Abstract
ADP-glucose pyrophosphorylase (AGPase) catalyzes the first committed step of starch synthesis in plants. The potato tuber enzyme contains a pair of catalytic small subunits (SSs) and a pair of non-catalytic large subunits (LSs). We have previously identified a LS mutant containing a P52L replacement, which rendered the enzyme with down-regulatory properties. To investigate the structure–function relationships between the two subunits with regard to allosteric regulation, putative SS mutants that could reverse the down-regulatory condition of LS P52L were identified by their ability to restore glycogen accumulation in an AGPase-deficient Escherichia coli glgC-strain. Two distinct LS-dependent classes, bona fide SS suppressors dependent on LS P52L but not LS WT and SS up-regulating allosteric mutants, were evident by kinetic analysis. These results indicate that both LS and SS have a regulatory function in controlling allosteric properties through enhancing cooperative subunit interactions.
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