ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) [1] (2.7.7.27) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP.

ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. It is a homotetramer in bacteria while in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits.

There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits.

1. Comparison of the primary sequences of two potato tuber ADP-glucose pyrophosphorylase subunits. Plant Mol. Biol. 17, 1089-93

ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) [
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