Open Access Research article

Similar temperature dependencies of glycolytic enzymes: an evolutionary adaptation to temperature dynamics?

Ana Luisa B Cruz12, Marit Hebly12, Giang-Huong Duong12, Sebastian A Wahl12, Jack T Pronk12, Joseph J Heijnen12, Pascale Daran-Lapujade12 and Walter M van Gulik12*

Author Affiliations

1 Department of Biotechnology, Delft University of Technology and Kluyver Centre for Genomics of Industrial Fermentation, Julianalaan 67, Delft, 2628 BC, The Netherlands

2 Netherlands Consortium for Systems Biology, PO Box 94215, Amsterdam, 1090 GE, The Netherlands

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BMC Systems Biology 2012, 6:151  doi:10.1186/1752-0509-6-151

Published: 7 December 2012

Additional files

Additional file 1:

Figure S1. A. Intracellular concentrations derived from model simulations considering that kcat of phosphofructokinase (PFK) is 2 times less sensitive to temperature than the other glycolytic enzymes. The symbols refer to simulations of: sinoidal temperature cycles (▵) and linear temperature shifts from 30°C steady-state chemostats (○); batch fermentations at different temperatures (□). The colors indicate the culture temperature at the time of sampling. All concentrations are normalized to the levels under glucose excess conditions at 30°C. B. Intracellular concentrations derived from model simulations considering that kcat of pyruvate kinase (PYK) is 2 times less sensitive to temperature than the other glycolytic enzymes. The symbols refer to simulations of: sinoidal temperature cycles (▵) and linear temperature shifts from 30°C steady-state chemostats (○); batch fermentations at different temperatures (□). The colors indicate the culture temperature at the time of sampling. All concentrations are normalized to the levels under glucose excess conditions at 30°C.

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Additional file 2:

Figure S2. Enzymatic capacities (Vmax) of the glycolytic enzymes that are not shown in figure 3, estimated from in vitro enzyme activity assays measured at 30°C in cell free extracts of S.cerevisiae cultivated in glucose-limited anaerobic chemostats subjected to circadian temperature cycles (CTC). A. Hexokinase (HXK); B. Fructose bi-phosphate aldolase (FBA); C. Triose phosphate isomerase (TPI); D. Phosphoglycerate kinase (PGK); E. Phosphoglycerate mutase (PGM); F. Enolase (ENO).

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Additional file 3:

Figure S3. Nucleotide levels profiles as a function of the extracellular glucose from experiments with sinoidal temperature cycles (▵), linear temperature shifts from 30°C (○) or 12°C (X) and from batches at different temperatures (□). The error bars refer to the standard error of two duplicate samples from at least two independent runs of experiments. The different colors indicate the temperature of the sample.

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Additional file 4:

Example of minimal flux changes upon temperature perturbations.

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