Investigation: Central Carbon Metabolism of Sulfolobus solfataricus
Study: Model gluconeogenesis
Assay type: Experimental Assay Type
Technology type: Initial Rate Experiment
Created: 29th Jan 2013 at 20:45
Last updated: 26th Oct 2017 at 09:57
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SysMO is a European transnational funding and research initiative on "Systems Biology of Microorganisms".
The goal pursued by SysMO is to record and describe the dynamic molecular processes going on in unicellular microorganisms in a comprehensive way and to present these processes in the form of computerized mathematical models.
Systems biology will raise biomedical and biotechnological research to a new quality level and contribute markedly to progress in understanding. Pooling European research ...
Web page: http://sysmo.net/
An investigation in the CCM of S. solfataricus with a focus on the unique temperature adaptations and regulation; using a combined modelling and experimental approach.
Submitter: Jacky Snoep
Assays: Experimental assays of the temperature dependent degradation of GAP and ..., FBPA/ase, FBPAase model, GAPDH, GAPDH modeling, Gluconeogenic model, Model reconstituted system, Modelling pathway optimisation, Modelling temperature dependent degradation of GAP and DHAP, PGK, PGK and FBPAase titrations, PGK modeling, Reconstituted system reference state, TPI, TPI modeling
Snapshots: Snapshot 1
Mathematical model of a subset of reactions comprising the three most temperature sensitive intermediates of the gluconeogenic pathway in S. solfataricus
Submitter: Jacky Snoep
Investigation: Central Carbon Metabolism of Sulfolobus solfata...
Assays: Experimental assays of the temperature dependent degradation of GAP and ..., FBPA/ase, FBPAase model, GAPDH, GAPDH modeling, Gluconeogenic model, Modelling temperature dependent degradation of GAP and DHAP, PGK, PGK modeling, TPI, TPI modeling
Snapshots: No snapshots
Model simulation and exp data for TIM kinetics, GAP and DHAP saturation, and PEP inhibition.
Preparation of cell free extracts of the recombinant E. coli strains expressing the respective S. solfataricus enzymes.
The recombinant enzymes were purified from the cell free extracts of E. coli expressing the respective enzymes.
Authors: T. Kouril, D. Esser, J. Kort, H. V. Westerhoff, B. Siebers, J. L. Snoep
Date Published: 22nd Aug 2013
Publication Type: Not specified
PubMed ID: 23865479
Citation: FEBS J. 2013 Sep;280(18):4666-80. doi: 10.1111/febs.12438. Epub 2013 Aug 22.