|PROSITE documentation PDOC00638|
ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) [1,2] (EC 22.214.171.124) catalyzes a very important step in the biosynthesis of α 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. We selected three of these regions as signature patterns. The first two are N-terminal and have been proposed to be part of the allosteric and/or substrate-binding sites in the Escherichia coli enzyme (gene glgC). The third pattern corresponds to a conserved region in the central part of the enzymes.Last update:
December 2004 / Patterns and text revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Nakata P.A. Greene T.W. Anderson J.M. Smith-White B.J. Okita T.W. Preiss J.|
|Title||Comparison of the primary sequences of two potato tuber ADP-glucose pyrophosphorylase subunits.|
|Source||Plant Mol. Biol. 17:1089-1093(1991).|
|2||Authors||Preiss J. Ball K. Hutney J. Smith-White B.J. Li. L. Okitsa T.W.|
|Source||Pure Appl. Chem. 63:535-544(1991).|