Cyanobacterial PFKs were thought to be ATP dependent, but isolation and characterisation of 2 PFK isoenzymes from Synechocystis revealed that they belong to the PFK-A family, use ADP as phosphate donor and form a separate phylogenetic class. Their allosteric regulation via 3-PG and ATP respectively allow for flexible switching between aactive and inactive enzymes dependent on the light and carbon status.
DOI: 10.15490/fairdomhub.1.investigation.660.1
Zenodo URL: None
Created at: 26th Oct 2024 at 12:52
PFK-1 and PFK-2 kinetics
PFK-1 and PFK-2 were cloned and expressed in E. coli, purified, and kinetically characterised in terms of substrates and allosteric regulators.
Experimental data for enzyme kinetic characterisation of PFK-1 and PFK-2
The purified enzymes were kinetically charactyerised in terms of substrate sensitivity and alloestric regulation.
Kinetic data for PFK-1 and PFK-2
Experimental data for kinetic characterisaton of PFK-1 and PFK-2.
- PFK1-PFK2-FAIRDOMHub.xlsx
Model simulation of PFK-1 and PFK-2 enzyme kinetics
The experimental data for PFK-1 and PFK-2 were analysed and fitted with a MWC equation. The model is described in Mathematica and the plots in the manuscript are generatedin the notebook.
Kinetic data for PFK-1 and PFK-2
Experimental data for kinetic characterisaton of PFK-1 and PFK-2.
- PFK1-PFK2-FAIRDOMHub.xlsx
Mathematica notebook for enzyme kinetic data analysis PFK-1 and PFK-2.
Mathematic notebook for enzyme kinetic analysis and model fit, including figure generation for manuscript.
- pfk-1-2-Model.nb
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Created: 26th Oct 2024 at 12:52
Last updated: 26th Oct 2024 at 12:52