10.3389/fpls.2018.01849.s002 Susan K. Boehlein Susan K. Boehlein Janine R. Shaw Janine R. Shaw L. Curtis Hannah L. Curtis Hannah Table_1_Enhancement of Heat Stability and Kinetic Parameters of the Maize Endosperm ADP-Glucose Pyrophosphorylase by Mutagenesis of Amino Acids in the Small Subunit With High B Factors.DOCX Frontiers 2018 AGPase (ADP-glucose pyrophosphorylase) yield loss at harvest heat lability climate change B-factors protein evolution 2018-12-13 07:35:07 Dataset https://frontiersin.figshare.com/articles/dataset/Table_1_Enhancement_of_Heat_Stability_and_Kinetic_Parameters_of_the_Maize_Endosperm_ADP-Glucose_Pyrophosphorylase_by_Mutagenesis_of_Amino_Acids_in_the_Small_Subunit_With_High_B_Factors_DOCX/7460657 <p>ADP-glucose pyrophosphorylase (AGPase) is an important enzyme in starch synthesis and previous studies showed that the heat lability of this enzyme is a determinant to starch synthesis in the maize endosperm and, in turn, seed yield. Here, amino acids in the AGPase endosperm small subunit with high B-factors were mutagenized and individual changes enhancing heat stability and/or kinetic parameters in an Escherichia coli expression system were chosen. Individual mutations were combined and analyzed. One triple mutant, here termed Bt2-BF, was chosen for further study. Combinations of this heat stable, 3-PGA-independent small subunit variant with large subunits also heat stable yielded complex patterns of heat stability and kinetic and allosteric properties. Interestingly, two of the three changes reside in a protein motif found only in AGPases that exhibit high sensitivity to 3-PGA. While not the 3-PGA binding site, amino acid substitutions in this region significantly alter 3-PGA activation kinetics.</p>