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Published on November 16, 2007; 10.1104/pp.107.109942

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Received September 27, 2007
Accepted November 7, 2007

Heat Stability and Allosteric Properties of the Maize Endosperm ADP- glucose Pyrophosphorylase are intimately intertwined

Susan K. Boehlein , Janine R. Shaw , Jon D. Stewart , and L. Curtis Hannah *

Program in Plant Molecular and Cellular Biology and Horticultural Sciences, University of Florida, Gainesville, Florida, 32611; Department of Chemistry, University of Florida, Gainesville, Florida, USA 32611-7200

* Corresponding author; email: Hannah{at}mail.ifas.ufl.edu.

ADP-glucose pyrophosphorylase (AGPase), a key regulatory enzyme in starch biosynthesis, is highly regulated. Transgenic approaches in four plant species showed that alterations in either thermal stability or allosteric modulation increase starch synthesis. Here we show that the classic regulators, 3-PGA and Pi stabilize maize endosperm AGPase to thermal inactivation. In addition we show that glycerol phosphate and ribose-5-phosphate increase the catalytic activity of maize AGPase to the same extent as the activator, 3-PGA, albeit with higher Ka values. Activation by fructose-6-phosphate and glucose-6-phosphate is comparable to that of 3-PGA. The reactants ATP and ADP-glucose, but not glucose-1-phosphate and PPi, protect AGPase from thermal inactivation, a result consistent with the ordered kinetic mechanism reported for other AGPases. 3-PGA acts synergistically with both ATP and ADP-glucose in heat protection, decreasing the substrate concentration needed for protection and increasing the extent of protection. Characterization of a series of activators and inhibitors suggests that they all bind at the same site or at mutually exclusive sites. Pi, the classic "inhibitor" of AGPase, binds to the enzyme in the absence of other metabolites, as determined by thermal protections experiments, but does not inhibit activity. Rather, Pi acts by displacing bound activators and returning the enzyme to its activity in their absence. Finally, we show from thermal inactivation studies that the enzyme exists in two forms that have significantly different stabilities and do not interconvert rapidly.






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