,34]. The K M value of 0.26 mM for 3-PG of PGK His is comparable to that of PGK from Mus musculus [33] and slightly lower than that of PGK from Pseudomonas sp .…”

Section: Discussionmentioning

confidence: 99%

Characterization of 3-phosphoglycerate kinase from Corynebacterium glutamicum and its impact on amino acid production

Reddy

Wendisch

2014

BMC Microbiology

View full text Add to dashboard Cite

BackgroundCorynebacterium glutamicum cg1790/pgk encodes an enzyme active as a 3-phosphoglycerate kinase (PGK) (EC 2.7.2.3) catalyzing phosphoryl transfer from 1,3-biphosphoglycerate (bPG) to ADP to yield 3-phosphoglycerate (3-PG) and ATP in substrate chain phosphorylation.ResultsC. glutamicum 3-phosphoglycerate kinase was purified to homogeneity from the soluble fraction of recombinant E. coli. PGKHis was found to be active as a homodimer with molecular weight of 104 kDa. The enzyme preferred conditions of pH 7.0 to 7.4 and required Mg2+ for its activity. PGKHis is thermo labile and it has shown maximal activity at 50–65°C. The maximal activity of PGKHis was estimated to be 220 and 150 U mg-1 with KM values of 0.26 and 0.11 mM for 3-phosphoglycerate and ATP, respectively. A 3-phosphoglycerate kinase negative C. glutamicum strain ∆pgk was constructed and shown to lack the ability to grow under glycolytic or gluconeogenic conditions unless PGK was expressed from a plasmid to restore growth. When pgk was overexpressed in L-arginine and L-ornithine production strains the production increased by 8% and by 17.5%, respectively.ConclusionUnlike many bacterial PGKs, C. glutamicum PGK is active as a homodimer. PGK is essential for growth of C. glutamicum with carbon sources requiring glycolysis and gluconeogenesis. Competitive inhibition by ADP reveals the critical role of PGK in gluconeogenesis by energy charge. Pgk overexpression improved the productivity in L-arginine and L-ornithine production strains.

show abstract

A new regulatory principle for in vivo biochemistry: Pleiotropic low affinity regulation by the adenine nucleotides – Illustrated for the glycolytic enzymes of Saccharomyces cerevisiae

Cited by 14 publications

References 28 publications

Multi‐tasking of biosynthetic and energetic functions of glycolysis explained by supply and demand logic

Multi‐tasking of biosynthetic and energetic functions of glycolysis explained by supply and demand logic

Reliable imaging of ATP in living budding and fission yeast

Characterization of 3-phosphoglycerate kinase from Corynebacterium glutamicum and its impact on amino acid production

Contact Info

Product

Resources

About