AUTHOR=Figueroa Carlos M. , Kuhn Misty L. , Hill Benjamin L. , Iglesias Alberto A. , Ballicora Miguel A. TITLE=Resurrecting the Regulatory Properties of the Ostreococcus tauri ADP-Glucose Pyrophosphorylase Large Subunit JOURNAL=Frontiers in Plant Science VOLUME=9 YEAR=2018 URL=https://www.frontiersin.org/journals/plant-science/articles/10.3389/fpls.2018.01564 DOI=10.3389/fpls.2018.01564 ISSN=1664-462X ABSTRACT=
ADP-glucose pyrophosphorylase (ADP-Glc PPase) catalyzes the first committed step for the synthesis of glycogen in cyanobacteria and starch in green algae and plants. The enzyme from cyanobacteria is homotetrameric (α4), while that from green algae and plants is heterotetrameric (α2β2). These ADP-Glc PPases are allosterically regulated by 3-phosphoglycerate (3PGA, activator) and inorganic orthophosphate (Pi, inhibitor). Previous studies on the cyanobacterial and plant enzymes showed that 3PGA binds to two highly conserved Lys residues located in the C-terminal domain. We observed that both Lys residues are present in the small (α) subunit of the