ADP dependent cyanobacterial PFK-A

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

Contents

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.