PROSITE documentation PDOC00638ADP-glucose pyrophosphorylase signatures
ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) [1,2] (EC 2.7.7.27) 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.
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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). | |
| PubMed ID | 1657244 |
| 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). |
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